Exploring bioactivities from distinct Cicer protein hydrolysate as influenced by enzymatic hydrolysis
The genus, Cicer, accomodate chickpeas which offer a highly nutritious profile for human wellness. In this study, we hydrolyzed different species of Cicer seed proteins using various proteolytic enzymes to determine DH, antioxidant, ACE-I inhibitory and anti-inflammatory activity. The alcalase hydro...
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| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Taylor & Francis Group
2024-12-01
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| Series: | CyTA - Journal of Food |
| Subjects: | |
| Online Access: | https://www.tandfonline.com/doi/10.1080/19476337.2024.2362688 |
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| Summary: | The genus, Cicer, accomodate chickpeas which offer a highly nutritious profile for human wellness. In this study, we hydrolyzed different species of Cicer seed proteins using various proteolytic enzymes to determine DH, antioxidant, ACE-I inhibitory and anti-inflammatory activity. The alcalase hydrolysis experimented for 120 minutes achieved maximum peptide content. And subsequent size fractionation of peptide by G-50 gel filtration column chromatography showed an enhancement in bioactivity. The alcalase hydrolysate demonstrated highest ACE inhibition (66.18 ± 2.65%, 64.22 ± 1.32%, and 60.19 ± 1.46%) in Cicer arietinum, Cicer reticulatum, and Cicer echinospermum, respectively. Furthermore, alcalase hydrolysate showed promising antioxidant efficacy measured by various techniques. Hyaluronidase inhibition was moderate, while lipoxygenase inhibition of alcalase hydrolysate showed an elevated response (IC50 = 32.6 ± 1.4 μg/ml for C. arietinum). Among all proteases, alcalase generated maximum degree of hydrolysis, resulting in peptides that exhibited significantly improved bioactivity. |
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| ISSN: | 1947-6337 1947-6345 |