Effect of enzymatic hydrolysis on bioactive properties and allergenicity of cricket (Gryllodes sigillatus) protein

被引:140
|
作者
Hall, Felicia [1 ]
Johnson, Philip E. [2 ]
Liceaga, Andrea [1 ]
机构
[1] Purdue Univ, Dept Food Sci, 745 Agr Mall Dr, W Lafayette, IN 47907 USA
[2] Univ Nebraska, Dept Food Sci & Technol, Food Allergy Res & Resource Program, 1901 N 21 St, Lincoln, NE 68588 USA
关键词
Cricket protein hydrolysates; Bioactive properties; Antioxidant; ACE inhibition; DPP-IV inhibition; Allergenicity; DIPEPTIDYL-PEPTIDASE IV; ANTIOXIDANT ACTIVITY; INHIBITORY PEPTIDES; ACE; SHRIMP; PRECURSORS; REACTIVITY;
D O I
10.1016/j.foodchem.2018.04.058
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Food-derived bioactive peptides have gained attention for their role in preventing chronic diseases. Edible insects are viable sources of bioactive peptides owing to their high protein content and sustainable production. In this study, whole crickets (Gryllodes sigillatus) were alcalase-hydrolyzed to a degree of hydrolysis (DH) ranging from 15 to 85%. Antioxidant activity, angiotensin converting enzyme (ACE), and dipeptidyl peptidase-4 (DPPIV)-inhibition of the cricket protein hydrolysates (CPH) were evaluated before and after simulated gastrointestinal digestion (SGD). Antioxidant activity was similar among CPH, whereas ACE and DPP-IV inhibition was greater (p < 0.05) in CPH with 60-85% DH. Bioactivity improved after SGD. CPH allergenicity was evaluated using human shrimp-allergic sera. All sera positively reacted to tropomyosin in the unhydrolyzed cricket and CPH with 15-50% DH, whereas 60-85% DH showed no reactivity. In conclusion, CPH (60-85% DH) had the greatest bioactive potential and lowest reactivity to tropomyosin, compared with other CPH and the unhydrolyzed control.
引用
收藏
页码:39 / 47
页数:9
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