Effect of enzymatic hydrolysis using endo- and exo-proteases on secondary structure, functional, and antioxidant properties of chickpea protein hydrolysates
Autor: | Magdalini Galanopoulos, Yixiang Xu, Zelalem Mersha, Edward Sismour, Patricia Lynch, Shuxin Ren, Abeer Almutaimi |
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Rok vydání: | 2019 |
Předmět: |
Antioxidant
biology DPPH General Chemical Engineering medicine.medical_treatment 010401 analytical chemistry 04 agricultural and veterinary sciences Exopeptidase 040401 food science 01 natural sciences Industrial and Manufacturing Engineering Hydrolysate 0104 chemical sciences chemistry.chemical_compound Hydrolysis 0404 agricultural biotechnology chemistry Enzymatic hydrolysis medicine biology.protein Food science Solubility Safety Risk Reliability and Quality Protein secondary structure Food Science |
Zdroj: | Journal of Food Measurement and Characterization. 14:343-352 |
ISSN: | 2193-4134 2193-4126 |
Popis: | Chickpea protein isolate was hydrolyzed batchwise using Alcalase as an endopeptidase and Flavourzyme as an exopeptidase, by either individual or sequential treatment. Secondary structure, SDS-PAGE molecular weight profile, functional properties, and antioxidant activity of the hydrolysates were investigated. Alcalase was more effective than Flavourzyme to cleave the peptide bonds, and the degree of hydrolysis (DH) of Alcalase-treated hydrolysate was 25.8% compared to Flavourzyme-treated counterpart with a DH of 11.9%. Sequential treatment increased the DH up to 50%. The hydrolysis process significantly changed the protein’s secondary structure characterized by decreased ordered structures and increased disordered structures. The more notable changes occurred for those that were treated sequentially. Protein banding patterns of the hydrolysates were also markedly changed, especially for those treated by Alcalase in which no visible band was observed. Furthermore, hydrolysates had a significant (P |
Databáze: | OpenAIRE |
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