Cloning and expression of an endoglucanase gene from the thermotolerant fungus Aspergillus fumigatus DBiNU-1 in Kluyveromyces lactis
Braz. j. microbiol
;
49(3): 647-655, July-Sept. 2018. graf
Article
in English
| LILACS
| ID: biblio-951810
ABSTRACT
Abstract An intronless endoglucanase from thermotolerant Aspergillus fumigatus DBINU-1 was cloned, characterized and expressed in the yeast Kluyveromyces lactis. The full-length open reading frame of the endoglucanase gene from A. fumigatus DBiNU-1, designated Cel7, was 1383 nucleotides in length and encoded a protein of 460 amino acid residues. The predicted molecular weight and the isoelectric point of the A. fumigatus Cel7 gene product were 48.19 kDa and 5.03, respectively. A catalytic domain in the N-terminal region and a fungal type cellulose-binding domain/module in the C-terminal region were detected in the predicted polypeptide sequences. Furthermore, a signal peptide with 20 amino acid residues at the N-terminus was also detected in the deduced amino acid sequences of the endoglucanase from A. fumigatus DBiNU-1. The endoglucanase from A. fumigatus DBiNU-1 was successfully expressed in K. lactis, and the purified recombinant enzyme exhibited its maximum activity at pH 5.0 and 60 °C. The enzyme was very stable in a pH range from 4.0 to 8.0 and a temperature range from 30 to 60 °C. These features make it suitable for application in the paper, biofuel, and other chemical production industries that use cellulosic materials.
Full text:
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Index:
LILACS (Americas)
Main subject:
Aspergillus fumigatus
/
Fungal Proteins
/
Gene Expression
/
Cellulase
/
Cloning, Molecular
Language:
English
Journal:
Braz. j. microbiol
Journal subject:
Microbiology
Year:
2018
Type:
Article
Affiliation country:
Thailand
Institution/Affiliation country:
Khon Kaen University/TH
/
Mahasarakham University/TH
/
Naresuan University/TH
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