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Purification of the cellulase complex produced byPenicillium camemberti and its partial characterization

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Abstract

Three cellulase components (FP-ase, CMC-ase and cellobiase) were purified by affinity binding on Avicel followed by Sephadex G-25, DEAE-Sepharose, DEAE-cellulose and Sephadex G-100 chromatography from the culture filtrate of the newly isolated strainPenicillium camemberti. The isolated enzymes had the properties of cellobiohydrolase, endo-1,4-β-d-glucanase and cellobiase and their respective molar masses were 99, 87 and 61 kDa as determined by molecular sieve chromatography on Sephadex G-100. The amino acid composition of each fraction was also determined.

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Authors and Affiliations

  1. Institute of Industrial Microbiology, Korean Academy of Sciences, Pchen-Song, D.P.R. of Korea

    Jun Choi Won, Min Ma Zengh & Sel Kang Mek

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  1. Jun Choi Won
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  2. Min Ma Zengh
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  3. Sel Kang Mek
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Choi Won, J., Ma Zengh, M. & Kang Mek, S. Purification of the cellulase complex produced byPenicillium camemberti and its partial characterization. Folia Microbiol 37, 199–204 (1992). https://doi.org/10.1007/BF02933147

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  • DOI: https://doi.org/10.1007/BF02933147

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