β-glucosidase is a pivotal enzyme that hydrolyzes bound volatile aromatic compounds. However, the activity of β-glucosidase in winemaking and the mechanism by which it affects the flavor and taste of wines have not been fully investigated. In this study, we profiled the characteristics of β-glucosidase derived from wine-related yeasts isolated from different wine-making regions in China, and analyzed the enzyme activity from different parts of the cells under aerobic and anaerobic conditions. A total of 56 strains of wine-related yeasts producing β-glucosidases were screened using the YNB-C medium (YNB 6.7 g L-1 , cellobiose 5 g L-1 , pH 5.0). We found that strain Clavispora lusitaniae C117 produced the highest enzyme activity (152.39 µmol pNP ml-1 h-1 ). In most strains, β-glucosidase were located in whole cells (periplasmic space) and permeabilized cells (intracellular). The non-Saccharomyces species had the highest enzymatic activity in a strain-dependent manner. Under aerobic conditions, C. lusitaniae C117, Hanseniaspora guilliermondii A27-3-4, Metschnikowia pulcherrima F-1-6, and Pichia anomala C84 had the highest β-glucosidase activity. We further investigated the β-glucosidase activity during the wine fermentation and the effects of sugar, pH, temperature, and ethanol on the enzyme activities of P. anomala C84 and commercial Saccharomyces yeast strains RC212 and VL1. The presence of fructose, glucose, and sucrose strongly inhibited enzyme activity. Similarly, low pH and low temperature inhibited the activity of β-glucosidase, whereas ethanol promoted enzyme activity. Our findings provide a theoretical basis on understanding the different yeast characteristics of β-glucosidase and their potential application for further improving wine aroma complexity.
Keywords: Pichia anomala; aroma complexity; transglycosylation; wine; yeasts; β-glucosidase.
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