plSSN : 0374-8111 | elSSN : 2287-8815
plSSN : 0374-8111 | elSSN : 2287-8815
plSSN : 0374-8111elSSN : 2287-8815
강상인·윤인성·김민교1·이정석·허민수1*
경상국립대학교 해양식품공학과/해양산업연구소, 1경상국립대학교 식품영양학과/해양산업연구소
In the present study, protein hydrolysates were prepared from olive flounder Paralichthys olivaceus roe concentrate using different commercial proteases, and their functional properties and bioactivities were examined. Protamex (PR; 21.6%) showed the highest degree of hydrolysis, followed by alcalase (AL; 21.1%) and aroase AP-10 (AA; 20.2%). With regard to foaming activity, trypsin, chymotrypsin (CH), and bromelain (BR) had values ranging 181-188%, followed by neutrase (152%) and AA (141%). CH (36%) and BR (70%) maintained foam stability for up to 15 min. The oil-in-water emulsifying activity index of CH (10.6 m2/g) was the highest among all the hydrolysates. Notably, the 2,2′-azino-bis-3-ethylbenzo-thiazoline-6-sulfonic acid (ABTS+) radical scavenging activities (IC50) were significantly higher in pantidase NP-2 (68.1 μg/mL) and flavourzyme (FL, 69.8 μg/mL) than in other hydrolysates. The tyrosinase inhibitory activities of FL, PR, and AA were inhibited by 12.5-19.8%. Aangiotensin I converting enzyme inhibitory activity of the control was 80.9%, and that of the hydrolysates of CH, AA, PR, and AL, which exhibited higher inhibitory activity, ranged 87.6-90.7%. CH, BR, and AA AP-10 hydrolysates exhibited superior bioactivity and functional properties. Therefore, these hydrolysates can be used as food ingredients in novel types of functional food-enhancing seafood and food processing industries.
Olive flounder, Roe, Steam-dried concentrate, Enzyme hydrolysates, Functionality