DOI: 10.12187/2025.06.001
Research progress on catalytic regulation of γ-glutamyl transpeptidase and its application in food processing
ZONG Wei
GAO Wenyu
LI Shunfeng
DU Xinxin
ZHANG Lihua
Abstract:γ-glutamyl transpeptidase(GGT,EC 2.3.2.2)is a pivotal enzyme that catalyzes γ-glutamyl group transfer and hydrolysis reactions,playing a critical role in bioactive substance synthesis and food flavor modulation.Against the backdrop of national salt reduction policies,GGT enhances the bioavailability of natural umami compounds,offering innovative solutions for"salt reduction without compromising flavor"in the food industry.This review systematically examines GGT's sources,catalytic mechanisms,preparation methods,enzymatic characteristics,molecular modification strategies,and immobilization techniques,along with its current applications in food processing.GGT exhibits broad distribution across animal,plant,and microbial sources.Its catalytic mechanism adheres to the"ping-pong"model,generating γ-glutamyl peptides via acylation-deacylation reactions that synergistically enhance saltiness perception and umami intensity.Molecular modification and immobilization techniques significantly improve GGT's catalytic efficiency,stability(thermal and pH stability),and recyclability.In food processing,GGT has been successfully applied in soy sauce umami enhancement,flavor compound synthesis,and low-salt meat product flavor optimization.However,large-scale implementation faces challenges including low microbial enzyme production yields and high immobilization carrier costs.Future studies should focus on:Exploring GGT's application potential,engineering high-yield microbial strains and developing efficient immobilized catalysts,and establishing metabolomics-based flavor modulation models to fully realize GGT's potential in sustainable food processing and quality enhancement.
Keywords:γ-glutamyl transpeptidasecatalytic mechanismmolecular modificationimmobilization technologyflavor
Publication Date:2025-12-15
Online Publishing Date:2025-12-22(First online date of this platform, not the publication date of the document)
Pages:12( 1-12 )
