넙치(Paralichthys olivaceus) 알의 분리단백질로부터 제조한 효소 가수 분해물의 식품기능 특성 및 생리활성
Food Functionality and Bioactivity of Enzyme Hydrolyzates Prepared Using Protein Isolates from Olive Flounder Paralichthys olivaceus Roes
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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.
Abstract
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.