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

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Ruminococcus
endo-1,4-beta-xylanase
Ruminococcus flavefaciens
Endo-1,4-beta Xylanases
Carboxymethylcellulose Sodium
Bacteriophages
Cellulase
carboxymethylcellulose
Cloning
xylanases
endo-1,4-beta-glucanase
bacteriophages
Escherichia coli
Organism Cloning
molecular cloning
Cellulose
Enzymes
Clone Cells
clones
Native Polyacrylamide Gel Electrophoresis

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Animal Science and Zoology

Cite this

Cloning In Escherichia Coli of A Bi-Functional Cellulase/Xylanase Enzyme from Ruminococcus flavefaciens Fd-1. / Howard, Gary T.; White, Bryan A.

In: Animal Biotechnology, Vol. 1, No. 1, 01.1990, p. 95-106.

Research output: Contribution to journalArticle

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