ScholarWorks@경상국립대학교

초록

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.

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