NDLI: Characterization of a recombinant aryl β-glucosidase from Neosartorya fischeri NRRL181

Content Provider	Springer Nature Link
Author	Kalyani, Dayanand Lee, Kyoung Mi Tiwari, Manish Kumar Ramachandran, Priyadharshini Kim, Hoon Kim, In Won Jeya, Marimuthu Lee, Jung Kul
Copyright Year	2011
Abstract	An isolated gene from Neosartorya fischeri NRRL181 encoding a β-glucosidase (BGL) was cloned, and its nucleotide sequence was determined. DNA sequence analysis revealed an open reading frame of 1,467 bp, capable of encoding a polypeptide of 488 amino acid residues. The gene was over-expressed in Escherichia coli, and the protein was purified using nickel-nitrilotriacetic acid chromatography. The purified recombinant BGL showed a high level of catalytic activity, with V max of 886 μmol min−1 mg-protein−1 and a K m of 68 mM for p-nitrophenyl-β-d-glucopyranoside (pNPG). The optimal temperature for enzyme activity was about 40°C, and the optimal pH was about 6.0. A homology model of N. fischeri BGL1 was constructed based on the X-ray crystal structure of Phanerochaete chrysosporium BGLA. Molecular dynamics simulation studies of the enzyme with the pNPG and cellobiose shed light on the unique substrate specificity of N. fischeri BGL1 only towards pNPG.
Starting Page	413
Ending Page	423
Page Count	11
File Format	PDF
ISSN	01757598
Journal	Applied Microbiology and Biotechnology
Volume Number	94
Issue Number	2
e-ISSN	14320614
Language	English
Publisher	Springer-Verlag
Publisher Date	2011-11-01
Publisher Place	Berlin, Heidelberg
Access Restriction	Subscribed
Subject Keyword	Characterization β-Glucosidase Glycoside hydrolase family 1 Homology modeling Substrate specificity Microbiology Biotechnology Microbial Genetics and Genomics
Content Type	Text
Resource Type	Article
Subject	Medicine Applied Microbiology and Biotechnology Biotechnology

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