Literature DB >> 7733957

Palladium--a new inhibitor of cellulase activities.

M D Shultz1, J P Lassig, M G Gooch, B R Evans, J Woodward.   

Abstract

Palladium complexes have been shown to strongly inhibit cellobiohydrolase I (CBH I) and endoglucanase II (EG II), two cellulases produced by Trichoderma reesei. Also inhibited were total cellulase (Avicelase) and beta-glucosidase (cellobiase) activities. The catalytic domain of CBH II, the second most abundant component of this cellulase, appeared less susceptible to inhibition by palladium. The inhibition was irreversible and could be prevented if histidine, cysteine or cystine was added to the enzyme reaction mixture simultaneously with the inhibitor. The binding of CBH I to microcrystalline cellulose (Avicel) was unaffected by palladium.

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Year:  1995        PMID: 7733957     DOI: 10.1006/bbrc.1995.1603

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

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Authors:  Alvin C M Kwok; Joseph T Y Wong
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4.  Use of substructure-specific carbohydrate binding modules to track changes in cellulose accessibility and surface morphology during the amorphogenesis step of enzymatic hydrolysis.

Authors:  Keith Gourlay; Valdeir Arantes; Jack N Saddler
Journal:  Biotechnol Biofuels       Date:  2012-07-24       Impact factor: 6.040

  4 in total

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