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• W3174393313 abstract "A strain of Aspergillus ochraceus was isolated from the stored low denatured soybean meals (LDSMs) and an extracellular protease was purified from the fungus grown culture to electrophoretical homogeneity. The protease had a molecular weight of approximately 70 kDa and showed proteolytic activities only in the presence of activators. The maximum activity was obtained in 1.4% sodium dodecyl sulfate (SDS) solution but similar activity could also be achieved in the presence of linoleic acid at the concentration as low as 0.05%. The protease was stable at pH 9.0–12.0 and remained active in the presence of methanol, ethanol, acetone and trichloromethane and was classified as serine protease. The thermal stability of the protease located in the temperature range of 4–40 °C and an activator independent autolysis was observed above 60 °C. Soy proteins was hydrolyzed by the purified protease in a model system using residual lipids from stored LDSMs as the activator and a degree of hydrolysis (DH) of 6.01% ± 0.27 was obtained after reaction for 60 min at pH 9.0 and 40 °C. This study gives new insights into the quality control of the soy protein production and the use of fungal proteases in the modification of soy proteins. • Aspergillus ochraceus was screened from the aged low denatured defatted soybean meal. • A extracellular serine protease was isolated from the grown culture of the Aspergillus ochraceus. • The protease showed extraodinary properties comparing with other proteases. • Soy proteins of aged LDSM can be hydrolyzed under alkali condition and mild temperature." @default.
• W3174393313 created "2021-07-05" @default.
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• W3174393313 date "2021-10-01" @default.
• W3174393313 modified "2023-09-29" @default.
• W3174393313 title "Isolation and characterization of an activator-dependent protease from Aspergillus ochraceus screened from low denatured defatted soybean meal and the proteolysis of soy proteins" @default.
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• W3174393313 doi "https://doi.org/10.1016/j.lwt.2021.112026" @default.
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