Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions
A great deal of attention has been paid to charactering the protein hydrolysates prepared by enzymatic hydrolysis, while the influence of molecular weight (MW) distributions on the resultant hydrolysates remains unclear. This study aimed to explore the physicochemical and antioxidant characteristics...
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| Format: | Article |
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Frontiers Research Foundation
2022
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| _version_ | 1825938533549867008 |
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| author | Chen, Yin Zheng, Zhaojun Ai, Zixuan Zhang, Yan Tan, Chin Ping Liu, Yuanfa |
| author_facet | Chen, Yin Zheng, Zhaojun Ai, Zixuan Zhang, Yan Tan, Chin Ping Liu, Yuanfa |
| author_sort | Chen, Yin |
| collection | UPM |
| description | A great deal of attention has been paid to charactering the protein hydrolysates prepared by enzymatic hydrolysis, while the influence of molecular weight (MW) distributions on the resultant hydrolysates remains unclear. This study aimed to explore the physicochemical and antioxidant characteristics of protein hydrolysate and its peptide fractions. Bromelain has been commonly used to hydrolyze black bean protein via response surface methodology (RSM). The optimal hydrolysis parameters were observed at 52°C, pH 7, E/S ratio of 2.2 (ratio of enzyme to substrate), and 4 h. Under these parameters, the hydrolysate (BPH) presented DPPH radical scavenging activity and Fe2+ chelating activity with IC50 values of 100.08 ± 2.42 and 71.49 ± 0.81 μg/mL, respectively. This might be attributed to structural characteristics, varying with different molecular weight distributions. Interestingly, among BPH and its peptide fractions, peptides smaller than 3 kDa were noted to exhibit the strongest DPPH and ABTS radical scavenging activity. More intriguingly, this peptide fraction (<3 kDa) could predominantly prolong the induction period of sunflower oil, which was, respectively increased to 1.31 folds. This may be due to high proportions of hydrophobic amino acids. Unexpectedly, the optimal Fe2+ chelating activity was observed in the peptide fraction measuring at 3–10 kDa, showing highly positive correlations with histidine and arginine. These identified peptide fractions derived from black bean protein can therefore be employed for food fortification acting as natural antioxidant alternatives. |
| first_indexed | 2024-03-06T11:15:13Z |
| format | Article |
| id | upm.eprints-101401 |
| institution | Universiti Putra Malaysia |
| last_indexed | 2024-03-06T11:15:13Z |
| publishDate | 2022 |
| publisher | Frontiers Research Foundation |
| record_format | dspace |
| spelling | upm.eprints-1014012023-06-19T08:09:06Z http://psasir.upm.edu.my/id/eprint/101401/ Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions Chen, Yin Zheng, Zhaojun Ai, Zixuan Zhang, Yan Tan, Chin Ping Liu, Yuanfa A great deal of attention has been paid to charactering the protein hydrolysates prepared by enzymatic hydrolysis, while the influence of molecular weight (MW) distributions on the resultant hydrolysates remains unclear. This study aimed to explore the physicochemical and antioxidant characteristics of protein hydrolysate and its peptide fractions. Bromelain has been commonly used to hydrolyze black bean protein via response surface methodology (RSM). The optimal hydrolysis parameters were observed at 52°C, pH 7, E/S ratio of 2.2 (ratio of enzyme to substrate), and 4 h. Under these parameters, the hydrolysate (BPH) presented DPPH radical scavenging activity and Fe2+ chelating activity with IC50 values of 100.08 ± 2.42 and 71.49 ± 0.81 μg/mL, respectively. This might be attributed to structural characteristics, varying with different molecular weight distributions. Interestingly, among BPH and its peptide fractions, peptides smaller than 3 kDa were noted to exhibit the strongest DPPH and ABTS radical scavenging activity. More intriguingly, this peptide fraction (<3 kDa) could predominantly prolong the induction period of sunflower oil, which was, respectively increased to 1.31 folds. This may be due to high proportions of hydrophobic amino acids. Unexpectedly, the optimal Fe2+ chelating activity was observed in the peptide fraction measuring at 3–10 kDa, showing highly positive correlations with histidine and arginine. These identified peptide fractions derived from black bean protein can therefore be employed for food fortification acting as natural antioxidant alternatives. Frontiers Research Foundation 2022-06-06 Article PeerReviewed Chen, Yin and Zheng, Zhaojun and Ai, Zixuan and Zhang, Yan and Tan, Chin Ping and Liu, Yuanfa (2022) Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions. Frontiers in Nutrition, 9. pp. 1-13. ISSN 2296-861X https://www.frontiersin.org/articles/10.3389/fnut.2022.884537/full 10.3389/fnut.2022.884537 |
| spellingShingle | Chen, Yin Zheng, Zhaojun Ai, Zixuan Zhang, Yan Tan, Chin Ping Liu, Yuanfa Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions |
| title | Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions |
| title_full | Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions |
| title_fullStr | Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions |
| title_full_unstemmed | Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions |
| title_short | Exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions |
| title_sort | exploring the antioxidant and structural properties of black bean protein hydrolysate and its peptide fractions |
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