Purification and characterization of an alkaline lipase from a newly isolated Acinetobacter radioresistens CMC-1

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Abstract

A novel alkaline lipase showing a broad range of specificity towards long chain triacylglycerols or p-nitrophenyl esters was purified to homogeneity from Acinetobacter radioresistens CMC-1. Its molecular mass was 45 kDa (by SDS-PAGE), pI of approx. 5.2, and optimally activity at 10.5 and 40°C. Using triolein as substrate, the lipase showed 1,3-positional specificity for hydrolyzing ester bonds. The enzyme was activated in 40% (v/v) dimethylsulfoxide and 20% (v/v) dimethylformamide.

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