水解物
响应面法
化学
中心组合设计
DPPH
胰蛋白酶
淀粉酶
阿布茨
色谱法
IC50型
水解
酶
食品科学
生物化学
体外
抗氧化剂
作者
Wedad Q. AL‐Bukhaiti,Sam Al‐Dalali,Anwar Noman,Silin Qiu,Sherif M. Abed,Sheng‐Xiang Qiu
出处
期刊:Foods
[MDPI AG]
日期:2022-10-21
卷期号:11 (20): 3303-3303
被引量:11
标识
DOI:10.3390/foods11203303
摘要
Optimization of the enzymolysis process for preparing peanut protein hydrolysates using alcalase and trypsin was performed by employing the central composite design (CCD) of response surface methodology (RSM). The independent variables were solid-to-liquid ratio (S/L), enzyme-to-substrate ratio (E/S), pH, and reaction temperature, while the response variables were degree of hydrolysate (DH), α-amylase, and α-glucosidase inhibitory activity. The highest DH (22.84% and 14.63%), α-amylase inhibition (56.78% and 40.80%), and α-glucosidase inhibition (86.37% and 86.51%) were obtained under optimal conditions, which were S/L of 1:26.22 and 1:30 w/v, E/S of 6% and 5.67%, pH of 8.41 and 8.56, and temperature of 56.18 °C and 58.75 °C at 3 h using alcalase (AH) and trypsin (TH), respectively. Molecular weight distributions of peanut protein hydrolysates were characterized by SDS-PAGE, which were mostly ˂10 kDa for both hydrolysates. Lyophilized AH and TH had IC50 values of 6.77 and 5.86 mg/mL for α-amylase inhibitory activity, and 6.28 and 5.64 mg/mL for α-glucosidase inhibitory activity. The IC50 of AH and TH against DPPH radical was achieved at 4.10 and 3.20 mg/mL and against ABTS radical at 2.71 and 2.32 mg/mL, respectively. The obtained hydrolysates with antidiabetic activity could be utilized as natural alternatives to synthetic antidiabetics, particularly in food and pharmaceutical products.
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