Our work will allow the design of biocatalysts for ligninolytic enzyme engineering and for efficient biocatalytic degradation of plant biomass in lignocellulose biorefineries.In this study, curdlan-based and calcium ion (Ca2+)-chelated magnetic microspheres (CCMM) were prepared for protein purification and oriented immobilization. Additional purification steps before immobilization were not required. CCMM samples were produced by reverse embedding of Fe3O4 nanoparticles with curdlan and chelated with Ca2+ in the presence of iminodiacetic acid. The β-xylanase XynII from Trichoderma reesei QM6a was used to investigate the efficiency of CCMM preparation. The resulting CCMM-XynII was found to be very stable, showing 82 % and 60 % of initial activities after storage for 35 days and after being assayed ten times, respectively. In addition, the CCMM-XynII showed higher stabilities in the presence of organic solvents and multiple chemicals than the free XynII, suggesting that the CCMM-XynII could be efficient for applications requiring the presence of organic solvents. In addition, CCMM may be more suitable than commercially available Ni-NTA for purification of proteins intolerant of Ni2+.Although lignocellulose is the most abundant and renewable natural resource for biofuel production, its use remains under exploration because of its highly recalcitrant structure. Its deconstruction into sugar monomers is mainly driven by carbohydrate-active enzymes (CAZymes). To develop highly efficient and fast strategies to discover biomass-degrading enzymes for biorefinery applications, an enrichment process combined with integrative omics approaches was used to identify new CAZymes. The lignocellulolytic-enriched mangrove microbial community (LignoManG) established on sugarcane bagasse (SB) was enriched with lignocellulolytic bacteria and fungi such as Proteobacteria, Bacteroidetes, Basidiomycota, and Ascomycota. These microbial communities were able to degrade up to 55 % of the total SB, indicating the production of lignocellulolytic enzymes. Metagenomic analysis revealed that the LignoManG harbors 18.042 CAZyme sequences such as of cellulases, hemicellulases, carbohydrate esterases, and lytic polysaccharide monooxygenase. Similarly, our metaproteomic analysis depicted several enzymes from distinct families of different CAZy families. Based on the LignoManG data, a xylanase (coldXynZ) was selected, amplified, cloned, expressed, and biochemically characterized. The enzyme displayed psicrofilic properties, with the highest activity at 15 °C, retaining 77 % of its activity when incubated at 0 °C. Moreover, molecular modeling in silico indicated that coldXynZ is composed of a TIM barrel, which is a typical folding found in the GH10 family, and displayed similar structural features related to cold-adapted enzymes. Collectively, the data generated in this study represent a valuable resource for lignocellulolytic enzymes with potential biotechnological applications.In this study, a novel one-step enzymatic acylation was developed for the synthesis of hydrophobic arbutin ester, by using supercritical carbon dioxide (SC-CO2) as the reaction solvent. Immobilized Novozym 435 from Candida antarctica was identified as the best biocatalyst for producing arbutin palmitate through transesterification between arbutin and palmitic acid ethyl ester in SC-CO2. A transesterification yield of 85.21 % was obtained in batch operation using palmitic acid ethyl ester as the acyl donor, hexane/propylene glycol as the co-solvent and Novozym 435 as the enzyme at 10 MPa and 60 °C for 20 h in SC-CO2. The yield of arbutin palmitate increased with increasing temperature over the range of 40-60 °C in the current study. Operating at an arbutin/palmitic acid ethyl ester molar ratio of 5.0, the conversion of arbutin decreased, probably due to an inhibitory effect of the high concentration of palmitic acid ethyl ester on the enzyme.  https://www.selleckchem.com/products/hg-9-91-01.html  The 38 % original enzyme activity of Novozym 435 was maintained after being used for 3 cycles (60 h) under optimized conditions.The β-glucosidase derived from microorganisms has attracted worldwide interest for their industrial applications, but studies on β-glucosidases from Oenococcus oeni are rare. In this paper, catalytic mechanism of a novel β-glucosidase BGL0224 of Oenococcus oeni SD-2a was explored for the first time by kinetic parameters determination, fluorescence spectroscopy and quenching mechanism analysis, molecular dynamics simulation. The results indicated that BGL0224 had universal catalytic effect on different types of glycoside substrates, but the catalytic efficiencies were different. Fluorescence quenching analysis results suggested that the quenching processes between BGL0224 and seven kinds of substrates were predominated by the static quenching mechanism. A reasonable three-dimensional model of BGL0224 was obtained using the crystal structure of E.coli BglA as a template. The analysis results of molecular simulation (RMSD, Rg, RMSF and hydrogen bonding) showed that the composite system 'BGL0224-pNPG' was very stable after 40 ns. The catalytic process of BGL0224 acting on 'p-Nitrophenyl β-d-glucopyranoside' conformed to the double displacement mechanism. Two glutamic acid residues 'Glu178 and Glu377' played a vital role in the whole catalytic process. Overall, this study gave specific insights on the catalytic mechanism of BGL0224, which was of great significance for developing its potential applications in food industry.Quorum quenching (QQ) has been proven to be an effective method to reduce MBR membrane biological contamination. In this paper, a novel and efficient QQ-PAC core-shell beads were prepared for mitigating the membrane contamination. The bead was composed of two parts QQ bacteria embedded in the core and PAC in the shell. The microstructure of the bead was observed by scanning electron microscopy (SEM) and the functional groups were revealed by Fourier transform infrared spectroscopy (FTIR). Meanwhile, the mechanical strength, swelling property, penetration property and QQ activity of the core bead, the core shell-without PAC bead and the core shell-with PAC bead were compared. The core shell-with PAC structure improved the adsorption capacity under good mass transfer conditions. Besides, the combined effect of QQ bacteria and PAC enhanced the QQ effect and alleviated the process of MBR membrane biological contamination consequently. Therefore, the QQ-PAC core-shell beads have a potential possibility in MBR membrane fouling control as the immobilization technology of QQ bacteria.