Production and characterization of a novel cold-active B-glucosidase and its influence on aromatic precursors of Muscat wine
作者机构：UNLP CONICET Ctr Invest & Desarrollo Fermentac Ind CINDEFI CCT La Plata Calle 47 & 115B1900ASH La Plata Buenos Aires Argentina UdelaR Dept Biociencias Area Bioquim Fac Quim Gen Flores 2124 Montevideo 1157 Uruguay
出 版 物：《FOOD BIOSCIENCE》 (Food BioSci.)
年 卷 期：2023年第53卷第3期
页 面：876-886页
核心收录：
学科分类：0832[工学-食品科学与工程（可授工学、农学学位）] 08[工学]
基 金：National Scientific and Technological Research Council National Agency for the Pro- motion of Science and Technology [PICT 2018- 3194, PICT 2019-3123] National Scientific and Tech- nological Research Council National Agency for the Promotion of Science and Technology (ANPCyT) [PICT 2019-3123, PICT 2018-3194]
主 题：Antarctic yeasts Wine-aroma enhancement Cold-active B-glucosidase Mrakia sp Monoterpenes Muscat wine
摘 要：B-Glucosidases (BGL)-widely used in the enological field-are enzymes that catalyze the liberation of aromatic volatiles from their glycosidic precursors during winemaking. In the present study, a BGL obtained from the Antarctic yeast Mrakia sp. LP 7.1.2016 was produced on a bioreactor scale, purified, characterized, and the enzyme s properties studied for a potential enological application. Sodium-dodecylsulfate-polyacrylamide-gel electrophoresis indicated a high molecular weight for this enzyme, it having at least two subunits of 134 and 14 kDa. BGL exhibited a pH optimum of 5.0 and retained substantial activity and stability at pH 4.0. The temper-ature range for optimal activity was 50-55 degrees C, with the enzyme demonstrating thermostability up to 50 degrees C and retaining 87% of residual activity at that temperature after 3 h. The respective kinetic constants determined with p-nitrophenyl-B-D-glucopyranoside and cellobiose were 0.38 and 1.79 mM for Km and 20.1 and 5.65 mu mol-1 mg- 1 min.1 for Vmax, B-Glucosidase manifested high activity in 10-25% (v/v) ethanol, 30.0 mg L-1 sulfur di-oxide, and 10-200 g L-1 fructose;but it was strongly inhibited by glucose, retaining only 6% of residual activity in the presence of 20 g L-1. Upon investigating the influence of the enzyme on Muscat-wine glycosidic pre-cursors, we found significant differences in terpene content after 14 days of BGL treatment at an eightfold in-crease over control-wine levels. The enzyme was more active toward the precursors of the monoterpenes nerol and geraniol and oxides of trans- and cis-linalool. These findings contribute to our understanding of the potential of cold-active enzymes in advantageous biotechnological applications to enology.
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