Effects of deamidation on aggregation and emulsifying properties of barley glutelin |
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Authors: | J Zhao Z TianL Chen |
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Affiliation: | Dept. of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Canada T6G 2P5 |
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Abstract: | The structure, solubility and emulsifying properties of the deamidated barley glutelin were investigated. The SDS–PAGE, size exclusion chromatography combined with a laser photometer (SEC-LP) and Fourier transform infrared spectroscopy (FTIR) results revealed that glutelin underwent a rapid hydrolysis and unfolding even at the initial stage of deamidation, leading to remarkably improved glutelin solubility at both acidic and neutral pHs. The deamidated glutelin demonstrated a strong tendency to form soluble aggregates of very large molecular weight (106–107 g/mol) probably due to disulphide-crosslinking and hydrophobic interactions. These aggregates played a major role in stabilising the emulsions at a broad range of deamidation levels (2.2–5.6% to 43%). In this way, undesirable property changes which result from excessive deamidation can be avoided, leading to wider applications of deamidated barley glutelin as an emulsifying ingredient in food and non-food applications. |
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Keywords: | Barley protein Glutelin Deamidation Aggregation Solubility Emulsifying property |
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