Purification and characterization of a low molecular weight endoxylanase from solid-state cultures of alkali-tolerant Aspergillus fischeri View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-08

AUTHORS

Sundar Rajan Senthilkumar, Balasubramaniem Ashokkumar, Krishnan Chandra Raj, Paramasamy Gunasekaran

ABSTRACT

A low molecular weight, alkaline-stable endoxylanase (XylB) was purified to homogeneity from solid-state culture of Aspergillus fischeri Fxn1. XylB had a molecular mass of 13 kDa which is the lowest of reported xylanases. Optimal activity was at pH 6 and 55 degrees C. XylB was stable from pH 4.5 to 10 and up to 60 degrees C. It was non-glycosylated. The apparent K(m) and V(max) values of XylB on birch wood xylan were 0.53 mg ml(-1) and 0.2 mmol min-1 mg-1, respectively. The activity of XylB was not inhibited by Cd2+, Zn2+, Co2+, EDTA, iodoacetamide, beta-mercaptoethanol and acetic anhydride but strongly inhibited by 10 mm of N-bromosuccinimide, Hg2+, Pb2+ and p-hydroxymercuric benzoate. XylB is an endoxylanase since it hydrolysed xylan resulting the formation of xylo-oligomers but not of xylose residues. More... »

PAGES

1283-1287

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/b:bile.0000044919.14176.de

DOI

http://dx.doi.org/10.1023/b:bile.0000044919.14176.de

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1010890221

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15483388


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