Production of Dual Inhibitory Hydrolysate by Enzymatic Hydrolysis of Squid Processing By-product

Squid processing by-product contains unutilized abundant proteins. In this study, 6 proteases (pepsin, protamex, trypsin, neutral protease, alkaline protease, and papain) were firstly employed to hydrolyze the squid processing by-product protein. The neutral protease-digested hydrolysate was found t...

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Veröffentlicht in:	Marine biotechnology (New York, N.Y.) N.Y.), 2022-04, Vol.24 (2), p.293-302
Hauptverfasser:	Liu, Qi, Yao, Yushan, Ibrahim, Mahmoud A. A., Halawany, Ali Mahmoud El, Yang, Li, Zhang, Xuewu
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkaline protease Angiotensin Angiotensin-Converting Enzyme Inhibitors - chemistry Angiotensin-Converting Enzyme Inhibitors - pharmacology Animals Biomedical and Life Sciences By-products Byproducts Decapodiformes - metabolism Digestive system Engineering Enzymes Enzymolysis Filtrate Freshwater & Marine Ecology Gastrointestinal tract Hydrolysates Hydrolysis Life Sciences Marine molluscs Microbiology Original Article Papain Pepsin Peptide Hydrolases - metabolism Peptidyl-dipeptidase A Polypeptides Protease Protein Hydrolysates - chemistry Proteins Renin Squid Trypsin Ultrafiltration Zoology
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Zusammenfassung:	Squid processing by-product contains unutilized abundant proteins. In this study, 6 proteases (pepsin, protamex, trypsin, neutral protease, alkaline protease, and papain) were firstly employed to hydrolyze the squid processing by-product protein. The neutral protease-digested hydrolysate was found to have the most promising ACE (angiotensin-converting enzyme) inhibitory activity. Based on Box-Behnken design, the optimal hydrolysis process was determined to be: 52.4 ℃ of temperature, 5.7 h of time, pH 7.1, and 8151 U/g of enzyme. Under these conditions, the ACE inhibition rate and polypeptide content of the hydrolysate were 84.26% and 229.09 mg/g, respectively. Subsequently, ultrafiltration was performed, and the ACE and renin inhibitory activities of the filtrate (
ISSN:	1436-2228 1436-2236
DOI:	10.1007/s10126-022-10104-4