Identification of a novel cellobiose 2-epimerase from Acidobacteriota bacterium and its application for in-situ milk catalysis

Frontiers in Microbiology, Journal Year: 2025, Volume and Issue: 16

Published: April 4, 2025

Introduction Cellobiose 2-epimerase (CE) catalyzes the interconversion of glucosyl and mannosyl groups at reducing end β -1,4-linked disaccharides. This enzyme is pivotal for converting lactose into prebiotics like epilactose, offering a potential solution lactose-intolerant-friendly dairy products. However, current CEs are hindered by pH thermal instability in milk processing, as their neutral-to-alkaline optima clash with milk’s mildly acidic conditions (pH 6.5–6.7), poor thermolability requires costly post-processing removal. Methods We identified novel CE from acidophilic Acidobacteriota bacterium (Acba-CE) characterized its properties. Its enzymatic activity was assessed under varying temperature conditions, including milk-processing environments. Results Acba-CE exhibits an optimum (6.0), retaining 95% (6.5). Notably, it undergoes rapid inactivation pasteurization temperatures, enabling complete deactivation during standard without additional steps. In systems, achieves 28.5% lactose-to-epilactose conversion refrigeration temperatures (10°C), demonstrating strong cold adaptability. Discussion To our knowledge, this first reported phylum, combining low-temperature represents breakthrough situ modification, eliminating key bottlenecks processing next-generation functional production.

Language: Английский

Enhancement of isomerization activity and thermostability of cellobiose 2-epimerase from Caldicellulosiruptor saccharolyticus using semi-rational design

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: unknown, P. 144061 - 144061

Published: May 1, 2025

Language: Английский