Cloning In Escherichia Coli of A Bi-Functional Cellulase/Xylanase Enzyme from Ruminococcus flavefaciens Fd-1

Gary T. Howard, Bryan A White

Research output: Contribution to journalArticle

Abstract

A genomic library of Ruminococcus flavefaciens FD-1 DNA was constructed using the Escherichia coli bacteriophage λ vector λDASH. A recombinant phage exhibiting activity against both Ostazin brilliant red-hydroxyethyl cellulose (OBR-HEC) and carboxymethyl cellulose (CMC) was isolated. This clone (designated FD1-1) was further analyzed by restriction endonuclease mapping and Southern blot. analysis. Substrate specificity data shows that the cloned gene(s) encodes both endoglucanase activity and endoxylanase activity. CMC and xylan zymograms of protein(s) produced by this clone and then separated by non-denaturing PAGE suggest that the endoglucanase/endoxylanase activities reside on the same polypeptide or protein complex. An additional xylanase product lacking CMCase activity was also detected.

Original languageEnglish (US)
Pages (from-to)95-106
Number of pages12
JournalAnimal Biotechnology
Volume1
Issue number1
DOIs
StatePublished - Jan 1990

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Animal Science and Zoology

Fingerprint Dive into the research topics of 'Cloning In Escherichia Coli of A Bi-Functional Cellulase/Xylanase Enzyme from Ruminococcus flavefaciens Fd-1'. Together they form a unique fingerprint.

  • Cite this