Adsorption and reactions of chitinase and lysozyme on chitin

  title={Adsorption and reactions of chitinase and lysozyme on chitin},
  author={John Skujins and A. H. Pukite and A. D. Mclaren},
  journal={Molecular and Cellular Biochemistry},
SummaryIsotherms for adsorption of chitinase on chitin and lysozyme on chitin have been determined at two temperatures and rates of hydrolysis of chitin catalysed by these enzymes have been measured at three temperatures and at several enzyme concentrations for each. Ribonuclease, not an enzyme for chitin, and heat-denatured lysozyme and chitinase show reduced or no adsorption to this substrate.Initial hydrolysis rates of chitin by both enzymes are proportional to total enzyme concentrations in… 
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Enzymic digestion, acidic hydrolysis, deuterium exchange, infrared absorption spectra, and differential thermal analysis of chitins show that not only do the structures of <x- and ~-chitins differ
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The mode of action of muramidase on glycol chitin was investigated following the degradation of glycol Chitin by the estimation of reducing power produced by hydrolysis and the optimum temperature as well as pH were found to lie at 50°C and pH 5 respectively, which nearly agree with those obtained by α viscosimetric determination of mur amidase activity.
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Structure of Some Crystalline Lysozyme-Inhibitor Complexes Determined by X-Ray Analysis At 6 Å Resolution
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