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- W2096152028 abstract "Abstract An extracellular endopolygalacturonase from extracts of solid-state cultures of Phanerochaete chrysosporium was purified to homogeneity as judged by electrophoresis under denaturing conditions. The purified enzyme preparation is a single subunit glycoprotein with an Mr value of 41 700 and is comprised of three isoenzymes with pI values of 4.26, 4.46 and 4.64, respectively. It is active against polygalacturonic acid, oligogalacturonates, and to a lesser extent against pectins. Activity against the latter substrates decreases with increasing degree of methyl esterification. The enzyme readily catalyzes the hydrolysis of oligomers from tetramers upwards but acts only slowly against trimers and not at all against dimers. Examination of the pattern of products released from various substrates including oligomers suggested that the active site is comprised of six subsites. The Km for polygalacturonate is 2.5 mg ml−1, the kcat is 440 s−1, the Hill coefficient is 1.04 and the Ea value is 33.4 kJ mol−1. The temperature and pH optima under assay conditions are 66°C and 4.7, respectively. The half-life of the enzyme at pH 5.0, 60°C is 14.5 min." @default.
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- W2096152028 date "1993-04-01" @default.
- W2096152028 modified "2023-09-30" @default.
- W2096152028 title "Isolation and characterization of an endopolygalacturonase from Phanerochaete chrysosporium" @default.
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- W2096152028 doi "https://doi.org/10.1016/0168-1656(93)90169-n" @default.
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