Search

Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Acta Edulis Fungi is the property of Acta Edulis Fungi and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The purpose of this experiment was to explore the structural characteristics, expression and enzymatic activity changes during germination of wheat α-amylase and β-amylase. The structural characteristics of α-amylase and β-amylase in wheat were predicted by bioinformatics, fluorescence quantitative PCR was used to detect the expression level of α-amylase and β-amylase gene in wheat seeds during the germination process, and their enzymatic activity was measured. The results showed that wheat α-amylase was an alkaline protein, β-amylase was an acidic protein, α-amylase had a signal peptide and a transmembrane region, while β-amylase did not, and the secondary and tertiary structures and number of phosphorylation sites of both amylases were similar. When wheat sprouted, the expression level of α-amylase gene first increased and then decreased, while the expression level of β-amylase gene was at a low level, the expression of α-amylase gene was induced by low concentration of salt alkali and inhibited by high concentration of salt alkali, the expression level of β-amylase gene increased with increasing salt alkali concentration, the activity of α-amylase and β-amylase significantly increased in the late stage and early stage of germination, respectively. The results indicated that wheat α-amylase was a secreted membrane protein, β-amylase was a stroma free protein, the stress responses of α-amylase and β-amylase to salt alkali were different, and they played a major role in the late and early stages of wheat germination respectively. [ABSTRACT FROM AUTHOR]

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

【Objective】The olecranon peach is known as one of the characteristic fruits in Lingnan region because of its good flavor and quality, and it is listed as “The top ten best fruits in Lingnan”. However, less studies on its allergens have been reported. By analyzing the epitope of allergen protein, it would provide a research basis for the preparation of the recombinant antigen of the allergen, and also provide a research basis for explaining the characteristic changes and sensitization characteristics of the allergen in the process of food processing.【Method】Phosphate buffer saline was used to extract the crude protein from the lyophilized powder of olecranon peach, and the allergens in the crude protein were identified by SDSPAGE protein electrophoresis and analyzed by mass spectrometry. The allergens were screened and compared by the protein database of UniProt, and the physicochemical properties, spatial structure and antigenic epitopes of the allergens were analyzed by bioinformatics methods.【Result】Seven kinds of allergenic proteins including A0A251RBV3, P86888, M5X697, M5WV03, M5WTQ8, Q2I6V8, and Q9LED1 were identified from olecranon peach, which belonged to the four classes of allergenic proteins, namely, pathogenesis-related proteins (Pru p 1), thaumatin-like proteins (Pru p 2), non-specific lipid transfer proteins (Pru p 3) and gibberellin-regulated proteins (Pru p 7). The seven kinds of allergenic proteins in olecranon peach had high stability, their molecular weight is 6.91-26.04 kD, with the aliphatic index between 29.37 and 81.54. M5WTQ8 and Q2I6V8 allergen proteins were acidic proteins, while the remaining allergen proteins were alkaline proteins. Except for Q9LED1 protein, all other allergen proteins were hydrophilic proteins. The regions with antigenic epitopes, hydrophilicity and flexibility greater than 0 and surface accessibility greater than 1 were screened, and regions with low protein bonding energy were analyzed by binding the secondary and tertiary structures of proteins to obtain the antigenic epitopes of allergens, including Pru p1 (EIP, GSQ, KEN, NL, KG, EIK, HPD), Pru p 2 (TGDQKPQ, SP, NQ, PPNDKPETCPPT, DDKSS, RP), Pru p 3 (RT, VN) and Pru p 7 (AGY, GTYGN, LKNSKGN).【Conclusion】By analyzing the structure, hydrophilicity, surface accessibility, flexibility and antigen index of olecranon peach, multiple epitopes of 7 allergens are obtained, which can provide a research basis for the sensitization characteristics of olecranon peach allergens in food processing. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Jilin University (Science Edition) / Jilin Daxue Xuebao (Lixue Ban) is the property of Zhongguo Xue shu qi Kan (Guang Pan Ban) Dian zi Za zhi She and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Science & Technology of Food Industry is the property of Science & Technology of Food Industry Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Acta Agriculturae Zhejiangensis is the property of Acta Agriculturae Zhejiangensis Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Superoxide dismutase (SOD) is a key enzyme in the antioxidant system of plants and plays a critical role in protecting plants from various biological and abiotic stresses. In this paper, using bioinformatics methods, 12 SOD genes were identified in quinoa by sequence alignment based on Arabidopsis SOD, which localized in the nucleus, microsomes and mitochondria, and distributed heterogeneously on 11 different chromosomes, and the tertiary structure of their encoded proteins showed that Cu/Zn-SODs were homodimers with Fe-SODs and Mn-SODs were homotetramers.The intron/exon distribution patterns of the CqSOD genes were different, with the number of introns ranging from 4 to 7, and the conserved motifs differing significantly. The phylogenetic relationships showed that the SOD proteins could be divided into 3 subfamilies: Cu/Zn-SODs, Fe-SODs and Mn-SODs. In addition, all CqFe- SODs and CqMn-SODs promoter regions contained abscisic acid(ABA)-responsive cis-elements, and CqSOD12 interacted with 11 CqSOD proteins and 4 CqCAT proteins. Expression profiling showed that the 12 CqSOD genes were strongly responsive to both mixed saline-alkali and nitroprusside. Above results laid the foundation for research on the role and molecular mechanism of SOD genes in plant development and stress response. [ABSTRACT FROM AUTHOR]

[Objective] Cassia obtusifolia Kunitz trypsin inhibitor 1 (CoTi1) is a group of functional peptides with 13-trefoil tertiary structure. To explore the effect of site-directed mutagenesis on the inhibitory activity of CoTi1 is of great significance for the study of its structure. [Method] Based on the structural analysis of CoTi1, three residues, Cys44 (between β2 and β3 folds of the top lid) and Tyr 134 and Lys135 (within β9 folds of the bottom β-barrel), were mutated to Ala, respectively. The inhibitory activity of these mutagenesis on bovine trypsin and cabbage worm trypsin-like protease were detected after protein expression. [Result] Compared with wild-type CoTi1, the inhibitory activity of CoTi1C44D on bovine trypsin increased by 41. 00%, while that of CoTi1Y134D and CoTi1Kl35D decreased by 45. 66% and 36. 73%, respectively. The inhibitory activities of CoTi1C44D, CoTi1Y134D and CoTi1Kl3SD on cabbage worm trypsin-like protease decreased by 46. 94%, 49. 00% and 38. 11 %, respectively. [Conclusion] Cys44, Tyrl34 and Lys135 were involved in the formation of l3-trefoil tertiary structure and were important residues for stabilizing the spatial structure and inhibiting the activity of CoTi1, which laid an important theoretical foundation for the structure study of CoTi1. [ABSTRACT FROM AUTHOR]

Pork myofibrillar protein (MP) was selected as the main research material. The Fenton oxidation system was employed to replicate the oxidation conditions of meat items, and curcumin with different concentrations (0, 5, 10, 15, 20 µmol/L) was added to it. Changes in amino acid side chain, secondary structure, tertiary structure and solubility of protein were analyzed. To explore the inhibitory effect of curcumin on the oxidation of pork myofibrillar protein at different concentrations and its specific effect on protein structure. The results showed that curcumin had good free radical scavenging performance and could effectively slow the protein oxidation and structural changes caused by hydroxyl radicals, and this inhibition was proportional to the concentration of curcumin in a specific concentration range (5-20 µmol/ L). Compared with the oxidation group, the curcumin treatment group significantly inhibited the formation of carbonyl groups and the increase of surface hydrophobicity, the curcumin treatment group of 20 µmol/L had the inhibition rates of 2.62% and 51.78%, respectively (P<0.05), can also significantly alleviate the decline of sulfhydryl, free amino and solubility (P<0.05), the inhibition rates were 80.02%, 59.34%, 70.84%, respectively, and the addition of curcumin can promote the MP tertiary structure unfolding, can also alleviate the secondary structure changes caused by hydroxyl radi¬cals. Therefore, curcumin can interact with MP to alleviate its oxidative deterioration and structural changes, and has a good effect on the quality and preservation of meat products. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Journal of Henan Agricultural Sciences is the property of Editorial Board of Journal of Henan Agricultural Sciences and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Phenylalanine ammonia-lyase (PAL) is a key enzyme in the metabolism of phenylpropane that regulates the biosynthesis of flavonoids in raspberry. To elucidate the function and regulation mechanism of the RiPAL1 gene in raspberry, total RNA was extracted from raspberry fruits to synthesize first-strand cDNA. The gene was successfully cloned, and related bioinformatics analyses were carried out. Our results showed that the coding sequence (CDS) of the RiPAL1 gene was 2 133 bp in length, encoding 710 amino acids, with a molecular weight of 77.5 ku and an isoelectric point of 6.21. The maximum hydrophobicity of RiPAL1 protein was 4.50, its minimum hydrophobicity was -4.50, and its average hydrophobicity index was -0.49. Based on these, it was determined that it is a hydrophilic protein with no transmembrane structure and no signal peptide. The RiPAL1 protein contained 4 N-glycosylation sites and 67 specific kinase sites. Its secondary structure was mainly composed of α-helices, while its tertiary structure was a homotetramer. Multiple sequence alignment showed that the RiPAL1 protein has a typical conserved domain of phenylalanine ammonia-lyase. Phylogenetic analysis indicated that the RiPAL1 protein is closely related to that of strawberry. This study provides a reference for further research on the molecular mechanism of the RiPAL1 gene in the biosynthesis of flavonoids in raspberry fruit. [ABSTRACT FROM AUTHOR]

To further explore the structure and function of the promoter and protein of human SIRT1 gene, our research used bioinformatic methods to analyze 5′-end promoter, promoter Motif, transcription factor binding sites, CpG island, single-nucleotide polymorphism, phylogenetic homology, physicochemical properties, hydrophilicity/hydrophobicity, secondary/tertiary structure, conserved domain, mutation site, N-glycosylation and phosphorylation sites, interacted proteins and biological function. The number of promoters predicted by TSSW and Neural Network Promoter Prediction database was 3 and 2 respectively. There were 3 Motifs found in the promoter region by using MEME database. The CpG islands were clustered in the 1 600～2 200 bp, which were found by using EMBOSS, MethPrimer and CpG Finder database. PROMO and AliBaba2.1 database showed that there were 22 transcription factors in their promoter regions. And there were 6 transcription factors found that bind to the positive and negative chains by using JASPAR software. Besides, there were differences found in allele frequencies between different ethnic groups by using SNP Function Prediction database. Human SIRT1 gene is located at chromosome 10q21.3 and widely distributed in different tissues, which is a hydrophilic and unstable protein with a high conservation among different species. The domain is located at the 254～489 amino acid sequence, belonging to the SIR2 superfamily, mainly located in the nucleus and mitochondria. The secondary structure of the protein mainly contains α-helices and irregular coiling. Compared with AlphaFold2, the tertiary structure model constructed by SWISS-MODEL database was reliable. SIRT1 contained 106 mutation sites, 1 N-glycosylation and 61 phosphorylation sites, which interacted with EP300, TP53 and other proteins. It also participated in circadian rhythm process, steroid hormone response, and intracellular receptor signaling etc., which were associated with longevity regulation pathway, AMPK signaling pathway, and FoxO signaling pathway etc. This study can provide a theoretical basis for further studying the effects on inflammatory reaction and other diseases of human SIRT1 gene. [ABSTRACT FROM AUTHOR]

WRKY is a plant-specific transcriptional regulator with zinc-finger domain, which is involved in regulating plant stress resistance, growth and development, and metabolism. To explore the biological function of the WRKY transcription factor ZjWRKY22 in the easily cracked jujube variety Huping, and provide a theoretical basis for revealing the molecular mechanism of jujube WRKY in response to abiotic stress, in this study, the coding region of the ZjWRKY22 gene sequence was cloned for bioinformatics prediction, and the differential expression analysis of the bearing branches, stem, leaf, flower, and fruit of the jujube were carried out. The results showed that the length of CDS sequence of ZjWRKY22 gene obtained in the jujube variety Huping was 1 068 bp, encoding 335 amino acids with a molecular weight of 38.9 ku and isoelectric point of 5.92. Its molecular formula was C1682H2582N472O568S13. The protein contained 18% of serine and was hydrophilic unstable protein. It embraced 76 phosphorylation sites without signal peptides and transmembrane domains. The secondary structure mainly consisted of random curl with a typical WRKY domain. The tertiary structure was mainly composed of four β-folds, namely WRKYGQK, RGYYR, RKQVER, and FIVTYT, which belonged to the IIe group of the WRKY family. The homologous sequence alignment showed that the homology of jujube with bayberry, peach, almond, and plum was 75.86%, 74.88%, 74.41%, and 74.88%, respectively. The phylogenetic tree showed that ZjWRKY22 was the closest relative to sour jujube. Real-time fluorescence quantification showed that the expression of ZjWRKY22 was the highest in fruits with tissue specificity. Further, the fusion expression vector pCAMBIA1300-GFP-ZjWRKY22 was constructed, and subcellular localization was performed by instantaneous injection of Agrobacterium into Ben's tobacco to verify that protein ZjWRKY22 was located in the nucleus, simultaneously, the plant overexpression vector pCAMBIA-1300-ZjWRKY22 was successfully constructed. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

[Objective] The effect of PPP3CA gene on growth traits of the Chishui black-bone silky fowl was explored, which provided the basis for genetic improvement and molecular breeding of Chishui black-bone silky fowl. [Method] All exons of PPP3CA gene of Chishui black-bone silky fowl were screened by PCR amplification and direct sequencing.RNAfold WebServer and Structural Bioinformatics Group were used to predict the secondary and tertiary structure of PPP3CA protein, and to calculate the gene frequency, genotype frequency, homozygosity, heterozygosity, number of effective alleles and polymorphic information content.The Hardy-Weinberg equilibrium state was analyzed, and the correlation between the genotypes corresponding to different polymorphic loci and the body size index were analyzed by SPSS. [Result] Three missense mutation sites (C29T,T50C and T63G) were found at exon 7,and one missense mutation site (G720A) was found at exon 16.The χ² test showed that all the above loci deviated from Hardy-Weinberg equilibrium.CC type with C29T mutation significantly increased body weight, pelvic width and chest circumference.CC type with T50C mutation significantly increased body weight, tibial length and keel length.The TT type at T63G site significantly increased the tibial length and keel length.The AA type at G720A significantly increased the tibial length and keel length, and the CC type significantly increased the body oblique length.The CC type at C29T,CC type at T50C, TT type at T63G and AA type at G720A were all dominant genotypes, but the C29T and T50C base mutations were unfavorable mutations, while the T63G and G720A base mutations were favorable mutations, and G720A was more conducive to the growth of black-bone silky fowl, which could be used as a reference site for molecular marker assisting breeding of Chishui black-bone silky fowl. [Conclusion] The study is the first to investigate the correlation between PPP3CA gene and chicken growth traits, and finds four polymorphic loci in the exon of PPP3CA gene in domestic chickens, indicating that PPP3CA gene has a certain effect on growth traits of Chishui black-bone silky fowl, and can be used as a reference site for molecular marker assisting breeding of Chishui black-bone silky fowl.The results of the study can provide reference for genetic improvement and breeding of Chishui black-bone silky fowl in the future, and lay a foundation for further research on PPP3CA gene of chicken. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of South China Fisheries Science is the property of South China Fisheries Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Acta Agriculturae Zhejiangensis is the property of Acta Agriculturae Zhejiangensis Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Tumor Necrosis Factor Superfamily (TNFSF) and Tumor Factor Receptor Superfamily (TNFRSF) regulate cell apoptosis, metabolism and development. To explore the expression and function of TNFSF and TNFRSF in teleosts, we cloned tnfsf10 and tnfrsf10 of the sterlet, Acipenser ruthenus, and analyzed their structure and evolution. Results showed that, Tnfsf10 and Tnfrsf10 of the sterlet were located at the base of actinopterygii branch in phylogenetic tree and have low homology with Tnfsf10 and Tnfrsf10 of the tetrapod, however, their tertiary structure is similar to Tnfsf10 and Tnfrsf10 of the human. Whole-mount in situ hybridization analysis showed that tnfsf10 and tnfrsf10 were mainly expressed in the horizontal muscle septum of the trunk, infraorbital canal of the head, preopercular lateral line, and neuromast of the ventral rostral. After being treated with Tnfrsf10 specific activator Bioymifi, the morphology of sterlet larvae did not change significantly, but the number of hair cells in neuromast increased significantly. The findings suggest that the Tnfsf10 and Tnfrsf10 of the sterlet represent the original form of the teleost homologous protein, which may be specifically involved in the development of hair cells in the lateral line neuromast. [ABSTRACT FROM AUTHOR]

[Objective] The resistance of Plutella xylostella to chemical insecticides is increasing year by year, which makes RNAi (RNA interference ) pesticides widely concerned. The P. xylostella SR have phagocytic and pathogenclearing abilities in cellular immunity, rendering them a promising target for RNAi pesticides. This study explores alternative targets for such pesticides by investigating the SR gene family in P. xylostella. [Method] Based on the P. xylostella genome, we comprehensively analyzed the physicochemical properties, transmembrane structure, phylogenetic evolution, secondary and tertiary structure prediction, conserved protein motifs and phosphorylation site prediction of SR gene family. [Result] The SR gene family of P. xylostella has 12 CD36 protein sequences with similar physicochemical properties and functional structures, all of which contain multiple hydrophilic and hydrophobic regions as well as two transmembrane helical regions. Their secondary and tertiary structures feature irregular coiling with the highest serine content in the phosphorylation site. A total of six species, including P. xylostella, Bombyx mori, Anopheles gambiae, Drosophila melanogaster, Manduca sexta and Tribolium castaneum contained 117 CD36 protein sequences that were classified into five distinct branches on the evolutionary tree. Genes with similar structures were grouped together within the same branch, indicating a high conservation throughout evolution. CD36px4 and CD36px5 exhibit more intricate tertiary structures. The motif 19 and motif 20 are exclusive to CD36px4, suggesting their potential involvement in species evolution. With a staggering 143 phosphorylation sites, CD36px4 may play a crucial role in the phagocytosis and clearance of apoptotic cells. [Conclusion] The 12 SRs identified are transmembrane proteins with abundant phosphorylation sites, predicted to participate in various physiological processes such as intracellular and extracellular material transport, signal transduction, energy metabolism, and apoptosis regulation. They also possess the functions of mediating phagocytosis and clearance of cellular debris. These receptors represent a promising target for RNAi-based pesticides. The results have provided a crucial foundation for the screening of RNAi pesticide targets. [ABSTRACT FROM AUTHOR]

[Objective] The present paper aimed to identify CBF family members using whole genome data of Prunus sibirica, and to analyze the characteristics and functions of the conserved domains and their expression patterns after low temperature stress of CBF transcription fac- tors. [Method] By the P. sibirica whole genome database, the CBF genes of P. sibirica were searched using BLASTP and HMM, and their conserved structural domains were verified by CDD and MEME. Bioinformatics tools such as Prot-Param, WOLF PSORT, MAGA X, Phyre2 and PlantCARE were used to analyze protein physicochemical properties, subcellular localization, phylogeny, tertiary structure, chromosom- al localization and cis-elements, respectively. Quantitative real-time PCR (RT-qPCR) was used to analyze the expression pattern of CBF gene after low temperature stress in P. sibirica. [Result] In the study, four PSCBF's were identified, all of which possessed the conserved structural domains PKKPAGR and DSAWR sequences of the AP2 gene family. The PSCBFs contained 206-246 amino acids, with a mean molecular weight of 25. 80 KDa and a mean isoelectric point of 5.92. PSCBF3 and PSCBF4 were similar in gene structure and had closer ge- netic relationship. The subcellular localization of 4 PSCBFs was located in the nucleus. Promoter cis-acting element analysis showed that CBF family members could participate in plant hormone and abiotic stress responses. Four CBF members were all acidic and hydrophilic pro- teins. The expression of PSCBF's was higher mainly in the early stage (15 min) after low temperature stress. [Conclusion] The study shows more complete information on the CBF gene family of P. sibirica, which offers new insights into the complex mechanisms and pathways of PSCBF in response to low-temperature stress at different stages. It lays an important theoretical foundation for further investigations into the biological functions of CBF family members. [ABSTRACT FROM AUTHOR]

Copyright of Food & Machinery is the property of Food & Machinery Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of South China Fisheries Science is the property of South China Fisheries Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Chinese Journal of Preventive Veterinary Medicine / Zhongguo Yufang Shouyi Xuebao is the property of Chinese Journal of Preventive Veterinary Medicine Editorial Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

The study was to investigate the structure and function of LPD06283 protein of Rhodococcus opacus PD630. Bioinformatics methods were used to analyze the physicochemical properties, hydrophilicity and hydrophobicity, amphiphilic α helix, homology, signal peptide, transmembrane region, secondary structure, domain, tertiary structure, phosphorylation modification sites and interacting proteins of LPD06283 protein. The results showed that LPD06283 protein was a stable acidic hydrophilic protein, the N-terminal hydrophobic region of which formed an amphiphilic α-helix, closely related to MLDS protein of Rhodococcus jostii RHA1, and contained no signal peptide or transmembrane region. The secondary structure of LPD06283 protein was composed of α-helix (81.88%), β-turn (3.62%) and random coil (14.49%), there was an apolipoprotein domain at N-terminus, the tertiary structure was predicted by comprehensive method and was of high quality; LPD06283 protein contained 19 phosphorylation sites, the strongest interacting protein was XRE family DNA-binding protein. The study indicates that LPD06283 protein may be involved in lipid metabolism of Rhodococcus opacus, which can be used as a potential target for microbial lipid research and development. [ABSTRACT FROM AUTHOR]

In order to explore the differences in the molecular mechanism of the Pueraria cultivars between isoflavone metabolic enzyme gene PtCHI, and to preliminarily reveal the difference content causes of the isoflavones. The materials of the study were Pueraria montana var. lobata and P. montana var. thomsonii. Puerarin and total flavonoids of P. montana var. lobata and P. montana var. thomsonii were extracted by ethanol, and their contents were measured by high-performance liquid chromatography. Based on the reported CHI gene of Pueraria montana var. lobata, the PtCHI gene from P. montana var. thomsonii was isolated by homologous cloning method, and the protein was expressed in vitro. At the same time, the location of the PtCHI gene was studied in Arabidopsis thaliana protoplasts. The results were as follows: (1) The content of puerarin in P. montana var. lobata was significantly higher than the P. montana var. thomsonii, and the content of total flavonoids was also higher but not significant. (2) The gene PtCHI was successfully isolated from P. montana var. thomsonii. The gene was 742 bp in length, containing a complete ORF frame of 672 bp, encoding 223 amino acids, and had up to 99% homology with P. montana var. lobata. (3) This study found that the expression of CHI gene in P. montana var. thomsonii was stem>root>leaf, P. montana var. lobata was root>stem>leaf. The expression of CHI gene from P. montana var. lobata was significantly higher than P. montana var. thomsonii besides in leaves. (4) Through the online tool prediction analysis, PtCHI was found to be stable hydrophilic protein and the size was 27.8 kD. The secondary and tertiary structures were based on α-helix, with 25 phosphorylation sites, closely relating P. montana var. lobata, Glycine max and Glycyrrhiza uralensis, and were more likely to interact with F3H2, F3H, 4CL4, DFR2 and CHS. (5) At the same time, the protein of PtCHI was successfully induced and isolated in vitro, with a single protein of 27.8 kD. (6) Through the Arabidopsis thaliana protoplasts revealed that PtCHI was mainly located in the chloroplasts. This study is in further analyzing the difference in flavonoids in P. montana var. lobata and P. montana var. thomsonii, as well as laying the foundation for the functional verification of P. montana var. thomsonii PtCHI and the research on the mechanism of isoflavone metabolism. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

【Objective】 Cloning and bioinformatics analysis of Bone morphogenetic protein receptor II (BMPRII)gene were carried out, and its expression differences in different tissues of Tibetan sheep were detected, which provided a reference for studying the biological function of BMPRII gene in Tibetan sheep.【Method】 In the present experiment, six Tibetan sheep with similar age and body weight were randomly selected for slaughter and samples of each tissue were collected. RNA was extracted and quality detection was performed, and Real-time qPCR was used to detect the expression levels of BMPRII gene in 13 tissues, including hypothalamus, pituitary, heart, liver, spleen, lung, kidney, ovary, uterus, oviduct, rumen, duodenum and longissimus dorsi of Tibetan sheep, and to analyze the specific expression and distribution of BMPRII gene in different tissues of Tibetan sheep. Coding region of BMPRII gene sequence in Tibetan sheep was amplified and analyzed through PCR, cloning, sequencing and the bioinformatics tools.【Result】BMPRII gene was expressed widely in all the above 13 tissues. The expression in liver was higher than that in uterus, ovary and spleen, but did not reach a significant level (P＞0.05), and significantly higher than that in other tissues (P＜0.05). The lowest expression was found in the longissimus dorsi. The CDS sequence of Tibetan sheep BMPRII gene was 3117 bp, encoding 1038 amino acids. The amino acid sequence of BMPRII was most closely related to sheep, cattle and yaks, and the furthest from zebras and chickens. Tibetan sheep BMPRII protein was a hydrophilic secretory protein with instability, containing 1 transmembrane structure and signal peptide, with 127 potential phosphorylation sites and 14 potential N-glycosylation sites, mainly distributed outside the cell. The secondary structure of Tibetan sheep BMPRII protein was mainly random coiling, followed by α-helix, extended chain and β-angle, and the prediction results of the tertiary structure were consistent with the secondary structure. 【Conclusion】BMPRII gene plays an important role in various physiological activities of Tibetan sheep. The results of experiment provide basic data for further research on the regulation mechanism of BMPRII gene of Tibetan sheep on reproductive performance of Tibetan sheep. [ABSTRACT FROM AUTHOR]

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

【Objective】The biological information characteristics of GATA transcription factors of mulberry were identified and analyzed, and the function and gene evolution of mulberry GATA family genes were explored, which provided a certain theoretical basis for subsequent research on mulberry molecular breeding and improved variety selection.【Method】The genome-wide identification, physicochemical analysis, homeogenic elements and conserved domains of the mulberry GATA family were analyzed by bioinformatics methods.【Result】The physical and chemical properties of the members of the mulberry GATA family were significantly different, but the subcellular localization prediction showed that they were all located in the nucleus; There were certain differences in the tertiary structure of GATA proteins as a whole, but the similarity of the same subfamily was high, and there may be a certain synergistic regulation function in some physiological response processes of plants; Phylogenetic analysis, the mulberry GATA members were divided into 4 subfamilies, and members in the same subfamily had similar conservation motif and gene structure; Expression pattern analysis showed that there were significant differences in the expression patterns of GATA genes in different tissues（roots, epidermal, leaves, winter buds and flowers） of mulberry, most of which had higher expression in roots, which may be closely related to root development and drought resistance of mulberry; Analysis of cis-acting elements in the GATA promoter of mulberry showed that MnGATAs may be involved in transcriptional regulation and plant hormone signaling regulation under biotic/abiotic stress. 【Conclusion】A total of 23 MnGATAs were identified in the whole genome of mulberry, with obvious conservation, and the expression patterns in various tissues of mulberry were significantly different, which may regulate the physiological response of mulberry under stress. The research on gene evolution, molecular breeding and selection of elite varieties provides a certain theoretical basis. [ABSTRACT FROM AUTHOR]

Copyright of Journal of Chinese Institute of Food Science & Technology / Zhongguo Shipin Xuebao is the property of Journal of Chinese Institute of Food Science & Technology Periodical Office and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Food Research & Development is the property of Food Research & Development Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Shipin Kexue/ Food Science is the property of Food Science Editorial Department and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

WD40, as a transcription factor family, is widely involved in regulating plant growth, development, secondary metabolite accumulation and environmental adaptation. In order to explore the role of the WD40 family in the growth, development, secondary metabolite accumulation and tolerance, the WD40 genes of Meconopsis horridula were identified in this study based on the full-length transcriptome sequencing data and conducted bioinformatics analysis of these genes and their encoded proteins. The results were as follows:(1) A total of 19 WD40 genes were identified, and all the proteins included typical WD40 domain, the amino acid numbers and molecular weight of the protein encoded by WD40 genes were 109-758 aa and within 11 830-84 130 Da, respectively, and most of the proteins localized in the nucleus, and all proteins belonged to hydrophilic protein;(2) Phylogenetic tree analysis showed that WD40 proteins of Meconopsis horridula were closely to Papaver somniferum and Macleaya cordata;(3) The promoter region of WD40 gene contained different amounts of hormones or stress-response elements, suggesting that this family genes may be involved in the regulation of various biological processes, such as growth, development and secondary metabolite accumulation;(4) The tertiary structure of WD40 proteins showed that these proteins evolved in different degrees during the evolutionary process. These results can provide a preliminary basis for further research on the specific mechanism of WD40 gene family in response to stress and secondary metabolite accumulation. [ABSTRACT FROM AUTHOR]

【Objective】The bioinformatics characteristics of FtCOP1 gene（Fagopyrum tartaricum Gaertn） fromCOP1（Constitutive Photomorphogenic 1） of Fagopyrum tartaricum Gaertn and the expression pattern in anthocyanin biosynthesis of tartary buckwheat are studied, which provides a basis for further studying the molecular mechanism of the involvement of COP1 gene in anthocyanins biosynthesis, and provides reference for improving the quality of tartary buckwheat by using FtCOP1. 【Method】The COP1 gene of tartary buckwheat was cloned by PCR and analyzed by bioinformatics. The physicochemical properties, secondary and tertiary structure, prediction of subcellular localization, conserved domain and evolutionary relationship with COP1 protein of other species were analyzed. RT-qPCR was used to analyze the relationship between the gene and the expression level of anthocyanin biosynthesis structure genes and the anthocyanins content in tartary buckwheat under normal light and dark conditions. 【Result】The complete length of CDS of FtCOP1 gene was 2082 bp, which consisted of 13 exons and 12 introns, encodings 693 amino acids. The theoretical pI value was 6. 23 and the protein size was 75. 876 kD. It was supposed to be hydrophilic, located in the nucleus and contained a transmembrane helical domain without signal peptide. The main components of the secondary and tertiary structures were random coil and α helix. The COP1 protein of tartary buckwheat was most closely genetic related to the COP1 of quinoa. The COP1 protein has similar motif and conserved domains as that of other species, and the gene structure were also similar. The expression level of FtCOP1 in dark cultured sprouts was significantly higher than that in normal light cultured, and was negatively related to the expression of anthocyanin biosynthesis structural genes and anthocyanins accumulation. 【Conclusion】 COP1 proteins of tartary buckwheat and other species in plant evolution is conservative, and it is speculated that FtCOP1 may negatively regulate light-dependent anthocyanin biosynthesis. [ABSTRACT FROM AUTHOR]