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- W1995319348 abstract "The hydrolytic activity of the purified yeast lipase OF 360 was greatly decreased by heating above 45°C and the residual activity after heating at 50°C for 15 min was about one-tenth of the original. Treatment of the lipase with a bifunctional reagent, dimethyl suberimidate (DMS), increased the heat stability. Stabilization by DMS treatment was supposed to be caused by non-covalent interaction between the lipase and DMS through electrostatic and/or hydrophobic forces. In addition, analysis of FT-IR spectra of the DMS- and non-treated lipases suggested that the main skeleton of the treated lipase was little perturbed by heating." @default.
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- W1995319348 date "1990-01-01" @default.
- W1995319348 modified "2023-09-23" @default.
- W1995319348 title "Effects of non-covalent interaction of dimethyl suberimidate on lipase stability." @default.
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- W1995319348 doi "https://doi.org/10.1271/bbb1961.54.2605" @default.
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