Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii.
Hydrolysis parameters (temperature, E/S ratio, pH, and time) for acid protease (from Aspergillus usamii) hydrolysis of wheat gluten were optimized by response surface methodology (RSM) using emulsifying activity index (EAI) as the response factor. A temperature of 48.9°C, E/S ratio of 1.60%, pH 3.0,...
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2016-01-01
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doaj-d908030febb4458aa84a9d110d894f722020-11-25T02:33:14ZengPublic Library of Science (PLoS)PLoS ONE1932-62032016-01-01117e016010110.1371/journal.pone.0160101Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii.Lingli DengZhaoxia WangSheng YangJunmei SongFei QueHui ZhangFengqin FengHydrolysis parameters (temperature, E/S ratio, pH, and time) for acid protease (from Aspergillus usamii) hydrolysis of wheat gluten were optimized by response surface methodology (RSM) using emulsifying activity index (EAI) as the response factor. A temperature of 48.9°C, E/S ratio of 1.60%, pH 3.0, hydrolysis time of 2.5 h was found to be the optimum condition to obtain wheat gluten hydrolysate with higher EAI. The solubility of wheat gluten was greatly improved by hydrolysis and became independent of pH over the studied range. Enzymatic hydrolysis resulted in dramatically increase in EAI, water and oil holding capacity. Molecular weight distribution results showed that most of the peptides above 10 kDa have been hydrolyzed into smaller peptides. The results of FTIR spectra and disulfide bond (SS) and sulfhydryl (SH) content suggested that a more extensional conformation was formed after hydrolysis, which could account for the improved functional properties.http://europepmc.org/articles/PMC4965038?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Lingli Deng Zhaoxia Wang Sheng Yang Junmei Song Fei Que Hui Zhang Fengqin Feng |
spellingShingle |
Lingli Deng Zhaoxia Wang Sheng Yang Junmei Song Fei Que Hui Zhang Fengqin Feng Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii. PLoS ONE |
author_facet |
Lingli Deng Zhaoxia Wang Sheng Yang Junmei Song Fei Que Hui Zhang Fengqin Feng |
author_sort |
Lingli Deng |
title |
Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii. |
title_short |
Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii. |
title_full |
Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii. |
title_fullStr |
Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii. |
title_full_unstemmed |
Improvement of Functional Properties of Wheat Gluten Using Acid Protease from Aspergillus usamii. |
title_sort |
improvement of functional properties of wheat gluten using acid protease from aspergillus usamii. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2016-01-01 |
description |
Hydrolysis parameters (temperature, E/S ratio, pH, and time) for acid protease (from Aspergillus usamii) hydrolysis of wheat gluten were optimized by response surface methodology (RSM) using emulsifying activity index (EAI) as the response factor. A temperature of 48.9°C, E/S ratio of 1.60%, pH 3.0, hydrolysis time of 2.5 h was found to be the optimum condition to obtain wheat gluten hydrolysate with higher EAI. The solubility of wheat gluten was greatly improved by hydrolysis and became independent of pH over the studied range. Enzymatic hydrolysis resulted in dramatically increase in EAI, water and oil holding capacity. Molecular weight distribution results showed that most of the peptides above 10 kDa have been hydrolyzed into smaller peptides. The results of FTIR spectra and disulfide bond (SS) and sulfhydryl (SH) content suggested that a more extensional conformation was formed after hydrolysis, which could account for the improved functional properties. |
url |
http://europepmc.org/articles/PMC4965038?pdf=render |
work_keys_str_mv |
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