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The Purification and Characterization of a Novel Neutral Protease from Volvariella volvacea Fruiting Bodies and the Enzymatic Digestion of Soybean Isolates

文献类型： 外文期刊

作者： Xu, Baoting 1 ; Li, Zhiping 2 ; Guo, Qian 2 ; Zha, Lei 2 ; Li, Chuanhua 2 ; Yu, Panling 1 ; Chen, Mingjie 2 ; Zhao, Yan 2 ;

作者机构： 1.Shanghai Ocean Univ, Coll Food Sci & Technol, Shanghai 201306, Peoples R China

2.Shanghai Acad Agr Sci, Inst Edible Fungi, Shanghai 201403, Peoples R China

关键词： Volvariella volvacea; proteases; purification; soybean-isolate protein

期刊名称：JOURNAL OF FUNGI （ 影响因子：4.0； 五年影响因子：4.5 ）

ISSN：

年卷期： 2025 年 11 卷 3 期

页码：

收录情况： SCI

摘要： A novel protease was isolated from the fruiting bodies of the straw mushroom Volvariella volvacea. The protease was purified 13.48-fold using a series of techniques, including ammonium sulfate precipitation, ultrafiltration, diethylaminoethyl fast-flow (DEAE FF) ion-exchange chromatography, and Superdex 75 gel filtration chromatography, resulting in a specific enzyme activity of 286.82 U/mg toward casein as a substrate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) analysis revealed that the purified protease had a molecular weight of 24 kDa. The enzyme exhibited optimal activity at pH 7 and 50 degrees C, showing sensitivity to alkaline conditions and instability at elevated temperatures. The presence of Ca2+ significantly enhanced enzyme activity, whereas Ni2+ and Cu2+ exerted strong inhibitory effects, with other metal ions showing weak inhibition. beta-mercaptoethanol, Tween-80, and Triton X-100 had more pronounced inhibitory effects, whereas PMSF, EDTA, and CTAB had weaker inhibitory effects. The Michaelis constant (Km) and maximum velocity (Vm) of the protease were determined to be 1.34 g/L and 3.45 mu g/(mLmin), respectively. The protease exhibited a greater degree of enzymatic degradation of soybean-isolate protein (7.58%) compared to trypsin (5.24%), with the enzyme product containing a high percentage of medicinal amino acids (73.54%), particularly phenylalanine (Phe) and arginine (Arg), suggesting their presence at the enzyme's active site. These findings suggest that the protease from V. volvacea holds promising potential for applications in the food industry, particularly in protein hydrolysate production and flavor enhancement.

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