Effects of a β-glucanase enzymatic preparation on yeast lysis during aging of traditional sparkling wines

被引:17
|
作者
Torresi, Sara [1 ]
Frangipane, Maria T. [1 ]
Garzillo, Anna M. V. [2 ]
Massantini, Riccardo [1 ]
Contini, Marina [1 ]
机构
[1] Dept Innovat Biol Agro Food & Forest Syst, I-01100 Viterbo, Italy
[2] Dept Ecol & Biol Sci, I-01100 Viterbo, Italy
关键词
On lees aging; Autolysis; Enzymatic preparation; beta-Glucanase; Methode champenoise; Sparkling wine; AUTOLYSIS; PROTEINS; STRAINS; LEES;
D O I
10.1016/j.foodres.2013.10.034
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Scientific researches on characterization of the commercial enological preparation of Lallzyme MMX (R) containing beta-glucanase and its influence on autolysis of different yeast strains typically employed in the production of sparkling wine are lacking. The aim of the present work was to plug a gap in this field, studying the beta-glucanase activity of Lallzyme MMX (R) and its interactions with BCS103 (R) and EC1118 (R) yeast strains. The results showed that beta-glucanase was slightly inhibited by ethanol, but its residual activity at wine pH was sufficient for the purposes. Kinetic parameters showed a better enzyme-substrate complex formation for the EC1118 (R) strain. The influence on yeast lysis during 12 months of bottle-aging was monitored, demonstrating that enzyme addition did not substantially influence either the content and progression of total proteins, or foam characteristics. However, scanning and transmission electron microscopy images and free amino acid analysis indicated beta-glucanase improved cell wall degradation of both selected yeasts, evidencing a lower autolytic capacity of the BCS103 (R) strain. Our study demonstrated that addition of beta-glucanase catalyzed cell disorganization and promoted release of yeast components into sparkling wine, with strain-dependent effects. Therefore, employment of beta-glucanase rich Lallzyme MMX (R) might effectively accelerate some aging characteristics of traditional sparkling wines. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码:83 / 92
页数:10
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