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Characterization of mung bean endogenous proteases and globulins and their effects on the production of mung bean protein.
Zhou, Qianqian; Wang, Lili; Zhang, Yaowen; Zhang, Caimeng; Kong, Xiangzhen; Hua, Yufei; Chen, Yeming.
Affiliation
  • Zhou Q; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
  • Wang L; Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China. Electronic address: wlland2013@163.com.
  • Zhang Y; College of Agriculture, Shanxi Agricultural University (Shanxi Academy of Agricultural Sciences), Taiyuan 030031, China.
  • Zhang C; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
  • Kong X; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
  • Hua Y; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China.
  • Chen Y; School of Food Science and Technology, Jiangnan University, Wuxi 214122, China. Electronic address: chenyeming@jiangnan.edu.cn.
Food Chem ; 442: 138477, 2024 Jun 01.
Article in En | MEDLINE | ID: mdl-38278107
ABSTRACT
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 °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 °C) preferred to liberate methionine and tryptophan. These proteases negatively affected protein yield, and short production time and low temperature were recommended.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Vigna / Globulins / Fabaceae Language: En Journal: Food Chem Year: 2024 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Vigna / Globulins / Fabaceae Language: En Journal: Food Chem Year: 2024 Document type: Article