Isolation and Characterization of Angiotensin Converting Enzyme Inhibitory Peptide from Buffalo Casein

Autor:	Venkatesa Perumal Shanmugam, Rajeev Kapila, Subramanian Muthukumar, Srinu Reddi, Durairaj Rajesh, Tanedjeu Sonfack Kemgang, Suman Kapila
Rok vydání:	2021
Předmět:	chemistry.chemical_classification Chymotrypsin biology 010405 organic chemistry Chemistry Bioengineering Peptide Angiotensin-converting enzyme Trypsin 01 natural sciences Biochemistry 0104 chemical sciences Analytical Chemistry chemistry.chemical_compound Pepsin Casein Drug Discovery biology.protein medicine Peptide synthesis Molecular Medicine Peptide sequence medicine.drug
Zdroj:	International Journal of Peptide Research and Therapeutics. 27:1481-1491
ISSN:	1573-3904 1573-3149
Popis:	Angiotensin-converting enzyme (ACE) enhances blood pressure by making potential vasoconstrictor, Angiotensin-II from Angiotensin-I. Thus, it is the key target enzyme in cardiovascular disease therapy. Hence, in the present study an attempt has been made for identification and characterization of ACE inhibitory peptide from buffalo milk casein. Buffalo milk casein was isolated and digested with different digestive enzymes (pepsin, trypsin, chymotrypsin and their combination). Pepsin-Trypsin hydrolysates shown highest (72.55 ± 2.23%/50 μg) ACE inhibitory activity, in further ultra-filtration
Databáze:	OpenAIRE
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