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Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases
The effect of enzymatic hydrolysis of apricot kernel protein with different proteases (Alcalase, pancreatin, pepsin, and trypsin) on the amino acid content, degree of hydrolysis (DH), antioxidant, and antibacterial characteristics of the resulting hydrolyzates was investigated in this study. The com...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10494656/ https://www.ncbi.nlm.nih.gov/pubmed/37701210 http://dx.doi.org/10.1002/fsn3.3467 |
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author | Sarabandi, Khashayar Mohammadi, Maryam Akbarbaglu, Zahra Ghorbani, Marjan Najafi, Shahla Safaeian Laein, Sara Jafari, Seid Mahdi |
author_facet | Sarabandi, Khashayar Mohammadi, Maryam Akbarbaglu, Zahra Ghorbani, Marjan Najafi, Shahla Safaeian Laein, Sara Jafari, Seid Mahdi |
author_sort | Sarabandi, Khashayar |
collection | PubMed |
description | The effect of enzymatic hydrolysis of apricot kernel protein with different proteases (Alcalase, pancreatin, pepsin, and trypsin) on the amino acid content, degree of hydrolysis (DH), antioxidant, and antibacterial characteristics of the resulting hydrolyzates was investigated in this study. The composition of amino acids (hydrophobic: ~35%; antioxidant: ~13%), EAA/TAA ratio (~34%), and PER index (~1.85) indicates the ability of the hydrolyzate as a source of nutrients and antioxidants with high digestibility. Enzymatic hydrolysis with increasing DH (from 3.1 to a maximum of 37.9%) led to improved solubility (especially in the isoelectric range) and changes in water‐ and oil‐holding capacity. The highest free radical scavenging activity of DPPH (83.3%), ABTS (88.1%), TEAC (2.38 mM), OH (72.5%), NO (65.7%), antioxidant activity in emulsion and formation of TBARS (0.36 mg MDA/L), total antioxidant (1.61), reducing power (1.17), chelation of iron (87.7%), copper (34.8%) ions, and inhibition of the growth of Escherichia coli (16.3 mm) and Bacillus cereus (15.4 mm) were affected by the type of enzymes (especially Alcalase). This research showed that apricot kernel hydrolyzate could serve as a nutrient source, emulsifier, stabilizer, antioxidant, and natural antibacterial agent in functional food formulations. |
format | Online Article Text |
id | pubmed-10494656 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-104946562023-09-12 Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases Sarabandi, Khashayar Mohammadi, Maryam Akbarbaglu, Zahra Ghorbani, Marjan Najafi, Shahla Safaeian Laein, Sara Jafari, Seid Mahdi Food Sci Nutr Original Articles The effect of enzymatic hydrolysis of apricot kernel protein with different proteases (Alcalase, pancreatin, pepsin, and trypsin) on the amino acid content, degree of hydrolysis (DH), antioxidant, and antibacterial characteristics of the resulting hydrolyzates was investigated in this study. The composition of amino acids (hydrophobic: ~35%; antioxidant: ~13%), EAA/TAA ratio (~34%), and PER index (~1.85) indicates the ability of the hydrolyzate as a source of nutrients and antioxidants with high digestibility. Enzymatic hydrolysis with increasing DH (from 3.1 to a maximum of 37.9%) led to improved solubility (especially in the isoelectric range) and changes in water‐ and oil‐holding capacity. The highest free radical scavenging activity of DPPH (83.3%), ABTS (88.1%), TEAC (2.38 mM), OH (72.5%), NO (65.7%), antioxidant activity in emulsion and formation of TBARS (0.36 mg MDA/L), total antioxidant (1.61), reducing power (1.17), chelation of iron (87.7%), copper (34.8%) ions, and inhibition of the growth of Escherichia coli (16.3 mm) and Bacillus cereus (15.4 mm) were affected by the type of enzymes (especially Alcalase). This research showed that apricot kernel hydrolyzate could serve as a nutrient source, emulsifier, stabilizer, antioxidant, and natural antibacterial agent in functional food formulations. John Wiley and Sons Inc. 2023-06-01 /pmc/articles/PMC10494656/ /pubmed/37701210 http://dx.doi.org/10.1002/fsn3.3467 Text en © 2023 The Authors. Food Science & Nutrition published by Wiley Periodicals LLC. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Original Articles Sarabandi, Khashayar Mohammadi, Maryam Akbarbaglu, Zahra Ghorbani, Marjan Najafi, Shahla Safaeian Laein, Sara Jafari, Seid Mahdi Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases |
title | Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases |
title_full | Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases |
title_fullStr | Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases |
title_full_unstemmed | Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases |
title_short | Technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases |
title_sort | technological, nutritional, and biological properties of apricot kernel protein hydrolyzates affected by various commercial proteases |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10494656/ https://www.ncbi.nlm.nih.gov/pubmed/37701210 http://dx.doi.org/10.1002/fsn3.3467 |
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