Advances in the bioproduction of d-allulose: A comprehensive review of current status and future prospects

Food Research International, Journal Year: 2025, Volume and Issue: 202, P. 115767 - 115767

Published: Jan. 18, 2025

Language: Английский

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Rational Design of Spontaneous Self-Cyclization Enzymes In Vivo and In Vitro with Improved Thermal Tolerance and Activity

ACS Catalysis, Journal Year: 2024, Volume and Issue: 14(7), P. 5469 - 5480

Published: March 28, 2024

Enzymes have selectivity, require mild catalytic conditions, and are important cornerstones in many industrial processes. Protein self-cyclization has opened up the possibility of preserving fragile enzymes during long-term high-temperature catalysis. However, mechanism for improvement thermal tolerance not been elucidated, severely limiting their applications. Herein, we provide a strategy rational design fusion proteins based on structural analysis to obtain cyclized with improved properties. First, constructed that preferentially translated SpyCatcher (CBT) or SpyTag (TBC), both which could form stable single significantly tolerance. Especially, half-life TBC obtained by modifying N-terminal at 40 °C was 10.83 times wild enzymes. Structural revealed terminus protein, SpyCatcher, folded into conformation adversely affected stability. In addition, structure pocket orientation residues CBT were different from those wild-type enzymes, led decrease activity. These conclusions confirmed when another enzyme, sucrose phosphorylase, cyclized. Finally, glucosidase also superior strain preparation ginsenoside F1 high titers as whole-cell catalyst extended use. conclusion, demonstrated first time conjugated long oligopeptide activity stability It necessary translate units less steric hindrance reduce impact protein structure. The provides simple effective modification poor tolerance, providing considerable prospects biosynthesis vivo vitro.

Language: Английский

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Green biotechnological synthesis of rare sugars/alcohols: D-allulose, Allitol, D-tagatose, L-xylulose, l-ribose

Food Research International, Journal Year: 2025, Volume and Issue: 206, P. 116058 - 116058

Published: Feb. 25, 2025

Language: Английский

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Recent advances in discovery, protein engineering, and heterologous production of ketose 3-epimerase for rare sugar biosynthesis

Trends in Food Science & Technology, Journal Year: 2024, Volume and Issue: 149, P. 104552 - 104552

Published: May 20, 2024

Language: Английский

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Advances in the biosynthesis of D-allulose

World Journal of Microbiology and Biotechnology, Journal Year: 2024, Volume and Issue: 40(12)

Published: Nov. 2, 2024

Language: Английский

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Advancements in the Heterologous Expression of Sucrose Phosphorylase and Its Molecular Modification for the Synthesis of Glycosylated Products

Molecules, Journal Year: 2024, Volume and Issue: 29(17), P. 4086 - 4086

Published: Aug. 28, 2024

Sucrose phosphorylase (SPase), a member of the glycoside hydrolase GH13 family, possesses ability to catalyze hydrolysis sucrose generate α-glucose-1-phosphate and can also glycosylate diverse substrates, showcasing wide substrate specificity. This enzyme has found extensive utility in fields food, medicine, cosmetics, garnered significant attention as focal point research transglycosylation enzymes. Nevertheless, SPase encounters numerous obstacles industrial settings, including low yield, inadequate thermal stability, mixed regioselectivity, limited activity. In-depth exploration efficient expression strategies molecular modifications based on crystal structure functional information is now critical priority. paper systematically reviews source microorganisms, structure, catalytic mechanism SPase, summarizes heterologous systems hosts vectors, examines application modification progress synthesizing typical glycosylated products. Additionally, it anticipates broad prospects production related fields, laying groundwork for its engineering application.

Language: Английский

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Green directional conversion of food waste into glycerol in a two-step differentiation enzymolysis and facultative fermentation using Saccharomyces cerevisiae: Performance assessment and mechanism

Biomass and Bioenergy, Journal Year: 2024, Volume and Issue: 189, P. 107360 - 107360

Published: Aug. 31, 2024

Language: Английский

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Semi-Rational Engineering of Aldoxime Dehydratase for Conducting a Chemoenzymatic Sequence to Prepare 2-Furonitrile from Xylose

ACS Sustainable Resource Management, Journal Year: 2024, Volume and Issue: 1(10), P. 2214 - 2224

Published: Oct. 15, 2024

Exploiting efficient methods for converting biomass-based resources into high-value-added chemicals has attracted extensive interest in sustainable development the chemical industry. Here, we have developed a chemoenzymatic sequence synthesizing 2-furonitrile (2-FN) from xylose, biobased five-carbon monosaccharide derived agricultural waste. Firstly, 1,2-dichloroethane (DCE)/H2O biphasic system (1:1, v/v) was adopted to produce 2-furaldehyde oxime (2-FOx) xylose by integrating two steps of dehydration and oximation one-pot using temporal compartmentalization strategy, resulting yield 2-FOx over 78%. Secondly, catalytic efficiency aldoxime dehydratase Pseudomonas putida F1 (OxdF1) significantly improved engineering substrate access tunnel distal residue. The activity an optimal mutant L318I–N266S reached 3.94 U·mg–1 towards 2-FOx, approximately 6 times higher than that wild-type OxdF1 (0.65 U·mg–1). Consequently, 2-FN prepared 400 mL reaction mixture at room temperature continuous feeding strategy. After 1.5 h, 100 mM completely converted with space-time 6.2 g·L–1·h–1. process proposed alternative strategy materials under mild conditions without highly toxic cyanide.

Language: Английский

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Fabricating compartmented nanoreactor via protein self-regulated biomimetic mineralization for multienzyme immobilization

Advanced Composites and Hybrid Materials, Journal Year: 2024, Volume and Issue: 7(6)

Published: Nov. 18, 2024

Language: Английский

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