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-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 degrees C, and the pectin lyase was found to be completely stable up to 40 degrees C when exposed for 1 h. The purified pectin lyase was found efficient in retting of Linum usitatissimum, Cannabis sativa, and Crotalaria juncea.
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Department of Chemistry, D. D. U. Gorakhpur University, Gorakhpur 273009, India. sangeeta_rahul@rediffmail.com
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D004795:Enzyme Stability; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D010407:Penicillium / Q000737:chemistry / Q000201:enzymology*; D011133:Polysaccharide-Lyases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D005656:Fungal Proteins; D011133:Polysaccharide-Lyases; C027349:pectin lyase