Method for characterization of the enzyme profile and the determination of CBH I (Cel 7a) core protein in Trichoderma reesei ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-08

AUTHORS

A. Zandoná Filho, M. Siika-Aho, L.P. Ramos

ABSTRACT

Fast protein liquid chromatography (FPLC) was used to characterize a commercial cellulase preparation (Celluclast 1.5L, Novozymes) in relation to its protein profile and activity against hydroxyethylcellulose (HEC) and other substrates. Co-elution of CBHII (Cel 6A) with other enzyme components of the cellulase system was characterized by immunochemical assays using monoclonal antibodies, whereas the occurrence of EGII (Cel 5A) was assessed based on its ability to cleave the heterosidic bond of 4-methylumbellyferyl-β-d-cellotrioside (MUmbG3). The main cellulase constituents of Celluclast 1.5L were pooled into six fractions containing EGII (Cel 5A) and EGIII (Cel 12A) (F1), EGII and CBHII (Cel 6A) (F2), CBHII and EGI (Cel 7B) (F3), EGI (F4), and CBHI (Cel 7A) (F5). The occurrence of CBHI core protein within the CBHI fraction of the FPLC profile was determined by hydrophobic interaction chromatography. Using this method, we were able to demonstrate that the batch of Celluclast 1.5L used in this study contained 10.9–18.8% of CBHI as its corresponding free core protein. More... »

PAGES

821-825

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11274-005-9109-x

DOI

http://dx.doi.org/10.1007/s11274-005-9109-x

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014989775


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