Search

λ-carrageenan oligosaccharides can be widely applied in the food, pharmaceutical, medicine and cosmetic industries due to their abundant bioactivities, and they are important products for the high-value utilization of λ-carrageenan. However, oligosaccharides with different degrees of polymerization have different properties, and the final products of λ-carrageenase reported so far are mainly λ-neocarrabiose, λ-neocarratetraose and λ-neocarrahexaose without longer-chain oligosaccharides. Further research is consequently required. Herein, a mutant λ-carrageenase was constructed by deleting the pyrroloquinoline quinone-like domain of OUC-CglA derived from Maribacter vaceletii. Interestingly, it was discovered that the majority of final products of the mutant OUC-CglA-DPQQ were long-chain oligosaccharides with a polymerization degree of 10–20, which underwent significant changes compared to that of OUC-CglA. Additionally, without the pyrroloquinoline quinone-like domain, fewer inclusion bodies were produced throughout the expression process, and the yield of the λ-carrageenase increased about five-fold. However, compared to its parental enzyme, significant changes were made to its enzymatic properties. Its optimal temperature and pH were 15 °C and pH 7.0, and its specific activity was 51.59 U/mg. The stability of the enzyme decreased. Thus, it was found that the deleting domain was related to the formation of inclusion bodies, the stability of the enzyme, the activity of the enzyme and the composition of the products. [ABSTRACT FROM AUTHOR]

Phospholipids are distinctive, adaptable molecules that are crucial to numerous biological systems. Additionally, their various architectures and amphiphilic characteristics support their unrivaled crucial functions in scientific and industrial applications. Due to their enormous potential for use in the fields of medicine, food, cosmetics, and health, structured phospholipids, which are modified phospholipids, have garnered increased attention. Traditional extraction methods, however, are pricy, resource-intensive, and low-yielding. The process of enzyme-catalyzed conversion is effective for producing several types of structured phospholipase. However, most frequently employed catalytic procedures involve biphasic systems with organic solvents, which have a relatively large mass transfer resistance and are susceptible to solvent residues and environmental effects due to the hydrophobic nature of phospholipids. Therefore, the adoption of innovative, successful, and environmentally friendly enzyme-catalyzed conversion systems provides a new development route in the field of structured phospholipids processing. Several innovative catalytic reaction systems are discussed in this mini-review, including aqueous-solid system, mixed micelle system, water-in-oil microemulsion system, Pickering emulsion system, novel solvent system, three-liquid-phase system, and supercritical carbon dioxide solvent system. However, there is still a glaring need for a thorough examination of these systems for the enzymatic synthesis of structural phospholipids. In terms of the materials utilized, applicability, benefits and drawbacks, and comparative effectiveness of each system, this research establishes further conditions for the system's selection. To create more effective biocatalytic processes, it is still important to build green biocatalytic processes with improved performance. Key points: • The latest catalytic systems of phospholipase D are thoroughly summarized. • The various systems are contrasted, and their traits are enumerated. • Different catalytic systems' areas of applicability and limitations are discussed. [ABSTRACT FROM AUTHOR]

The conventional agar extraction method has drawbacks such as high energy consumption, low yield, poor quality, and possible residual harmful factors, which greatly limit its application in high-end fields such as biomedicine and high-end materials. This work explored a new freezing-thawing-high-temperature coupling technique for agar extraction. It increased the yield and the strength of agar by 10.6 % and 13.7 %, respectively, as compared to direct high-temperature extraction of agar (HA). The greater molecular weight and lower sulfate content of agar obtained from freeze-thaw cycles combined with high temperature extraction (FA) may be attributed to the desulfurization effect caused by freeze-thaw cycles and the preservation of the molecular chain structure. The reduction in sulfate content decreases the steric hindrance resistance of the polysaccharide chains, enhances their interactions, and promotes the regularity and density of the agar structure, while also improving its water retention and thermal stability. In conclusion, this research can offer a theoretical basis and guidance for the eco-friendly extraction of agar with improved agar characteristics and expended its applications., Competing Interests: Declaration of competing interest The authors declare no competing interests., (Copyright © 2024 Elsevier B.V. All rights reserved.)

Lipases are widely used in the modification of functional lipids, particularly in the enrichment of docosahexaenoic acid (DHA) and eicosapentaenoic acid (EPA). In this study, a lipase named OUC-Sb-lip2 was expressed in Yarrowia lipolytica, achieving a promising enzyme activity of 472.6 U/mL by optimizing the culture medium, notably through olive oil supplementation. A significant proportion (58.8%) of the lipase activity was located in the cells, whereas 41.2% was secreted into the supernatant. Both whole-cell and immobilized OUC-Sb-lip2 were used to enrich DHA and EPA from fish oil. The whole-cell approach increased the DHA and EPA contents to 2.59 and 2.55 times that of the original oil, respectively. Similarly, the immobilized OUC-Sb-lip2 resulted in a 2.00-fold increase in DHA and an 1.99-fold increase in EPA after a 6-h hydrolysis period. Whole cell and the immobilized OUC-Sb-lip2 retained 48.7% and 52.7% of their activity after six cycles of reuse, respectively., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

The use of convertible immobilized enzyme carriers is crucial for biphasic catalytic reactions conducted in Pickering emulsions. However, the intense mechanical forces during the conversion process lead to enzyme leakage, affecting the stability of the immobilized enzymes. In this study, a CO 2 -responsive switchable Janus (CrSJ) nanoparticle (NP) was developed using silica NP, with one side featuring aldehyde groups and the other side adsorbing N , N -dimethyldodecylamine. A switchable Pickering emulsion catalytic system for biphasic interface reactions was prepared by covalently immobilizing lipase onto the CrSJ NPs. The CO 2 -responsive nature of the CrSJ NPs allowed for rapid conversion of the Pickering emulsion, and covalent immobilization substantially reduced lipase leakage while enhancing the stability of the immobilization during the conversion process. Impressively, after repeated transformations, the Pickering emulsion still maintains its original structure. Following 10 consecutive cycles of esterification and hydrolysis reactions, the immobilized enzyme's activity remains at 77.7 and 79.5% of its initial activity, respectively. The K m of the CrSJ catalytic system showed no significant change compared to the free enzyme, while its V max values were 1.2 and 1.6 times that of the free enzyme in esterification and hydrolysis reactions, respectively.

The whole enzymatic conversion of chitin is a green and promising alternative to current strategies, which are based on lytic polysaccharide monooxygenases (LPMOs) and chitinases. However, the lack of LPMOs with high activity toward α-chitin limits the efficient bioconversion of α-chitin. Herein, we characterized a high chitin-active LPMO from Oceanobacillus sp. J11TS1 ( Os LPMO10A), which could promote the decrystallization of the α-chitin surface. Furthermore, when coupled with Os LPMO10A, the conversion rate of α-chitin to N -acetyl chitobiose [(GlcNAc) 2 ] by three chitinases ( Serratia marcescens , ChiA, -B, and -C) reached 30.86%, which was 2.03-folds that without the addition of Os LPMO10A. Moreover, the results of synergistic reactions indicated that Os LPMO10A and chitinases promoted the degradation of α-chitin each other mainly on the surface. To the best of our knowledge, this study achieved the highest yield of N -acetyl chitooligosaccharides ( N -acetyl COSs) among reported LPMOs-driven bioconversion systems, which could be regarded as a promising candidate for α-chitin bioconversion.