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- W2897712218 abstract "The hydrolysates of soy protein and milk protein are nutritional and functional food ingredients. Aspergillus pseudoglaucus aspergillopepsin I (App) is an acidic protease, including signal peptide, propeptide, and catalytic domain. Here, we cloned the catalytic domain App with or without propeptide in Escherichia coli. The results showed that the App without propeptide was not expressed or did not exhibit activity and App with propeptide (proApp) was highly expressed with a specific activity of 903 U/mg. Moreover, the denaturation temperature of proApp was 4.1 °C higher than App’s. The proApp showed 104 U/mg and 252 U/mg hydrolysis activities towards soy protein and milk protein under acidic conditions. By RP-HPLC analysis, the peptides obtained from the hydrolysates of soy protein and milk protein were hydrophilic peptides. This work first demonstrates efficient proteolysis of soy protein and milk protein through the functional expression of full-length proApp, which will likely have valuable industrial applications." @default.
- W2897712218 created "2018-10-26" @default.
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- W2897712218 date "2018-09-14" @default.
- W2897712218 modified "2023-10-16" @default.
- W2897712218 title "The high expression of <i>Aspergillus pseudoglaucus</i> protease in <i>Escherichia coli</i> for hydrolysis of soy protein and milk protein" @default.
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- W2897712218 doi "https://doi.org/10.1080/10826068.2018.1508035" @default.
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