32 results on '"Jirawat Yongsawatdigul"'
Search Results
2. Thigh muscle metabolic response is linked to feed efficiency and meat characteristics in slow-growing chicken
- Author
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Pramin Kaewsatuan, Chotima Poompramun, Satoshi Kubota, Jirawat Yongsawatdigul, Wittawat Molee, Pekka Uimari, and Amonrat Molee
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Animal Science and Zoology ,General Medicine - Published
- 2023
3. Meat quality and Raman spectroscopic characterization of Korat hybrid chicken obtained from various rearing periods
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Amonrat Molee, Kanjana Thumanu, Jirawat Yongsawatdigul, and Sasikan Katemala
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Market needs ,2019-20 coronavirus outbreak ,Meat ,Coronavirus disease 2019 (COVID-19) ,chicken ,Guanosine Monophosphate ,Spectrum Analysis, Raman ,Crossbreed ,meat quality ,principle component analysis ,Protein content ,Inosine Monophosphate ,Fourier transform Raman spectroscopy ,Animals ,Food science ,Spectral data ,lcsh:SF1-1100 ,Fourier Analysis ,business.industry ,Chemistry ,Fatty Acids ,Broiler ,Age Factors ,Proteins ,food and beverages ,General Medicine ,Processing and Products ,Poultry farming ,Hydrogen-Ion Concentration ,Cholesterol ,age ,Purines ,Animal Science and Zoology ,Collagen ,lcsh:Animal culture ,business ,Shear Strength ,Chickens - Abstract
Meat quality attributes vary with chicken age. Understanding the relationship between poultry age and the quality of the meat would be beneficial for efficient poultry farming to meet market needs. The Korat hybrid chicken (KC) is a new crossbred chicken whose meat quality is distinct from that of commercial broiler (CB) chickens and has not been well characterized. In this study, we characterized the physico-chemical properties of KC meat and correlate the findings with Raman spectral data. The protein content of KC breast and thigh meat increased with age. The pH of thigh meat decreased, while the water-holding capacity of breast meat increased as the age of the chickens increased. The amount of cholesterol in breast meat decreased as the rearing period was extended. Inosine 5′-monophosphate and guanosine 5′-monophosphate of breast meat decreased as KC grew older. The shear force values of meat from older birds increased concomitantly with an increase in total collagen. Principle component analysis revealed that the meat quality of CB was greatly different from that of KC meat. High shear force values of KC meat at 20 wk of age were well correlated with an increase in the β-sheet structure (amide I) and amide III of collagen. Raman spectra at 3,207 cm−1 and relative α-helical content were negatively correlated with shear force values of KC breast meat. These could be used as markers to evaluate KC meat quality.
- Published
- 2021
4. Heating temperatures affect meat quality and vibrational spectroscopic properties of slow- and fast-growing chickens
- Author
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Sasikan Katemala, Amonrat Molee, Kanjana Thumanu, and Jirawat Yongsawatdigul
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Animal Science and Zoology ,General Medicine - Published
- 2023
5. Reduction of red blood spots in cooked marinated chicken breast meat by combined microwave heating and steaming
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Matthanee Jantaranikorn, Kanjana Thumanu, and Jirawat Yongsawatdigul
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Animal Science and Zoology ,General Medicine - Abstract
One of the defects commonly found in cooked marinated chicken breast products is a red blood spot (RBS), which is caused by undercooked blood in vessels. This problem was alleviated by microwave (MW) pre-heating for 6 to 7 min, followed by steaming. RBS formation decreased when samples were heated to a core temperature of 80°C and were completely eliminated at a core temperature of 82°C and 85°C when a MW pre-heating step was applied for 7 min. Based on synchrotron-based Fourier transform infrared spectroscopy (SR-FTIR), blood remaining in the blood vessel had a lower α-helical content when samples were cooked by the combination of MW heating and steaming as compared with those prepared by steaming alone (P0.05). MW pre-heating decreased cooking time by 28 to 48% as compared with steaming alone. Heating regimes had no effect on cooking loss, pH, water-holding capacity, and shear force. MW pre-heating for 7 min followed by steaming to a core temperature of 82°C appeared to be an effective heating regime to reduce the occurrence of RBS, with acceptable cooking loss.
- Published
- 2022
6. Effects of β-alanine and L-histidine supplementation on carnosine contents in and quality and secondary structure of proteins in slow-growing Korat chicken meat
- Author
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Chanadda Suwanvichanee, Panpradub Sinpru, Kasarat Promkhun, Satoshi Kubota, Cindy Riou, Wittawat Molee, Jirawat Yongsawatdigul, Kanjana Thumanu, and Amonrat Molee
- Subjects
Meat ,Carnosine ,Dietary Supplements ,beta-Alanine ,Animals ,Animal Science and Zoology ,Female ,Histidine ,General Medicine ,Anserine ,Muscle, Skeletal ,Chickens - Abstract
Carnosine enrichment of slow-growing Korat chicken (KRC) meat helps differentiate KRC from mainstream chicken. We aimed to investigate the effects of β-alanine and L-histidine supplementation on the carnosine synthesis in and quality and secondary structure of proteins in slow-growing KRC meat. Four hundred 21-day-old female KRC were used, and a completely randomized design was applied. The chickens were divided into 4 experimental groups: basal diet (A), basal diet supplemented with 1.0% β-alanine (B), 0.5% L-histidine (C), and 1.0% β-alanine combined with 0.5% L-histidine (D). Each group consisted of 5 replicates (20 chickens per replicate). On d 70, 2 chickens per replicate were slaughtered, and the levels of carnosine, anserine, and thiobarbituric acid reactive substances were analyzed. Biochemical changes were monitored using synchrotron radiation-based Fourier transform infrared microspectroscopy; 5 chickens per replicate were slaughtered, and the meat quality was analyzed. Statistical analysis was performed using ANOVA and principal component analysis (PCA). Group D chickens exhibited the highest carnosine meat content, followed by those in groups B and C. However, amino acid supplementation did not affect anserine content and growth performance. Higher carnosine levels correlated with increasing pH
- Published
- 2021
7. Comparative proteomics revealed duodenal metabolic function associated with feed efficiency in slow-growing chicken
- Author
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Pramin Kaewsatuan, Chotima Poompramun, Satoshi Kubota, Jirawat Yongsawatdigul, Wittawat Molee, Pekka Uimari, Amonrat Molee, Helsinki One Health (HOH), Department of Agricultural Sciences, Animal Science Research, and University of Helsinki
- Subjects
Slow-growing chicken ,Male ,Proteomics ,Proteome ,Duodenum ,Feed efficiency ,General Medicine ,Label-free proteomics ,Animals ,Animal Science and Zoology ,412 Animal science, dairy science ,Chickens ,Metabolic Networks and Pathways ,Korat chicken - Abstract
The Korat chicken (KR), developed in Thailand, is a slow-growing breed developed as an alternative breed for Thai chicken producers. The growing interest in slow-growing chicken meat, due to its unique taste, distinct texture, health benefits, and higher broiler welfare have led to higher market demand for KR. However, its low feed efficiency (FE) has a significant negative impact on farm profitability. Understanding the molecular mechanism regulating FE allows for designing a suitable selection program and contributing to breeding more efficient chicken for poultry production. Thus, the objective of our study was to investigate the proteome differences and possible pathways associated with FE in male KR using a label-free quantitative proteomic approach. Seventy-five KR males were individually evaluated for FE, and duodenum samples from 6 animals (3 high-FE and 3 low-FE chickens) were collected at 10 wk of age for differential abundant proteins (DAPs), protein networks, functional enrichment, and pathway analyses. In this study, we found 40 DAPs significantly associated with FE pathways, including glycolysis/gluconeogenesis, peroxisome, oxidative phosphorylation, tight junction, and cysteine and methionine metabolism. Thus, variations in observed DAPs or genes related to DAPs could be interesting biomarker candidates for selection for higher feed utilization efficiency in chicken.
- Published
- 2021
8. A comparative study of meat quality and vibrational spectroscopic properties of different chicken breeds
- Author
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Sasikan Katemala, Amonrat Molee, Kanjana Thumanu, and Jirawat Yongsawatdigul
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Meat ,Inosine Monophosphate ,Spectrum Analysis ,Animals ,Animal Science and Zoology ,General Medicine ,Chickens ,Lipids ,Inosine - Abstract
Chicken breed is one of the key factors that influence meat quality. The quality attributes of breast meat from commercial broiler (CB), Thai native chicken (NC, Leung Hang Khao), and the crossbred Korat chicken (KC) were investigated via synchrotron radiation-based Fourier transform infrared (SR-FTIR) microspectroscopy, Fourier transform Raman (FT-Raman) spectroscopy, and physicochemical analysis. The protein and carbonyl contents of KC and NC meats were higher than that of CB meat, but the lipid content was lower (P0.05). CB meat was characterized by high moisture, lightness (L*), and presence of taste-active nucleotides, namely, inosine 5'-monophosphate (IMP) and guanosine 5'-monophosphate (GMP). Moreover, NC meat had the highest insoluble collagen and inosine contents (P0.05). The predominant protein secondary structures of KC and NC meats were β-turns and random coils, whereas α-helices were mainly found in CB meat. Based on principal component analysis, the meat quality and spectra were clearly separated by breeds. The high moisture and lipid content of meat corresponded to O-H stretching (3,203 cm
- Published
- 2022
9. Production and characterization of chicken blood hydrolysate with antihypertensive properties
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Soichiro Nakamura, Jirawat Yongsawatdigul, Takakazu Mitani, Shigeru Katayama, and Wasana Wongngam
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hypertension ,Protein Hydrolysates ,Angiotensin-Converting Enzyme Inhibitors ,Blood Pressure ,Hydrolysate ,Hydrolysis ,Oral administration ,spontaneously hypertensive rat (SHR) ,Renin–angiotensin system ,Animals ,Food science ,Antihypertensive Agents ,lcsh:SF1-1100 ,chemistry.chemical_classification ,General Medicine ,Blood Proteins ,Processing and Products ,angiotensin I-converting enzyme (ACE) ,Amino acid ,Rats ,Disease Models, Animal ,Enzyme ,Blood pressure ,chemistry ,Animal Science and Zoology ,lcsh:Animal culture ,Digestion ,chicken blood ,Chickens ,protein hydrolysate - Abstract
Chicken blood has limited utilization despite its high protein content. Production of a blood hydrolysate exhibiting angiotensin I-converting enzyme (ACE)–inhibitory activity would be means of valorizing chicken blood. The optimized conditions used to produce chicken blood corpuscle hydrolysate (BCH) by Alcalase were 51.1°C, 4% enzyme, and pH 9.6 for 6 h, resulting in a 35.8% degree of hydrolysis and 37.7% ACE inhibition at a peptide concentration of 0.2 mg/mL. The permeate of a 1-kDa membrane, BCH-III, showed a 2.5-fold increase in ACE inhibition compared with that of BCH. BCH-III was resistant to in vitro gastrointestinal digestion, whereas the BCH digesta exhibited an increased ACE-inhibitory activity after digestion. Both BCH and BCH-III were rich in hydrophobic amino acids. A single administration of BCH and BCH-III to spontaneously hypertensive rats at concentrations of 600 and 100 mg/kg, respectively, lowered the systolic blood pressure by −57.7 and −70.9 mmHg, respectively, 6 h after oral administration compared with the control group. The blood pressure–lowering effect of the 600 mg/kg BCH dose was comparable with that of the 100 mg/kg BCH-III dose after 4 wk of oral administration. Both BCH and BCH-III could be developed for use as nutraceutical products with antihypertensive effects.
- Published
- 2019
10. Immunomodulatory activity of protein hydrolysates derived from Virgibacillus halodenitrificans SK1-3-7 proteinase
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Tidarat Toopcham, Jurriaan J. Mes, Jirawat Yongsawatdigul, and Harry J. Wichers
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Fish Proteins ,Lipopolysaccharides ,0301 basic medicine ,Protein Hydrolysates ,Interleukin-1beta ,Anti-Inflammatory Agents ,Hydrolysate ,Analytical Chemistry ,Immunomodulation ,03 medical and health sciences ,Hydrolysis ,Virgibacillus ,Casein ,Gene expression ,Animals ,Humans ,Interleukin 8 ,Cells, Cultured ,Food, Health & Consumer Research ,VLAG ,Plant Proteins ,Inflammation ,030109 nutrition & dietetics ,biology ,Interleukin-6 ,Tumor Necrosis Factor-alpha ,Chemistry ,Macrophages ,Pea protein ,Interleukin-8 ,Peas ,Caseins ,Cichlids ,General Medicine ,Protein hydrolysate ,biology.organism_classification ,Immunity, Innate ,Health & Consumer Research ,Gene Expression Regulation ,Biochemistry ,Food ,Cyclooxygenase 2 ,Tumor necrosis factor alpha ,Peptide Hydrolases ,Food Science - Abstract
Modulation of inflammation-related immune response on THP-1 macrophages of protein hydrolysates derived from tilapia mince, casein and pea protein, were investigated. The protein substrates were hydrolyzed by Virgibacillus halodenitrificans SK1-3-7 proteinase. The degree of hydrolysis (DH) of casein was observed to be the highest throughout the course of hydrolysis. When challenging THP-1 macrophages, tilapia mince hydrolysate (TMH) enhanced innate immunity through induction of IL-1β and COX-2 expression. Anti-inflammatory activity was observed in casein hydrolysate (CH) and pea protein hydrolysate (PPH) by attenuating lipopolysaccharide- (LPS) induced pro-inflammatory gene expression in THP-1 macrophages. CH suppressed IL-1β, IL-6, IL-8, TNF-α and COX-2, while PPH reduced LPS-induced IL-6 and TNF-α responses. In addition, CH and PPH showed stronger suppression of LPS-induced pro-inflammatory gene expression compared with non-hydrolyzed casein and pea protein. These results suggest that TMH, CH and PPH prepared from V. halodenitrificans SK1-3-7 proteinase are potential functional food ingredients with immunomodulatory activity.
- Published
- 2017
11. Cellular and chemical antioxidant activities of chicken blood hydrolysates as affected by in vitro gastrointestinal digestion
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Ali Hamzeh, Wasana Wongngam, Jirawat Yongsawatdigul, and Ratana Kiatsongchai
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animal structures ,Antioxidant ,Protein Hydrolysates ,medicine.medical_treatment ,In Vitro Techniques ,Hydrolysate ,Antioxidants ,03 medical and health sciences ,chemistry.chemical_compound ,Pepsin ,Thermolysin ,Blood plasma ,medicine ,Animals ,Food science ,030304 developmental biology ,0303 health sciences ,ABTS ,biology ,Chemistry ,0402 animal and dairy science ,04 agricultural and veterinary sciences ,General Medicine ,040201 dairy & animal science ,Red blood cell ,medicine.anatomical_structure ,biology.protein ,Animal Science and Zoology ,Animal Nutritional Physiological Phenomena ,Digestion ,Chickens - Abstract
The effects of in vitro gastrointestinal (GI) digestion on the antioxidative activity of hydrolysates prepared from chicken blood plasma and red blood cell (RBC) by pepsin and thermolysin were investigated. The pepsin-hydrolyzed plasma (PHP) showed the highest scavenging activity of ABTS radicals (P < 0.05). RBC and plasma hydrolysates prepared by pepsin were hydrolyzed by GI proteases to a greater extent than hydrolysates prepared by thermolysin as evidenced by MALDI-TOF mass spectra. The antioxidative activity of all digesta increased compared to their respective parent hydrolysates, and PHP digesta showed the highest activity (P < 0.05). The digesta of PHP and thermolysin-hydrolyzed plasma showed cytoprotective properties in a dose-dependent manner, and 100 μg/mL of PHP digesta exhibited the highest protection of HepG2 cells against tert-butyl hydroperoxide (P < 0.05). Based on dichloro-dihydro-fluorescein diacetate assay, PHP digesta exhibited the greatest intracellular reactive oxygen species scavenging activity of approximately 71% at 100 μg/mL (P < 0.05). The peptide sequencing of PHP digesta revealed that they contained less than 10 amino acid residues, with an average hydrophobicity of 18.6. Chicken blood plasma is a better protein source for protein hydrolysates, and their digesta showed higher antioxidant activity compared to RBCs.
- Published
- 2018
12. Chemical and cellular antioxidative properties of threadfin bream (Nemipterus spp.) surimi byproduct hydrolysates fractionated by ultrafiltration
- Author
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Hang Xiao, Chompoonuch Wiriyaphan, Eric A. Decker, and Jirawat Yongsawatdigul
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Antioxidant ,Protein Hydrolysates ,medicine.medical_treatment ,Ultrafiltration ,Antioxidants ,Hydrolysate ,Analytical Chemistry ,chemistry.chemical_compound ,Lactate dehydrogenase ,Endopeptidases ,medicine ,Animals ,Humans ,Cytotoxicity ,biology ,Nemipterus ,Fishes ,General Medicine ,biology.organism_classification ,In vitro ,Perciformes ,chemistry ,Biochemistry ,Threadfin bream ,Reactive Oxygen Species ,Intracellular ,Food Science - Abstract
Protein hydrolysate from frame, bone and skin (FBSH) of threadfin bream was prepared using Virgibacillus sp. SK33 proteinase and fractionated using sequential ultrafiltration membranes with molecular weight cut-offs (MWCO) of 30, 5 and 1 kDa, respectively. Four fractions, namely FBSH-I (>30 kDa), FBSH-II (5-30 kDa), FBSH-III (1-5 kDa), and FBSH-IV (
- Published
- 2015
13. Transepithelial transport across Caco-2 cell monolayers of angiotensin converting enzyme (ACE) inhibitory peptides derived from simulated in vitro gastrointestinal digestion of cooked chicken muscles
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Kiattawee Choowongkomon, Sittiruk Roytrakul, Jirawat Yongsawatdigul, Papungkorn Sangsawad, Xiu-Min Chen, David D. Kitts, Guangtao Meng, and Eunice C.Y. Li-Chan
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0301 basic medicine ,Cell ,Muscle Proteins ,Angiotensin-Converting Enzyme Inhibitors ,Peptidyl-Dipeptidase A ,Permeability ,Analytical Chemistry ,03 medical and health sciences ,0404 agricultural biotechnology ,Monolayer ,Myosin ,medicine ,Animals ,Humans ,Cooking ,biology ,Chemistry ,Angiotensin-converting enzyme ,04 agricultural and veterinary sciences ,General Medicine ,Permeation ,040401 food science ,Molecular biology ,In vitro ,Molecular Docking Simulation ,Protein Transport ,030104 developmental biology ,medicine.anatomical_structure ,Caco-2 ,Permeability (electromagnetism) ,biology.protein ,Digestion ,Caco-2 Cells ,Peptides ,Chickens ,Food Science - Abstract
Korat-chicken breast and thigh were subjected to heating at 70, 100 or 121 °C for 30 min and simulated in vitro gastrointestinal digestion. At 70 or 100 °C heating, digests of breast possessed higher ACE inhibitory activity than those of thigh. The highest ACE inhibitory activity was found in the digest of breast cooked at 70 °C (B/H-70), whereas breast heated at 121 °C (B/H-121) exhibited the lowest. The 1-kDa permeate of the B/H-70 digest revealed higher permeability through colorectal adenocarcinoma monolayers and ACE inhibitory activity than did B/H-121. Among nine transported peptides, APP derived from myosin showed the highest ACE inhibition, with a non-competitive characteristic (Ki 0.93 μM). Molecular docking showed that APP interacts with ACE via hydrogen bonds, electrostatic and van der Waals interactions. In conclusion, mild thermal treatment of chicken breast resulted in a higher amount of transported peptides, exerting higher ACE inhibitory activity, which could lead to potential health benefits.
- Published
- 2017
14. Production and purification of antioxidant peptides from a mungbean meal hydrolysate by Virgibacillus sp. SK37 proteinase
- Author
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Nawaporn Lapsongphon and Jirawat Yongsawatdigul
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Antioxidant ,Food Handling ,Protein Hydrolysates ,medicine.medical_treatment ,Size-exclusion chromatography ,Ultrafiltration ,Antioxidants ,Hydrolysate ,Analytical Chemistry ,Hydrolysis ,chemistry.chemical_compound ,Bacterial Proteins ,Virgibacillus ,medicine ,Butylated hydroxytoluene ,Plant Proteins ,Chromatography ,ABTS ,biology ,Chemistry ,Fabaceae ,General Medicine ,biology.organism_classification ,Peptides ,Peptide Hydrolases ,Food Science - Abstract
Antioxidant peptides of mungbean meal hydrolysed by Virgibacillus sp. SK37 proteinases (VH), Alcalase (AH) and Neutrase (NH) were investigated. The antioxidant activities based on 2,2′-azinobis (3-ethyl-benzothiazoline-6-sulphonate) (ABTS) radical-scavenging, ferric-reducing antioxidant power (FRAP) and metal chelation of VH were comparable to those of NH. VH was purified using ultrafiltration, ion exchange and gel filtration chromatography. The purified peptides (F37) from VH, which had the highest specific antioxidant activity, consisted of four peptides containing an arginine residue at their C-termini. In addition, the ABTS radical-scavenging activity of the purified peptides (F42) at 0.148 mg/ml was comparable to that of 1 mM of butylated hydroxytoluene (BHT). These two fractions were stable over a wide pH (4–10) and temperature (25–121 °C) range. Virgibacillus sp. SK37 proteinase is a potential processing-aid for the production of a mungbean meal hydrolyzate with antioxidant properties.
- Published
- 2013
15. Bioavailability of angiotensin I-converting enzyme (ACE) inhibitory peptides derived from Virgibacillus halodenitrificans SK1-3-7 proteinases hydrolyzed tilapia muscle proteins
- Author
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Jirawat Yongsawatdigul, Sittiruk Roytrakul, Harry J. Wichers, Jurriaan J. Mes, and Tidarat Toopcham
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food.ingredient ,Protein Hydrolysates ,Sarcoplasm ,Biological Availability ,Muscle Proteins ,Peptide ,Angiotensin-Converting Enzyme Inhibitors ,Hydrolysate ,Analytical Chemistry ,Hydrolysis ,0404 agricultural biotechnology ,food ,Virgibacillus ,Animals ,Humans ,Caco-2 permeability ,IC50 ,VLAG ,Food, Health & Consumer Research ,chemistry.chemical_classification ,ACE inhibitory activity ,Tilapia ,04 agricultural and veterinary sciences ,General Medicine ,040401 food science ,Bioavailability ,Muscle proteins ,Health & Consumer Research ,Enzyme ,Protein hydrolysates ,Biochemistry ,chemistry ,Food ,Caco-2 Cells ,Peptides ,Food Science ,Peptide Hydrolases - Abstract
The angiotensin I-converting enzyme (ACE) inhibitory activity of protein hydrolysates from tilapia muscle fractions, namely mince (M), washed mince (WM), and sarcoplasmic protein (SP), were investigated. Each fraction was hydrolyzed by Virgibacillus halodenitrificans SK1-3-7 proteinases for up to 24 h. After 8 h of hydrolysis, the M hydrolysate (48% degree of hydrolysis (DH)) showed the highest ACE inhibitory activity, with an IC50 value of 0.54 mg/ml, while the SP hydrolysate exhibited the lowest DH and ACE inhibition. In vitro gastrointestinal digestion reduced the ACE inhibitory activity of the M hydrolysate but enhanced its transport across Caco-2 cell monolayers. The transported peptides were found to contain 3–4 amino acid residues showing strong ACE inhibition. The novel ACE inhibitory peptide with the highest inhibition was found to be MCS, with an IC50 value of 0.29 μM. Therefore, tilapia mince hydrolyzed by V. halodenitrificans proteinases contained ACE inhibitory peptides that are potentially bioavailable.
- Published
- 2016
16. Hydrolytic activity of Virgibacillus sp. SK37, a starter culture of fish sauce fermentation, and its cell-bound proteinases
- Author
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Jirawat Yongsawatdigul, Sureelak Rodtong, and Sornchai Sinsuwan
- Subjects
Fish Proteins ,Hydrolyzed protein ,Physiology ,Biology ,Applied Microbiology and Biotechnology ,Substrate Specificity ,Calcium Chloride ,Hydrolysis ,Bacterial Proteins ,Virgibacillus ,Casein ,Enzyme Stability ,Animals ,Zymography ,Soy protein ,chemistry.chemical_classification ,Molecular mass ,Fishes ,General Medicine ,Enzyme ,Biochemistry ,chemistry ,Fermentation ,Food Microbiology ,Food Technology ,Peptide Hydrolases ,Biotechnology - Abstract
Fish sauce production relies on a natural fermentation process requiring 12-18 months for process completion. Virgibacillus sp. SK37 has been shown to be a potential strain for fish sauce acceleration. However, hydrolytic activity of proteinases bound at cell surface of this strain has not been well elucidated. Addition of 0.2 % CaCl(2) (w/w) in conjunction with starter cultures of Virgibacillus sp. SK 37 increased protein hydrolysis as measured by α-amino group content throughout fermentation (P0.05). Cell-bound proteinases from Virgibacillus sp. SK 37 were extracted into a free form by incubating the washed cells in Ca(2+)-free buffer at 37 °C for 2 h. Cell-bound proteinases revealed molecular mass of 19, 20, 22, 32, 34, and 44 kDa based on a synthetic peptide zymogram. The proteinases showed subtilisin-like serine characteristics with the highest activity at 50 °C and pH 8 and 11. Activity of the extracted proteinases increased ~4 times at ≥100 mM CaCl(2). In addition, CaCl(2) enhanced thermal stability of the extracted proteinases. Enzymes showed proteolytic activity in either the absence or presence of 10 and 25 % NaCl toward fish muscle, soy protein isolate, and casein substrates. Cell-bound proteinases were likely to play an important role in protein hydrolysis during fish sauce fermentation.
- Published
- 2012
17. Identification of novel halotolerant bacillopeptidase F-like proteinases from a moderately halophilic bacterium, Virgibacillus sp. SK37
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Ekkarat Phrommao, Jirawat Yongsawatdigul, and Sureelak Rodtong
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chemistry.chemical_classification ,Thermophile ,Subtilisin ,Peptide ,General Medicine ,Biology ,Applied Microbiology and Biotechnology ,Halophile ,Microbiology ,Isoelectric point ,Enzyme ,chemistry ,Biochemistry ,Halotolerance ,Peptide-mass fingerprint ,Biotechnology - Abstract
Aims: Virgibacillus sp. SK37 isolated from Thai fish sauce produced numerous NaCl-activated subtilisin-like proteinases. Our objectives were to purify, characterize and identify these extracellular proteinases. Methods and Results: Three major subtilisin-like enzymes including 19, 34 and 44 kDa were partially purified and showed maximum activity at pH 8, 55– 60� C, 25–30% NaCl and 70–100 mmol l )1 CaCl2. Enzymes showed stability at 0–30% NaCl and
- Published
- 2010
18. Conformational changes and dynamic rheological properties of fish sarcoplasmic proteins treated at various pHs
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Jirawat Yongsawatdigul, Panchaporn Tadpitchayangkoon, and Jae W. Park
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Chromatography ,Molecular mass ,Chemistry ,Extraction (chemistry) ,Sarcoplasm ,General Medicine ,musculoskeletal system ,Analytical Chemistry ,Hydrophobic effect ,Isoelectric point ,Differential scanning calorimetry ,Rheology ,Food Science ,Catfish - Abstract
The conformational changes and rheological properties of soluble sarcoplasmic proteins isolated from striped catfish (Pangasius hypophthalmus), treated at various pHs (2–12), were investigated. Isoelectric point of striped catfish sarcoplasmic proteins was determined to be pH 5. SDS–PAGE of sarcoplasmic proteins treated at various pHs, showed molecular masses ranging from 11 to 97 kDa. Most sarcoplasmic proteins, regardless of treated pHs, showed a molecular mass of 43 kDa. A decrease in total sulfhydryl content was observed when the pH was shifted away from 6, indicating disulfide formation at pH lower and higher than 6. Gradual increases of S0-ANS and S0-PRODAN were observed as pH increased from 6 to 12, indicating the unfolding of sarcoplasmic proteins during alkaline extraction. DSC thermograms of sarcoplasmic proteins treated at pH 5–9 exhibited an exothermic transition peak, probably due to disulfide bond formation, and/or hydrophobic interactions, which was highly related to the onset temperature of G′ rising. Gel network formation of sarcoplasmic proteins did not take place at extreme pHs ( 9) where proteins were highly charged while the viscoelastic properties of sarcoplasmic proteins were observed at pH 5.5–9. The highest G′ value at 90 °C was observed at pH 5.5 and 8 (P ⩽ 0.05). The gel point, a temperature at which G′ = G″, increased to higher temperature as pH was shifted away from 7.
- Published
- 2010
19. A NaCl-stable serine proteinase from Virgibacillus sp. SK33 isolated from Thai fish sauce
- Author
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Jirawat Yongsawatdigul, Sureelak Rodtong, and Sornchai Sinsuwan
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chemistry.chemical_classification ,Chromatography ,biology ,Sodium ,Subtilisin ,chemistry.chemical_element ,General Medicine ,biology.organism_classification ,Enzyme assay ,Analytical Chemistry ,Divalent ,Serine ,chemistry.chemical_compound ,Enzyme ,chemistry ,Biochemistry ,biology.protein ,Virgibacillus ,PMSF ,Food Science - Abstract
An extracellular proteinase from Virgibacillus sp. SK33, isolated from 1 month-old fish sauce, was purified to electrophoretic homogeneity, using hydrophobic interaction chromatography and hydroxyapatite with purification fold of 2.5 and 7% yield. The anomalous molecular weight (MW) of 19 kDa was obtained from SDS–PAGE, whereas a MW of 33.7 kDa was determined by MALDI-TOF. Optimum conditions for catalytic activity were 55 °C and pH 7.5. The proteinase was strongly inhibited by phenylmethanesulfonyl fluoride (PMSF) and preferentially hydrolysed Suc-Ala-Ala-Pro-Phe-AMC, indicating a serine proteinase with subtilisin-like characteristics. K m and k cat of the purified proteinase were 27 μM and 12 s −1 , respectively. Proteinase activity, toward both synthetic and anchovy substrates, increased with NaCl up to 25%. The proteinase exhibited high stability in both the absence and presence of NaCl up to 25%. Approximately 2.5-fold increase in activity was observed in the presence of divalent cations, including Ca 2+ , Mg 2+ and Sr 2+ at 100 mM. MALDI-TOF MS and LC–ESI-MS/MS analyses, as well as N-terminal sequences, revealed that the purified enzyme did not match microbial proteinases in the database, indicating it to be a novel proteinase.
- Published
- 2010
20. Identification of glutaminyl sites on β-lactoglobulin for threadfin bream liver and microbial transglutaminase activity by MALDI-TOF mass spectrometry
- Author
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Jirawat Yongsawatdigul, Bung-Orn Hemung, and Eunice C.Y. Li-Chan
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chemistry.chemical_classification ,Chromatography ,biology ,Tissue transglutaminase ,General Medicine ,Mass spectrometry ,biology.organism_classification ,Trypsin ,Analytical Chemistry ,Amino acid ,Matrix-assisted laser desorption/ionization ,Biochemistry ,chemistry ,Threadfin bream ,medicine ,biology.protein ,Time-of-flight mass spectrometry ,Beta-lactoglobulin ,Food Science ,medicine.drug - Abstract
The cross-linking of β-lactoglobulin (BLG) was efficiently catalysed by microbial transglutaminase (MTG) but not by fish (threadfin bream) liver transglutaminase (FTG). BLG cross-linking was inhibited by 2 mM 5-(biotinamido) pentylamine (BPNH2) and MTG incorporated BPNH2 into BLG ∼5 times more than was FTG. The glutaminyl sites for the incorporation of BPNH2 into BLG by FTG and MTG were identified using matrix-assisted laser desorption/ionisation-time of flight mass spectrometry (MALDI-TOF MS). MALDI-TOF MS analyses showed that MTG and FTG incorporated 4 and 1 residues of BPNH2 per molecule of BLG, respectively. The BPNH2-tagged BLG was digested by trypsin and BPNH2-tagged peptides were selectively purified by avidin-affinity chromatography. Amino acid sequences of BPNH2-tagged peptides were identified by comparing their MALDI-TOF mass spectra with the theoretical mass profiles from the MASCOT database. The BPNH2-modification sites catalysed by MTG were glutamine (Q)13, Q68, Q15 or Q20, Q155 or Q159, whilst FTG only incorporated BPNH2 into BLG at Q68. The different reactivities between FTG and MTG might be due to the different accessibilities of these TGases to the Q residues as well as to differences in substrate specificities.
- Published
- 2009
21. Chemical and biochemical changes of hybrid catfish fillet stored at 4°C and its gel properties
- Author
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Kasem Nantachai, Channarong Chomnawang, Somjintana Tungkawachara, Supawan Thawornchinsombut, and Jirawat Yongsawatdigul
- Subjects
Clarias gariepinus ,biology ,Fish fillet ,General Medicine ,Anatomy ,biology.organism_classification ,Age and sex ,Clarias ,Analytical Chemistry ,Atpase activity ,Food science ,Fillet (mechanics) ,Food Science ,Catfish ,Total protein - Abstract
Chemical and biochemical changes of aquacultured hybrid catfish fillet ( Clarias macrocephalus × Clarias gariepinus ) and its gel-forming ability as affected by age and sex of fish along with storage time were investigated. Fillets were stored at 4 °C for 0, 3, 6, 9, 12 and 15 days. There was no significant effect of sex and age of fish as well as storage time on fat, moisture and ash contents ( P > 0.05). The total protein, water soluble protein, and salt soluble protein contents of the fillets significantly decreased with storage time ( P P 2+ -ATPase activity and gel properties were observed as storage time increased. However, there was no significant effect of either sex or age of fish on textural properties of gel ( P > 0.05). Hybrid catfish fillet stored at 4 °C should be processed within 6 days.
- Published
- 2007
22. Partial purification and characterization of trypsin-like proteinases in Indian anchovy (Stolephorus spp.)
- Author
-
Nongnuch Raksakulthai, Patcharin Siringan, and Jirawat Yongsawatdigul
- Subjects
Ammonium sulfate ,Chromatography ,biology ,Kunitz STI protease inhibitor ,Indian anchovy ,Leupeptin ,Size-exclusion chromatography ,General Medicine ,biology.organism_classification ,Trypsin ,Analytical Chemistry ,chemistry.chemical_compound ,chemistry ,Stolephorus ,medicine ,Ammonium sulfate precipitation ,Food Science ,medicine.drug - Abstract
Four fractions (P111, P21, P31, and P4) of proteinases were obtained from various purification steps including heat treatment (60 °C, 10 min), 30–60% ammonium sulfate precipitation, anion exchange, hydrophobic interaction, and gel filtration chromatography. Optimal temperature and pH of all fractions were 50–60 °C and 8.5, respectively. All partially purified proteinases preferably hydrolyzed substrates containing Arg at the P1 position. All proteinases were inhibited by soybean trypsin inhibitor, leupeptin, and N-tosyl- l -lysine chloromethyl ketone. Partially purified proteinases were stable at 35 °C up to 12 h. However, their activity decreased about 40% when incubated at the optimal temperature (50–55 °C) for 2 h. Only P111 was stable at its optimal temperature (60 °C) up to 12 h. Molecular weight (MW) of P111, P21, and P31 was estimated to be 27, 33, 37, 43, 48, 55, 60, and 65 kDa, while MW of P4 was 39 kDa based on activity staining. All partially purified proteinases hydrolyzed washed anchovy mince at 4.0 M NaCl, pH 8.5, at 35 °C and at their optimal temperatures (50–60 °C).
- Published
- 2007
23. Autolytic activity and biochemical characteristics of endogenous proteinases in Indian anchovy (Stolephorus indicus)
- Author
-
Jirawat Yongsawatdigul, Patcharin Siringan, and Nongnuch Raksakulthai
- Subjects
chemistry.chemical_classification ,Chromatography ,biology ,Kunitz STI protease inhibitor ,Indian anchovy ,Leupeptin ,General Medicine ,biology.organism_classification ,Trypsin ,Analytical Chemistry ,chemistry.chemical_compound ,Enzyme ,chemistry ,Stolephorus ,Casein ,medicine ,PMSF ,Food Science ,medicine.drug - Abstract
Maximum autolytic activity of Indian anchovy ( Stolephorus indicus ) was found at 60 °C. Autolytic activity decreased with increased NaCl concentration. Remaining autolytic activity at 25% NaCl (w/w) was 52%. Crude proteinase extracts exhibited the highest activity at 60 °C, using either casein or acid-denatured hemoglobin (dHb) as a substrate. Optimal pH of crude extracts was found at 8.5 for casein and 9.5 for dHb. Activity of crude extract decreased >50% when NaCl concentration was greater than 0.1 M. Crude extract was stable for up to 8 h at 4, 30, and 60 °C. Crude proteinase hydrolyzed several synthetic substrates of trypsin, including Boc-Asp(oBzl)-Pro-Arg-MCA, Boc-Val-Leu-Lys-MCA, and Boc-Gln-Ala-Arg-MCA. Soybean trypsin inhibitor (SBTI), leupeptin, phenylmethanesulfonyl fluoride (PMSF), and N -tosyl- l -lysine chloromethyl ketone (TLCK) inhibited activities of proteinase, indicating trypsin-like characteristics. Molecular weight of proteinases exhibiting caseinolytic activity at 4.0 M NaCl were estimated to be 63, 53, 46, 40, 35, and 31 kDa, using electrophoresis activity staining.
- Published
- 2006
24. Antioxidant activities and antiproliferative activity of Thai purple rice cooked by various methods on human colon cancer cells
- Author
-
Steven J. Schwartz, Rassarin Chatthongpisut, and Jirawat Yongsawatdigul
- Subjects
Antioxidant ,medicine.medical_treatment ,Microwave oven ,Antineoplastic Agents ,Cell Growth Processes ,Protocatechuic acid ,Antioxidants ,Analytical Chemistry ,Ferulic acid ,Anthocyanins ,chemistry.chemical_compound ,Phenols ,Cell Line, Tumor ,medicine ,Vanillic acid ,Hydroxybenzoates ,Humans ,Food science ,Cooking ,IC50 ,Chemistry ,Plant Extracts ,food and beverages ,Oryza ,General Medicine ,Sterilization (microbiology) ,Biochemistry ,Caco-2 ,Colonic Neoplasms ,Caco-2 Cells ,Food Science - Abstract
The changes in anthocyanins, phenolic compounds, and antioxidant activities of Thai purple rice cooked by various cooking devices, including an electric rice cooker, an autoclave and a microwave oven, were investigated. In raw rice, cyanidin-3-glucoside (cy-3-glu) and peonidin-3-glucoside (pn-3-glu) are predominant anthocyanins, whereas protocatechuic acid (PCA) and vanillic acid (VA) are major free phenolic acids, and ferulic acid (FA) and VA are major bound phenolic acids. The microwave cooking method resulted in a marked loss of phenolics, anthocyanins and antioxidant activities (p
- Published
- 2014
25. Purification and characterization of transglutaminase from Tropical tilapia ()
- Author
-
Jirawat Yongsawatdigul and Anulak Worratao
- Subjects
food.ingredient ,Chromatography ,integumentary system ,biology ,Ethylenediaminetetraacetic acid ,Tilapia ,General Medicine ,biology.organism_classification ,Dithiothreitol ,Analytical Chemistry ,chemistry.chemical_compound ,Oreochromis ,food ,Isoelectric point ,Biochemistry ,chemistry ,Iodoacetamide ,Sodium dodecyl sulfate ,human activities ,Polyacrylamide gel electrophoresis ,Food Science - Abstract
Transglutaminase (TGase) from Tropical tilapia (Oreochromis niloticus) was purified to electrophoretic homogeneity using successive chromatographies of DEAE-Sephacel, Sephacryl S-4 HR and HiTrap Heparin with a yield and purification-fold of 12.9% and 69.8, respectively. The molecular weight (MW) of the purified tilapia TGase was estimated to be 85 kDa using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The isoelectric point (pI) of tilapia TGase was 6.53. Optimal temperature and optimal pH of tilapia TGase were 37–50 °C and 7.5, respectively. Optimal concentrations of CaCl2 and dithiothreitol (DTT) were at 1.25 and 5 mM, respectively. The activity of TGase towards monodansylcadaverine (MDC) decreased as the NaCl concentration increased. Chelating agents, ethylenediaminetetraacetic acid (EDTA) and ethylene glycol-O,O′-bis(2-aminoethyl)-N,N,N′,N′-tetraacetic acid (EGTA), inhibited TGase activity. Tilapia TGase was strongly inactivated by ρ-chloromercuribenzoic acid (PCMB), N-ethylmaleimide (NEM), iodoacetamide (IAA), Cu2+, and Zn2+, suggesting a thiol group at the active site.
- Published
- 2005
26. Inhibition of autolytic activity of lizardfish surimi by proteinase inhibitors
- Author
-
Jirawat Yongsawatdigul and Penprapha Piyadhammaviboon
- Subjects
chemistry.chemical_classification ,Whey protein ,Oligopeptide ,Autolysis (biology) ,Chromatography ,medicine.diagnostic_test ,Proteolysis ,General Medicine ,Analytical Chemistry ,Serine ,Hydrolysis ,Enzyme ,chemistry ,medicine ,Food Science ,Egg white - Abstract
Optimum autolytic activities of lizardfish ( Saurida tumbil ) mince and surimi were at pH 6 and 7, respectively, with optimum temperature at 65 °C. Autolysis of surimi was mainly inhibited by phenylmethanesulfonyl fluoride and p -tosyl- l -phenylalanyl-chloromethylketone, indicating the involvement of myofibrillar-associated serine proteinase. Myosin heavy chain (MHC) and tropomyosin were preferentially hydrolyzed, resulting in poor textural properties. Based on TCA-soluble oligopeptide assay, egg white powder (EW) and whey protein concentrate (WPC) showed 77% and 96% inhibition, respectively. However, a significant loss of MHC was found. At any pre-incubation condition (25 °C/4 h, 40 °C/1 h and 65 °C/1 h), EW improved gel-forming ability of lizardfish surimi to a greater extent than WPC. Addition of 1% EW and pre-incubation at 25 °C resulted in an increase of higher molecular weight cross-linked proteins, corresponding to a twofold increase in the breaking force.
- Published
- 2004
27. Detergent-Stable Salt-Activated Proteinases from Virgibacillus halodenitrificans SK1-3-7 Isolated from Fish Sauce Fermentation
- Author
-
Jirawat Yongsawatdigul, Aungkawipa Montriwong, and Sureelak Rodtong
- Subjects
Hot Temperature ,Detergents ,Bioengineering ,Sodium Chloride ,Applied Microbiology and Biotechnology ,Biochemistry ,chemistry.chemical_compound ,Hydrolysis ,Bacterial Proteins ,Virgibacillus ,Enzyme Stability ,Fish Products ,Molecular Biology ,Laundry detergent ,chemistry.chemical_classification ,Chromatography ,biology ,Chemistry ,Butanol ,General Medicine ,biology.organism_classification ,Enzyme ,Biocatalysis ,Fermentation ,PMSF ,Biotechnology ,Peptide Hydrolases - Abstract
The NaCl-activated and detergent-stable proteinases from Virgibacillus halodenitrificans SK1-3-7 isolated from fish sauce fermentation were purified and characterized. The enzymes with molecular masses of 20 and 36 kDa showed caseinolytic activity on a zymogram. Optimum azocaseinolytic activity was at 60 °C and pH 9. The proteolytic activity increased in the presence of 10 mM CaCl2 and 0.5 M NaCl and showed high stability at 0–2 M NaCl. The enzymes were stable at pH 4–10 and 10–50 °C. The enzymes preferably hydrolyzed Suc-Ala-Ala-Pro-Phe-pNA and were completely inhibited by phenylmethanesulfonyl fluoride (PMSF), showing subtilisin-like characteristics. Activity and stability remained high in the presence of H2O2 and various surfactants. The enzymes exhibited high stability (>95 %) in various organic solvents (DMSO, butanol, ethanol, 2-propanol, and acetonitrile) at concentration of 50 %. The V. halodenitrificans SK1-3–7 proteinases showed potential as a biocatalyst in aqueous-organic solvent systems and as an additive in laundry detergent.
- Published
- 2014
28. Proteinase-producing halophilic lactic acid bacteria isolated from fish sauce fermentation and their ability to produce volatile compounds
- Author
-
Jirawat Yongsawatdigul, Sureelak Rodtong, Natteewan Udomsil, and Somboon Tanasupawat
- Subjects
food.ingredient ,Gram-positive bacteria ,Molecular Sequence Data ,Enterococcaceae ,Sodium Chloride ,Microbiology ,chemistry.chemical_compound ,food ,Bacterial Proteins ,Tetragenococcus halophilus ,Fish Products ,Animals ,Lactic Acid ,Tetragenococcus ,Phylogeny ,Volatile Organic Compounds ,biology ,Fishes ,General Medicine ,biology.organism_classification ,Fish products ,16S ribosomal RNA ,Lactic acid ,chemistry ,Fermentation ,Bacteria ,Food Science ,Peptide Hydrolases - Abstract
Halophilic lactic acid bacteria were isolated from fish sauce mashes fermented at 1 to 12 months. Seven out of sixty-four isolates were selected according to their proteolytic activity and growth at 25% NaCl for characterization and investigation of volatile compound production. All selected isolates were Gram-positive cocci with pairs/tetrads and grew at 0-25% NaCl, pH 4.5-9.0. Results of 16S rRNA gene sequence analysis showed 99% homology to Tetragenococcus halophilus ATCC 33315. The restriction fragment length polymorphism (RFLP) patterns of all isolates were also similar to those of T. halophilus ATCC 33315. These isolates were, thus, identified as T. halophilus. All isolates hydrolyzed fish protein in the medium containing 25% NaCl. Intracellular aminopeptidase of 7 isolates exhibited the highest activity of 2.85-3.67 U/ml toward Ala-p-nitroanilide (Ala-pNA). T.halophilus strains MS33 and M11 showed the highest alanyl aminopeptidase activity (P
- Published
- 2010
29. Thermal stability of fish natural actomyosin affects reactivity to cross-linking by microbial and fish transglutaminases
- Author
-
Bung-Orn Hemung, Eunice C.Y. Li-Chan, and Jirawat Yongsawatdigul
- Subjects
Circular dichroism ,animal structures ,biology ,Tissue transglutaminase ,Chemistry ,food and beverages ,General Medicine ,biology.organism_classification ,Whiting ,Analytical Chemistry ,Differential scanning calorimetry ,Biochemistry ,Threadfin bream ,biology.protein ,Biophysics ,Reactivity (chemistry) ,Thermal stability ,Solubility ,health care economics and organizations ,Food Science - Abstract
Natural actomyosin (NAM) from Pacific whiting (PW) showed thermal transition temperatures by circular dichroism at 31.8 and 43.1°C, which were lower than those of threadfin bream (TB) NAM, 35.0 and 49.3°C. Endothermic transitions of PW-NAM by differential scanning calorimetry were at 31.8, 42.1 and 75.3°C, compared to 36.1, 50.9 and 78.4°C for TB-NAM. Based on surface hydrophobicity, α-helical content, and solubility, PW-NAM unfolded to a greater extent than did TB-NAM when incubated at 25°C for 4h and 40°C for 2h, suggesting its lower thermal stability. Transglutaminase generally catalyzed more extensive cross-linking of PW-myosin heavy chain (MHC) than TB-MHC, and the MHC cross-linking mediated by microbial transglutaminase (MTG) was greater than by fish transglutaminase (FTG). Textural properties of PW-NAM gels increased approximately 3.6-6.1-fold and 1.3-1.5-fold in the presence of MTG and FTG, respectively.
- Published
- 2007
30. Characterization of NaCl-activated proteinases from moderate halophile isolated from fish sauce fermentation
- Author
-
Sornchai Sinsuwan, Sureelak Rodtong, and Jirawat Yongsawatdigul
- Subjects
Chemistry ,%22">Fish ,Bioengineering ,Fermentation ,General Medicine ,Food science ,Molecular Biology ,Halophile ,Biotechnology - Published
- 2009
31. Characterization of Virgibacillus sp. SK33 cell-bound proteinases and its application as a starter culture for fish sauce fermentation
- Author
-
Jirawat Yongsawatdigul, Siriwan Nawong, Sureelak Rodtong, Nongnuch Raksakulthai, and Sornchai Sinsuwan
- Subjects
Starter ,Chemistry ,Virgibacillus sp ,%22">Fish ,Bioengineering ,Fermentation ,General Medicine ,Food science ,Applied Microbiology and Biotechnology ,Biotechnology ,Microbiology - Published
- 2008
32. Biogenic amines degradation by moderate halophile, Brevibacillus sp. SK35
- Author
-
Aungkawipa Montriwong, Jirawat Yongsawatdigul, Sornchai Sinsuwan, and Sureelak Rodtong
- Subjects
chemistry.chemical_classification ,Brevibacillus ,biology ,Bioengineering ,General Medicine ,biology.organism_classification ,Applied Microbiology and Biotechnology ,Halophile ,Microbiology ,chemistry ,Biogenic amine ,Brevibacillus sp ,Degradation (geology) ,Food science ,Biotechnology - Published
- 2010
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