Purification, characterization, and substrate specificities of multiple xylanases from Streptomyces sp. strain B-12-2

G. Elegir, G. Szakács, T. W. Jeffries

Research output: Contribution to journalArticle

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Abstract

The endoxylanase complex from Streptomyces sp. strain B-12-2 was purified and characterized. The organism forms five distinct xylanases in the absence of significant cellulase activity when grown on oat spelt xylan. This is the largest number of endoxylanases yet reported for a streptomycete. On the basis of their physiochemical characteristics, they can be divided into two groups: the first group (xyl 1a and xyl 1b) consists of low-molecular-mass (26.4 and 23.8 kDa, respectively) neutral- to high-pI (6.5 and 8.3, respectively) endoxylanases. Group 1 endoxylanases are unable to hydrolyze aryl-β-D-cellobioside, have low levels of activity against xylotetraose (X4) and limited activity against xylopentaose, produce little or no xylose, and form products having a higher degree of polymerization with complex substrates. These enzymes apparently carry out transglycosylation. The second group (xyl 2, xyl 3, and xyl 4) consists of high-molecular-mass (36.2, 36.2, and 40.5 kDa, respectively), low-pI (5.4, 5.0, and 4.8, respectively) xylanases. Group 2 endoxylanases are able to hydrolyze aryl-β-D- cellobioside, show higher levels of activity against X4, and hydrolyze xylopentaose completely with the formation of xylobiose and xylotriose plus limited amounts of X4 and xylose. The enzymes display intergroup synergism when acting on kraft pulp. Despite intragroup similarities, each enzyme exhibited a unique action pattern and physiochemical characteristic. xyl 2 was highly glycosylated, and xyl 1b (but no other enzyme) was completely inhibited by p-hydroxymercuribenzoate.

Original languageEnglish
Pages (from-to)2609-2615
Number of pages7
JournalApplied and Environmental Microbiology
Volume60
Issue number7
Publication statusPublished - 1994

Fingerprint

endo-1,4-beta-xylanase
Endo-1,4-beta Xylanases
Streptomyces
xylanases
substrate specificity
Substrate Specificity
purification
enzyme
substrate
Xylose
Enzymes
enzymes
xylose
Organism Forms
synergism
Triticum aestivum subsp. spelta
molecular weight
Xylans
kraft pulp
polymerization

ASJC Scopus subject areas

  • Environmental Science(all)
  • Biotechnology
  • Microbiology

Cite this

Purification, characterization, and substrate specificities of multiple xylanases from Streptomyces sp. strain B-12-2. / Elegir, G.; Szakács, G.; Jeffries, T. W.

In: Applied and Environmental Microbiology, Vol. 60, No. 7, 1994, p. 2609-2615.

Research output: Contribution to journalArticle

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