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Isolation and characterization of extracellular pectin lyase from Penicillium canescens

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Abstract

Pectin lyase A (molecular weight 38 kD by SDS-PAGE, pI 6.7) was purified to homogeneity from culture broth of the myoelial fungus Penicillium canescens using chromatographic techniques. During genomic library screening, the gene encoding pectin lyase A from P. canescens (pelA) was isolated and sequenced, and the amino acid sequence was generated by applying the multiple alignment procedure (360 residues). A theoretical model for the three dimensional structure of the protein molecule was also proposed. Different properties of pectin lyase A were investigated: substrate specificity, pH-and temperature optimum of activity, stability under different pH and temperature conditions, and the effect of Ca2+ on enzyme activity. In the course of the laboratory trials, it was demonstrated that pectin lyase A from P. canescens could be successfully applied to production and clarification of juice.

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Abbreviations

MD:

methylation degree

PGA:

polygalacturonic acid

pI :

isoelectric point

PL A, PL B:

pectin lyases A and B, respectively

RS:

reducing sugars

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Correspondence to O. A. Sinitsyna.

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Original Russian Text © O. A. Sinitsyna, E. A. Fedorova, M. V. Semenova, A. V. Gusakov, L. M. Sokolova, T. M. Bubnova, O. N. Okunev, A. M. Chulkin, E. A. Vavilova, Y. P. Vinetsky, A. P. Sinitsyn, 2007, published in Biokhimiya, 2007, Vol. 72, No. 5, pp. 699–706.

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Sinitsyna, O.A., Fedorova, E.A., Semenova, M.V. et al. Isolation and characterization of extracellular pectin lyase from Penicillium canescens . Biochemistry Moscow 72, 565–571 (2007). https://doi.org/10.1134/S0006297907050148

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  • DOI: https://doi.org/10.1134/S0006297907050148

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