Open AccessIsolasi Penghambat Aktivitas Enzim Pengubah Angiotensin Dari Protein Susu
Author(s) -
Amhar Abubakar
Publication year - 2016
Publication title -
jurnal agripet
Language(s) - English
Resource type - Journals
eISSN - 2460-4534
pISSN - 1411-4623
DOI - 10.17969/agripet.v7i2.3212
Subject(s) - thermolysin , papain , pepsin , chemistry , chymotrypsin , whey protein , trypsin , proteases , thermostability , digestion (alchemy) , enzyme , biochemistry , proteolytic enzymes , food science , chromatography
. Three kinds of samles (whey protein containing casenoglycopeptide, whey protein removed casenoglycopeptide and cheese whey powder digested with 7 kinds of proteases at 37 0C for 24 hr (trypsin, protenase-K, actinase-E, thermolysin, and papain) or 25 0C (pepsin and chymotrypsin). Strong inhibotory activity against the angiotensin converting enzyime (ACE, EC 3.4.15.1) was generated in all samples by 5 proteases digestion (pepsin, chymotrypsin, protinase-K, thermolysin and papain). In whey protein removed caseinoglycopeptide digestion by thermolysin induced the highest activity (95,25%). In cheese whey powder, the highest activity was derived by thermolysin (98.25%). On the other hand, week ACE inhibitory activity were derived by trypsin and actinase-E digestion. As no remarkable differences in inhibitory activity were observed between whey protein containing casenoglycopeptide and whey protein removed casenoglycopeptide samples, the bioactive peptides are considered to come mainly not from casenoglycopeptide but from cheese whey powder components.