Protein hydrolysates from silkworm (Bombyx mori) pupae protein treated with a novel neutral protease

文献类型： 外文期刊

第一作者： Herman, R. A.

作者： Herman, R. A.;Li, Z-N;Xie, C.;Wang, J-Z;Hu, Y.;Shittu, S.;You, S.;Wang, J.;You, S.;Wang, J.

作者机构：

关键词： enzymatic hydrolysis; silkworm (Bombyx mori) pupae protein; neutral protease; Stenotrophomonas maltophilia

期刊名称：JOURNAL OF INSECTS AS FOOD AND FEED （ 影响因子：5.099； 五年影响因子：5.08 ）

ISSN：

年卷期： 2022 年 8 卷 3 期

页码：

收录情况： SCI

摘要： Edible insects, regarded as a potential contributor to food security are currently given wide consideration due to their rich protein and other micronutrients contents. In this study, protease-assisted hydrolysis proposes an economically effective approach to hydrolyse proteins from silkworm (Bombyx mori) pupae to improve its functional properties. The proteolytic activity of a novel neutral protease (265.14 U/ml) with appreciable thermal activities, was identified using 16S rDNA as Stenotrophomonas maltophilia JW20 (SmNP20). The neutral protease with an apparent molecular weight of 28 kDa emerged active at pH 7 and maintained stability in pH range 6.0-8.0. The optimum temperature was 60 degrees C and stable at 55-60 degrees C, maintaining over 80% of its initial activity, with a half-life of 78.75, 89, 66.8 and 44 min at 50, 60, 70 and 80 degrees C. It was purified to 9.98-fold with a specific activity of 455.06 U/mg and 63.73% yield. The K-m and V-max values were 0.70 mg/ml and 9.48 1.mu mol/min/mg, respectively. Enzymolysis with neutral protease enhanced the degree of hydrolysis (97.46 +/- 4.87%), increased water solubility over 50%, and a significant protein solubility of 63.44 +/- 0.65%. The K-m and V-max of the protein yield were 0.24 mg/ml and 165.63 mu mol/min/mg respectively. A total of 17 amino acids have been detected in the hydrolysates obtained from the silkworm pupae protein. In comparison with neutrase and flavorzyme, the enzyme possesses an elevated hydrolytic and catalytic efficiency. Emulsion activity and foam capacity ranged from 8-48 m(2)/g and 6-25% respectively. Hence, this study confirms the unique and efficient characteristics of an insect-enzyme correlation that is practically significant with potential improvement in nutritional composition and functional quality of insect proteins.

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