강상인·윤인성·김민교1·허민수1*
경상국립대학교 해양식품공학과/해양산업연구소, 1경상국립대학교 식품영양학과/해양산업연구소
Roe protein hydrolyzates were prepared from protein isolate of olive flounder Paralichthys olivaceus roe using various proteases, and their bioactivity and functional properties were investigated. Pantidase NP-2 (PN, 14.2%) showed the highest degree of hydrolysis, followed by flourzyme (FL, 6.7%) and aroase AP-10 (AA, 6.5%). Free and released amino acid contents were significantly higher in PN (2,931.2 mg/100 g) and FL (2,725.6 mg/100 g) than in the other hydrolyzates (437.3-812.8 mg/100 g). The foaming activities (%) of papain (PA), trypsin (TR), and bromelain (BR) hydrolyzates were 193.4%, 176.7%, and 144.2%, respectively. The emulsifying activity indices of PA, BR, chymotrypsin, and TR (9.5-30.9 m2/g-protein) were superior to those of other the hydrolyzates (2.0-8.0 m2/g-protein, (P<0.05). The 2,2′-azino-bis-3-ethylbenzo- thiazoline-6-sulfonic acid (ABTS+) radical scavenging activities of protamex (PR, 108 μg/mL) and AA (115.5 μg/mL) were more potent (P<0.05). Angiotensin I converting enzyme inhibitory activities of all enzyme hydrolyzates (52.0-83.3%) were more robust compared with that of control. Among the enzyme hydrolyzates, AA, FL, and PR showed relatively good tyrosinase inhibitory activities compared to that of the control (29.3%). Bioactivity and food functional properties showed that TR, BR, AA, and FL were superior.
Enzyme hydrolysates, Food functionality, Protein isolate, Olive flounder, Roe