| Specificity of Carboxypeptidases from Actinomucor elegans and Their Debittering Effect on Soybean Protein Hydrolysates. | |
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MedLine Citation:
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PMID: 21858525 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The specificities of carboxypeptidases from Actinomucor elegans were investigated by determining enzymatic activities at pH 7.0 and pH 4.0 with 16 Z-dipeptides and three Z-tripeptides as substrates. The debittering effect was evaluated and the free amino acid compositions of the soybean protein hydrolysates were analyzed before and after treatment with A. elegans extract at pH 7.0 and pH 4.0, with carboxypeptidases from Aspergillus oryzae as control. The results of the enzyme activity determinations indicated that carboxypeptidases from A. elegans prefer hydrophobic substrates, such as Z-Phe-Leu, Z-Phe-Tyr-Leu, and Z-Phe-Tyr. The sensory evaluation and free amino acid composition analysis showed that these carboxypeptidases are efficient tools for decreasing the bitterness of peptides because they liberated the fewest free amino acids, which consisted of 73% hydrophobic amino acids, under acidic conditions. Carboxypeptidases from A. elegans display promising prospects for future applications in the protein hydrolysate industry. |
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Authors:
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Jing Fu; Li Li; Xiao-Quan Yang |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-8-20 |
Journal Detail:
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Title: Applied biochemistry and biotechnology Volume: - ISSN: 1559-0291 ISO Abbreviation: - Publication Date: 2011 Aug |
Date Detail:
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Created Date: 2011-8-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8208561 Medline TA: Appl Biochem Biotechnol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Research and Development Center of Food Proteins, College of Light Industry and Food Science, South China University of Technology, Guangzhou, 510641, China. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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