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Two glycoside hydrolase family 1 proteins mediate glycosylated modification at the 5-position of anthocyanin in grape hyacinth.
Int J Biol Macromol
January 2025
College of Landscape Architecture and Art, Northwest A & F University, Yangling, Shaanxi 712100, China; State Key Laboratory of Crop Stress Resistance and High-Efficiency Production, Northwest A & F University, Yangling, Shaanxi 712100, China. Electronic address:
Glycosylation modification of anthocyanins is important as a preceding step to acylation modification. Cyanidin-3-O-(p-coumaroyl)glucoside-5-O-malonylglucoside (Cy3pCG5MaG) is one of the major anthocyanin substances in blue-flowered grape hyacinth, but its 5-position glycosylation is unknown. Here, we identified two glycoside hydrolase family 1 genes, MaAGGT1 and MaAGGT5, which use acyl-glucose as a donor and are involved in the glycosylation modification of anthocyanins in grape hyacinth.
View Article and Find Full Text PDFSubstrate preference triggers metabolic patterns of indigenous microbiome during initial composting stages.
Bioresour Technol
January 2025
Jiangsu Provincial Key Lab of Solid Organic Waste Utilization, Jiangsu Collaborative Innovation Center of Solid Organic Wastes, Nanjing Agricultural University, Nanjing 210095, Jiangsu, PR China. Electronic address:
Composting organic waste is a sustainable recycling method in agricultural systems, yet the microbial preferences for different substrates and their influence on composting efficiency remain underexplored. Here, 210 datasets of published 16S ribosomal DNA amplicon sequences from straw and manure composts worldwide were analyzed, and a database of 278 bacterial isolates was compiled. Substrate-driven microbiome variations were most prominent during the initial composting stages.
View Article and Find Full Text PDFSubstrate-specific responses to mixing conditions in high-solids enzymatic hydrolysis: Insights from microcrystalline cellulose and dilute-acid pretreated corncob.
Int J Biol Macromol
January 2025
Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest, Resources, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, PR China. Electronic address:
This study investigates the mixing effects on the enzymatic hydrolysis of microcrystalline cellulose (MCC) and dilute-acid pretreated corncob substrates under high-solid conditions. Enzymatic hydrolysis experiments were conducted to assess cellulose conversion rates under varying mixing conditions (0, 50, 150, and 250 rpm) and solids loadings (5 %, 15 %, 25 %, and 35 %, w/v), and distinct physicochemical properties of the substrates were characterized. Additionally, the role of mixing conditions and solid loadings on cellulose hydrolysis kinetics and enzyme adsorption on both substrates and lignin were elucidated.
View Article and Find Full Text PDFTargeted Adherence and Enhanced Degradation of Feather Keratins by a Novel Prepeptidase C-Terminal Domain-Fused Keratinase.
J Agric Food Chem
January 2025
College of Light Industry and Food Engineering, Guangxi University, Nanning 530004, People's Republic of China.
Keratinases are valuable enzymes for converting feather keratin waste into bioactive products but often suffer from poor substrate specificity and low catalytic efficiency. This study reported the creating of a novel keratinase with targeted adherence and specific degradation on feather keratins by fusing prepeptidase C-Terminal (PPC) domain. A PPC domain of metalloprotease E423 specifically adsorbed feather keratins by hydrogen bonds and hydrophobic interactions in a time- and temperature-dependent manner.
View Article and Find Full Text PDFSpecific Substrate Activity of Lotus Root Polyphenol Oxidase: Insights from Gaussian-Accelerated Molecular Dynamics and Markov State Models.
Int J Mol Sci
September 2024
Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, School of Life Sciences, Jilin University, Changchun 130012, China.
Polyphenol oxidase (PPO) plays a key role in the enzymatic browning process, and this study employed Gaussian-accelerated molecular dynamics (GaMD) simulations to investigate the catalytic efficiency mechanisms of lotus root PPO with different substrates, including catechin, epicatechin, and chlorogenic acid, as well as the inhibitor oxalic acid. Key findings reveal significant conformational changes in PPO that correlate with its enzymatic activity. Upon substrate binding, the alpha-helix in the Q53-D63 region near the copper ion extends, likely stabilizing the active site and enhancing catalysis.
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