Oat protein solubility and emulsion properties improved by enzymatic deamidation

被引：107

作者：

Jiang, Zhong-qing ^{[1
]}

Sontag-Strohm, Tuula ^{[1
]}

Salovaara, Hannu ^{[1
]}

Sibakov, Juhani ^{[2
]}

Kanerva, Paivi ^{[1
]}

Loponen, Jussi ^{[1
]}

机构：

[1] Univ Helsinki, Dept Food & Environm Sci, FIN-00014 Helsinki, Finland

[2] Tech Res Ctr Finland VTT, Espoo, Finland

来源：

JOURNAL OF CEREAL SCIENCE | 2015年 / 64卷

关键词：

Oat proteins; Deamidation; Solubility; Emulsions; FUNCTIONAL-PROPERTIES; SOY PROTEIN; CHRYSEOBACTERIUM-PROTEOLYTICUM; MICROBIAL TRANSGLUTAMINASE; SECONDARY STRUCTURE; GLUTAMINASE; ISOLATE; HYDROLYSIS; GLOBULIN; SUCCINYLATION;

D O I：

10.1016/j.jcs.2015.04.010

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Oat protein produced by a dry milling process was enzymatically deamidated by a food-grade protein-glutaminase (PG), and the effects on structure, solubility and emulsifying properties of oat proteins were studied. The reactions were conducted at neutral pH and low salt concentration conditions. Oat proteins were deamidated up to a deamidation degree of 59%. The solubility of proteins doubled. Oil-in-water emulsions prepared with the native and deamidated oat proteins differed as the emulsions prepared from oat proteins with high deamidation degree had a more uniform oil droplet particle size and longer stability. Fourier transform infrared (FT-IR) analysis demonstrated that oat protein secondary structure became more flexible by deamidation. Protein-glutaminase mediated deamidation appeared to be a promising technique to improve oat protein functionality such as emulsifying ability and solubility. (C) 2015 Elsevier Ltd. All rights reserved.

引用

页码：126 / 132

页数：7

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