2004AFRICAN JOURNAL OF BIOTECHNOLOGYOpen access

Mutation induced enhanced biosynthesis of lipase

K. V. V. S. N. Bapiraju, P. Sujatha, P Ellaiah, T. Ramana

Open full text 49 citations

Abstract

The purpose of the present investigation is to enhance production of biomedically important enzyme lipase by subjecting the indigenous lipase producing strain Rhizopus sp. BTS-24 to improvement by natural selection and random mutagenesis (UV and N-methyl-N'-nitro-N-nitroso guanidine, NTG). The isolation of mutants and the lipolytic activity of selected mutants were described. The best natural selectant BTNS 12 showed 110% higher lipase activity than the wild strain (BTS-24). The lipase yield of the best UV mutant BTUV3 was 164% higher than the parent strain (BTNS 12 ) and 180% times higher than the wild strain (BTS-24). Also, the lipase yield of the best NTG mutant BTNT 2 was 133 % higher than the parent strain (BTUV 3 ) and 232% higher than the wild strain (BTS-24). The results indicated that UV and NTG were effective mutagenic agents for strain improvement of Rhizopus sp . BTS-24 for enhanced lipase productivity. Key Words: Lipase, Rhizopus, UV, NTG. African Journal of Biotechnology Vol.3(11) 2004: 618-621

About this research paper

What this paper is about

The purpose of the present investigation is to enhance production of biomedically important enzyme lipase by subjecting the indigenous lipase producing strain Rhizopus sp. BTS-24 to improvement by natural selection and random mutagenesis (UV and N-methyl-N'-nitro-N-nitroso guanidine, NTG). The isolation of mutants and the lipolytic activity of selected mutants were described. The best natural selectant BTNS 12 showed 110% higher lipase activity than the wild strain (BTS-24). The lipase yield of the best UV mutant BTUV3 was 164% higher than the parent strain (BTNS 12 ) and 180% times higher than the wild strain (BTS-24). Also, the lipase yield of the best NTG mutant BTNT 2 was 133 % higher than the parent strain (BTUV 3 ) and 232% higher than the wild strain (BTS-24). The results indicated that UV and NTG were effective mutagenic agents for strain improvement of Rhizopus sp . BTS-24 for enhanced lipase productivity. Key Words: Lipase, Rhizopus, UV, NTG. African Journal of Biotechnology Vol.3(11) 2004: 618-621

Why it matters

OpenAlex reports 49 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

The purpose of the present investigation is to enhance production of biomedically important enzyme lipase by subjecting the indigenous lipase producing strain Rhizopus sp. BTS-24 to improvement by natural selection and random mutagenesis (UV and N-methyl-N'-nitro-N-nitroso guanidine, NTG). The isolation of mutants and the lipolytic activity of selected mutants were described. The best natural selectant BTNS 12 showed 110% higher lipase activity than the wild strain (BTS-24). The lipase yield of the best UV mutant BTUV3 was 164% higher than the parent strain (BTNS 12 ) and 180% times higher than the wild strain (BTS-24). Also, the lipase yield of the best NTG mutant BTNT 2 was 133 % higher than the parent strain (BTUV 3 ) and 232% higher than the wild strain (BTS-24). The results indicated that UV and NTG were effective mutagenic agents for strain improvement of Rhizopus sp . BTS-24 for enhanced lipase productivity. Key Words: Lipase, Rhizopus, UV, NTG. African Journal of Biotechnology Vol.3(11) 2004: 618-621

Key concepts: Lipase, Mutant, Strain (injury), Rhizopus, Mutagenesis, Guanidine, Biochemistry, Enzyme

Related papers

Back to paper searchBrowse research topicsOriginal source
Mutation induced enhanced biosynthesis of lipase — Research Paper | ScholarLens