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The xylan-degrading enzyme system of Talaromyces emersonii : novel enzymes with activity against aryl β-D-xylosides and unsubstituted xylans

(1993) BIOCHEMICAL JOURNAL. 290(2). p.515-523
Author
Organization
Abstract
Talaromyces emersonii, a thermophilic aerobic fungus, produces a complete xylan-degrading enzyme system when grown on appropriate substrates. In this paper we present the physicochemical and catalytic properties of three enzymes, xylosidase (Xy1) I (M, 181 000; pI 8.9), II (M, 131 000; pl 5.3) and III (M(r) 54200; pI 4.2). Xyl I and II appear to be dimeric and Xyl III is a single-subunit protein. All three enzymes catalyse the hydrolysis of aryl beta-D-xylosides and xylo-oligosaccharides. Xyl I is a classic beta-xylosidase (1,4-beta-D-Xylan xylohydrolase; EC 3.2.1.37), and Xyl II and III are novel xylanases (endo- 1,4-beta-D-xylan xylanohydrolase; EC 3.2.1.8) which we believe have not hitherto been reported. In addition to the above substrates, they also catalyse the extensive hydrolysis of unsubstituted xylans, and may have considerable biotechnological potential. The hydrolysis product profiles and bond-cleavage frequencies with various substrates are presented.
Keywords
ASPERGILLUS-NIGER, ESCHERICHIA-COLI, STREPTOMYCES-LIVIDANS, THERMOSTABLE XYLANASE, CERATOCYSTIS-PARADOXA, CRYPTOCOCCUS-ALBIDUS, PURIFICATION, DEGRADATION, EXPRESSION, IDENTIFICATION

Citation

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Chicago
Tuohy, MG, J Puls, Marc Claeyssens, M Vršanská, and MP Coughlan. 1993. “The Xylan-degrading Enzyme System of Talaromyces Emersonii : Novel Enzymes with Activity Against Aryl β-D-xylosides and Unsubstituted Xylans.” Biochemical Journal 290 (2): 515–523.
APA
Tuohy, M., Puls, J., Claeyssens, M., Vršanská, M., & Coughlan, M. (1993). The xylan-degrading enzyme system of Talaromyces emersonii : novel enzymes with activity against aryl β-D-xylosides and unsubstituted xylans. BIOCHEMICAL JOURNAL, 290(2), 515–523.
Vancouver
1.
Tuohy M, Puls J, Claeyssens M, Vršanská M, Coughlan M. The xylan-degrading enzyme system of Talaromyces emersonii : novel enzymes with activity against aryl β-D-xylosides and unsubstituted xylans. BIOCHEMICAL JOURNAL. 1993;290(2):515–23.
MLA
Tuohy, MG, J Puls, Marc Claeyssens, et al. “The Xylan-degrading Enzyme System of Talaromyces Emersonii : Novel Enzymes with Activity Against Aryl β-D-xylosides and Unsubstituted Xylans.” BIOCHEMICAL JOURNAL 290.2 (1993): 515–523. Print.
@article{201241,
  abstract     = {Talaromyces emersonii, a thermophilic aerobic fungus, produces a complete xylan-degrading enzyme system when grown on appropriate substrates. In this paper we present the physicochemical and catalytic properties of three enzymes, xylosidase (Xy1) I (M, 181 000; pI 8.9), II (M, 131 000; pl 5.3) and III (M(r) 54200; pI 4.2). Xyl I and II appear to be dimeric and Xyl III is a single-subunit protein. All three enzymes catalyse the hydrolysis of aryl beta-D-xylosides and xylo-oligosaccharides. Xyl I is a classic beta-xylosidase (1,4-beta-D-Xylan xylohydrolase; EC 3.2.1.37), and Xyl II and III are novel xylanases (endo- 1,4-beta-D-xylan xylanohydrolase; EC 3.2.1.8) which we believe have not hitherto been reported. In addition to the above substrates, they also catalyse the extensive hydrolysis of unsubstituted xylans, and may have considerable biotechnological potential. The hydrolysis product profiles and bond-cleavage frequencies with various substrates are presented.},
  author       = {Tuohy, MG and Puls, J and Claeyssens, Marc and Vr\v{s}ansk{\'a}, M and Coughlan, MP},
  issn         = {0264-6021},
  journal      = {BIOCHEMICAL JOURNAL},
  language     = {eng},
  number       = {2},
  pages        = {515--523},
  title        = {The xylan-degrading enzyme system of Talaromyces emersonii : novel enzymes with activity against aryl \ensuremath{\beta}-D-xylosides and unsubstituted xylans},
  url          = {http://dx.doi.org/10.1042/bj2900515},
  volume       = {290},
  year         = {1993},
}

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