Solid-state tyrosinase stability as affected by water activity and glass transition

被引:18
作者
Chen, YH
Aull, JL
Bell, LN
机构
[1] Auburn Univ, Dept Nutr & Food Sci, Auburn, AL 36849 USA
[2] Auburn Univ, Dept Chem, Auburn, AL 36849 USA
关键词
enzyme; tyrosinase; class transition; water activity; stability;
D O I
10.1016/S0963-9969(99)00109-X
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The effects of water activity (a(w)) and the state of the system as dictated by the glass transition temperature (Tg) on tyrosinase storage stability were evaluated in a model food system. Tyrosinase was incorporated into low and high molecular weight polyvinylpyrrolidone (PVP-LMW and PVP-K30, respectively). Samples were equilibrated and stored in desiccators from a(w) 0.33 to 0.77 at 20 degrees C. Tyrosinase activity was monitored for a week, and pseudo-first order rate constants for activity loss were calculated. Residual activity after equilibration correlated with T-g rather than a(w). An apparent rate constant increase slightly above T-g was observed and rate constants were the same at constant T-g, suggesting that molecular mobility as dictated by T-g was influencing tyrosinase storage stability. (C) 2000 Canadian Institute of Food Science and Technology. Published by Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:467 / 472
页数:6
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