Properties and Chemical Modification of Lipase from Trichosporon sp.

Abstract:

A lipase from Trichosporon sp. screened by my lab was purified to homogeneity by ammonia sulphate precipitation and a series of chromatographic steps. The properties of purified Trichosporon sp. Lipase were investigated. Its Molecular weight and isoelectric point were 28kD and pH 8.7, the optimum temperature and pH were 40℃ and pH 8.0. Several chemical modification agents were applied to investigate amino acid residues in active site of this enzyme and the results demonstrated that histidine, serine, glutamic acid/asparaginic acid are located in the active site. The composition of amino acid of the enzyme was also analyzed，which indicated that the contents of asparaginic acid, serine, glutamic acid, glycin, alanine are the most, lysine, histidine also have high contents and there are a few praline, tryptophan.