Efficient expression of OUC-Sb-lip2 in Yarrowia lipolytica and its comprehensive utilization in the enrichment of DHA and EPA from fish oil.

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.

Characterization of a GH20 β--Acetylhexosaminidase from Suitable to Synthesize Lacto--triose II.

β--Acetylhexosaminidases have attracted much attention in the enzymatic synthesis of lacto--triose II (LNT2) as a backbone precursor of human milk oligosaccharides (HMOs). In this study, a novel glycoside hydrolase (GH) 20 family β--acetylhexosaminidase, FlaNag2353, from was biochemically characterized and applied to synthesize LNT2. FlaNag2353 displayed optimal activity to -nitrophenyl -acetyl-β-d-glucosaminide (NP-GlcNAc) at 40 °C and pH 8.

Structure-based mining of a chitosanase with distinctive degradation mode and product specificity.

Chitosan derivates with varying degrees of polymerization (DP) have attracted great concern due to their excellent biological activities. Increasing the abundance of chitosanases with different degradation modes contributes to revealing their catalytic mechanisms and facilitating the production of chitosan derivates. However, the identification of endo-chitosanases capable of producing chitobiose and D-glucosamine (GlcN) from chitosan substrates has remained elusive.

Chimeric versus isolated proteins: Biochemical characterization of the NADP-dependent formate dehydrogenase from Pseudomonas sp. 101 fused with the Baeyer-Villiger monooxygenase from Thermobifida fusca.

The expression of multifunctional proteins can facilitate the setup of a biotechnology process that requires multiple functions absolved by different proteins. Herein the functional and conformational characterization of a formate dehydrogenase-monooxygenase chimera enzyme is presented. The fused enzyme (FDH-PAMO) was prepared by linking the C-terminus of the mutant NADP-dependent formate dehydrogenase from Pseudomonas sp.

Expanding the application range of the ‑carrageenase OUC-FaKC16A when preparing oligosaccharides from -carrageenan and furcellaran.

Unlabelled: Carrageenan oligosaccharides are important products that have demonstrated numerous bioactivities useful in the food, medicine, and cosmetics industries. However, the specific structure-function relationships of carrageenan oligosaccharides are not clearly described due to the deficiency of high specific carrageenases. Here, a truncated mutant OUC-FaKC16Q based on the reported -neocarratetrose (N4)-producing -carrageenase OUC-FaKC16A from was constructed and further studied.