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Studies on cellulose hydrolysis by Acetivibrio cellulolyticus

AuteurRechercher : 1; Rechercher : 2; Rechercher : 1
Affiliation
  1. Conseil national de recherches Canada
  2. Conseil national de recherches Canada. Institut des sciences biologiques du CNRC
FormatTexte, Article
Résumé
Acetivibrio cellulolyticus extracellular cellulase extensively hydrolyzed crystalline celluloses such as Avicel (FMC Corp., Food and Pharmaceutical Products Div., Philadelphia, Pa.) but only if it was desalted and supplemented with Ca. The Ca effect was one of increased enzyme stability in the presence of the ion. Although preincubation of the cellulase complex at 40 degrees C for 5 h without added Ca had a negligible effect on endoglucanase activity or on the subseqent hydrolysis of amorphous cellulose, the capacity of the enzyme to hydrolyze crystalline cellulose was almost completely lost. Adsorption studies showed that 90% of the Avicel-solubilizing component of the total enzyme preparation bound to 2% Avicel at 40 degrees C. Under these conditions, only 15% of the endoglucanase and 25% of the protein present in the enzyme preparation adsorbed to the substrate. The protein profile of the bound enzyme, as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was complex and distinctly different from the profile observed for total cellulase preparations. The specific activity of A. cellulolyticus cellulase with respect to Avicel hydrolysis was compared with that of commercially available Trichoderma reesei cellulase.
Date de publication
Dans
  • Applied and Environmental Microbiology 50 (1985) : 243–248.
Langueanglais
Numéro du CNRCMACKENZIE1985
NRCC 24532
Numéro NPARC9365587
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Identificateur de l’enregistrement854abb2e-d615-4077-bbf0-acf0a7b48614
Enregistrement créé2009-07-10
Enregistrement modifié2020-03-17

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