Enzymatic properties and intracellular localization of the novel Trichoderma reesei β-glucosidase BGLII (Cel1A)

Markku Saloheimo (Corresponding Author), Juha Kuja-Panula, Erkko Ylösmäki, Michael Ward, Merja Penttilä

Research output: Contribution to journalArticleScientificpeer-review

126 Citations (Scopus)

Abstract

This paper describes the characterization of an intracellular β-glucosidase enzyme BGLII (Cel1a) and its gene (bgl2) from the cellulolytic fungus Trichoderma reesei (Hypocrea jecorina). The expression pattern of bgl2 is similar to that of other cellulase genes known from this fungus, and the gene would appear to be under the control of carbon catabolite repression mediated by the cre1 gene. The BGLII protein was produced in Escherichia coli, and its enzymatic properties were analyzed. It was shown to be a specific β-glucosidase, having no β-galactosidase side activity. It hydrolyzed both cellotriose and cellotetraose. BGLII exhibited transglycosylation activity, producing mainly cellotriose from cellobiose and sophorose and cellobiose from glucose. Antibodies raised against BGLII showed the presence of the enzyme in T. reesei cell lysates but not in the culture supernatant. Activity measurements and Western blot analysis of T. reesei strains expressing bgl2 from a constitutive promoter further confirmed the intracellular localization of this β-glucosidase.

Original languageEnglish
Pages (from-to)4546-4553
JournalApplied and Environmental Microbiology
Volume68
Issue number9
DOIs
Publication statusPublished - 1 Sep 2002
MoE publication typeA1 Journal article-refereed

Fingerprint

Glucosidases
Trichoderma reesei
glucosidases
Trichoderma
Cellobiose
cellobiose
gene
Genes
Hypocrea
Fungi
genes
fungus
Galactosidases
enzyme
Catabolite Repression
galactosidases
fungi
Cellulase
Enzymes
enzymes

Keywords

  • antibodies
  • Enzymes
  • Escherichia coli
  • fungi
  • genes
  • eukaryota
  • Hypocrea jecorina
  • Trichoderma
  • Cellulase
  • glucose
  • sophorose

Cite this

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title = "Enzymatic properties and intracellular localization of the novel Trichoderma reesei β-glucosidase BGLII (Cel1A)",
abstract = "This paper describes the characterization of an intracellular β-glucosidase enzyme BGLII (Cel1a) and its gene (bgl2) from the cellulolytic fungus Trichoderma reesei (Hypocrea jecorina). The expression pattern of bgl2 is similar to that of other cellulase genes known from this fungus, and the gene would appear to be under the control of carbon catabolite repression mediated by the cre1 gene. The BGLII protein was produced in Escherichia coli, and its enzymatic properties were analyzed. It was shown to be a specific β-glucosidase, having no β-galactosidase side activity. It hydrolyzed both cellotriose and cellotetraose. BGLII exhibited transglycosylation activity, producing mainly cellotriose from cellobiose and sophorose and cellobiose from glucose. Antibodies raised against BGLII showed the presence of the enzyme in T. reesei cell lysates but not in the culture supernatant. Activity measurements and Western blot analysis of T. reesei strains expressing bgl2 from a constitutive promoter further confirmed the intracellular localization of this β-glucosidase.",
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Enzymatic properties and intracellular localization of the novel Trichoderma reesei β-glucosidase BGLII (Cel1A). / Saloheimo, Markku (Corresponding Author); Kuja-Panula, Juha; Ylösmäki, Erkko; Ward, Michael; Penttilä, Merja.

In: Applied and Environmental Microbiology, Vol. 68, No. 9, 01.09.2002, p. 4546-4553.

Research output: Contribution to journalArticleScientificpeer-review

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