Research Progress of α-L-Arabinofuranosidase from Microorganisms

Abstract

Alpha-L-arabinofuranosidase (α-L-AFase) belongs to glycosyl hydrolases. Its main function is to hydrolyze the arabinose substituents in arabinoxylan and promote the hydrolysis of hemicellulose with other hydrolases synergistically, so as to improve the biotransformation rate of hemicellulose. In this article, the recent research advances on the enzymatic characteristic and its improvement, structure, catalytic mechanism and synergistic catalytic effect of α-L-AFase from microorganisms are reviewed. It is found that the physicochemical properties, molecular structures and catalytic mechanisms of α-L-AFases from different microbial sources are diverse, and the method of recombinant expression could effectively improve the enzymatic activity and stability of α-L-AFase. This synergistic catalysis of α-L-AFase with other hemicelluloses hydrolases can significantly improve the substrate conversion efficiency. α-L-AFase has been widely used in many fields such as improving the texture of fermented dough, juice clarification, optimizing the brewing technique, preparation of high digestion feed, and preparing the functional health products. This review provides some references for the subsequent fundamental research, development and utilization of α-L-AFase in the future.

Keywords

• α-l-arabinofuranosidase (α-l-afase)
• araboxylan
• catalytic mechanism
• synergistic effect