Continuous hydrolysis of modified wheat gluten in an enzymatic membrane reactor

文献类型： 外文期刊

第一作者： Cui, Jie

作者： Cui, Jie;Kong, Xiangzhen;Hua, Yufei;Zhou, Huiming;Liu, Qing

作者机构：

关键词： wheat gluten;modification;Alcalase;hydrolysates;enzymatic membrane reactor (EMR)

期刊名称：JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE （ 影响因子：3.638； 五年影响因子：3.802 ）

ISSN： 0022-5142

年卷期： 2011 年 91 卷 15 期

页码：

收录情况： SCI

摘要： BACKGROUND: The low solubility of wheat gluten is one of the major limitations to its use in food processing, and enzymatic hydrolysis has been found to be an effective way to prepare more soluble bioactive peptides from gluten. The aim of this study was to prepare bioactive peptides from modified wheat gluten (MWG) in a continuous enzymatic membrane reactor (EMR) that allowed rapid separation of low-molecular-weight peptides from hydrolysates, thus avoiding the disadvantages of batch reaction such as inefficient use of enzymes, inconsistent products due to batch-to-batch variation, substrate-product inhibition, low productivity and excessive hydrolysis. RESULTS: Wheat gluten was modified to decrease its lipid and starch contents in order to prevent membrane fouling. The optimal working conditions for Alcalase to hydrolyse MWG in the EMR were a substrate concentration of 20 g L-1, an enzyme/substrate ratio of 0.03, an operating pressure of 0.04 MPa, a temperature of 40 degrees C and a pH of 9. The operating stability of the EMR (including residual enzyme activity, productivity and capacity) was high. The permeate fractions showed antioxidant activities that were mostly due to low-molecular-weight peptides. A simple theoretical kinetic model was successfully applied to the enzymatic hydrolysis of MWG in the EMR. CONCLUSION: Modification of wheat gluten made the continuous enzymatic membrane reaction more efficient and the EMR proved to be an effective means of producing peptides with particular properties and bioactivities. The permeate fractions (mainly <1000 Da) were homogeneous and stable and also showed strong antioxidant activities. (C) 2011 Society of Chemical Industry

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