Characterization of mung bean endogenous proteases and globulins and their effects on the production of mung bean protein

被引:1
|
作者
Zhou, Qianqian [1 ]
Wang, Lili [2 ]
Zhang, Yaowen [3 ]
Zhang, Caimeng [1 ]
Kong, Xiangzhen [1 ]
Hua, Yufei [1 ]
Chen, Yeming [1 ]
机构
[1] Jiangnan Univ, Sch Food Sci & Technol, Wuxi 214122, Peoples R China
[2] Chinese Acad Agr Sci, Inst Food Sci & Technol, Beijing 100193, Peoples R China
[3] Shanxi Agr Univ, Shanxi Acad Agr Sci, Coll Agr, Taiyuan 030031, Peoples R China
关键词
Mung bean protein; Protein extraction; Endogenous proteases; Cleavage specificity; Mung bean 11S globulin; RADIATA L. WILCZEK; TRYPSIN-INHIBITOR; STORAGE PROTEIN; PURIFICATION; CARBOXYPEPTIDASE; ENDOPEPTIDASE; ARABIDOPSIS; DEGRADATION; COTYLEDONS; EXTRACTION;
D O I
10.1016/j.foodchem.2024.138477
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
Mung bean protein possesses several health benefits, and aqueous processing methods are used for its production. However, mung bean protein yields are different with different methods, which are actually different in conditions (e.g., pH, temperature, and time). Herein, liquid chromatography tandem mass spectrometry identified 28 endopeptidases and exopeptidases in mung bean protein extract, and the positions of 8S and 11S globulins on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gel were confirmed in our experimental conditions. The SDS-PAGE, trichloroacetic acid-nitrogen solubility index, and free amino acid analysis revealed that (1) 8S globulins showed strong resistance to the endopeptidases (optimal at pH 5 and 50 degrees C) at pH 3-9, and 11S globulin exhibit strong resistance expect at pH 3-3.5; (2) the exopeptidases (optimal at pH 6 and 50 degrees C) preferred to liberate methionine and tryptophan. These proteases negatively affected protein yield, and short production time and low temperature were recommended.
引用
收藏
页数:10
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