Purification and characterization of pectin lyase secreted by Penicillium citrinum

The importance of various parameters such as sugarcane juice concentration, pH of the medium, and effects of different solid supports for maximum secretion of pectin lyase from Penicillium citrinum MTCC 8897 has been studied. The enzyme was purified to homogeneity by Sephadex G-100 and DEAE-cellulos...

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Bibliographic Details
Published in:Biochemistry (Moscow) 2009-07, Vol.74 (7), p.800-806
Main Authors: Yadav, S, Yadav, P. K, Yadav, D, Yadav, K. D. S
Format: Article
Language:English
Subjects:
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Cellulose
Enzyme Stability
Enzymes
Fungal Proteins - chemistry
Fungal Proteins - isolation & purification
Fungal Proteins - metabolism
Kinetics
Life Sciences
Microbiology
Molecular Weight
Penicillium - chemistry
Penicillium - enzymology
Polysaccharide-Lyases - chemistry
Polysaccharide-Lyases - isolation & purification
Polysaccharide-Lyases - metabolism
Substrate Specificity
Sugarcane
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Summary:The importance of various parameters such as sugarcane juice concentration, pH of the medium, and effects of different solid supports for maximum secretion of pectin lyase from Penicillium citrinum MTCC 8897 has been studied. The enzyme was purified to homogeneity by Sephadex G-100 and DEAE-cellulose chromatography. The molecular mass determined by SDS-PAGE was 31 kDa. The K m and k cat values were found to be 1 mg/ml and 76 sec⁻¹, respectively. The optimum pH of the purified pectin lyase was 9.0, though it retains activity in the pH 9.0-12.0 range when exposed for 24 h. The optimum temperature was 50°C, and the pectin lyase was found to be completely stable up to 40°C when exposed for 1 h. The purified pectin lyase was found efficient in retting of Linum usitatissimum, Cannabis sativa, and Crotalaria juncea.
ISSN:0006-2979
1608-3040
DOI:10.1134/S0006297909070141