Cover Image

In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1

β-glucosidases (Bgl) are widely utilized for releasing non-reducing terminal glucosyl residues. Nevertheless, feedback inhibition by glucose end product has limited its application. A noticeable exception has been found for β-glucosidases of the glycoside hydrolase (GH) family 1, which exhibit toler...

Full description

Saved in:
Bibliographic Details
Main Authors: Mohamad Sobri, Mohamad Farhan, Abd Aziz, Suraini, Abu Bakar, Farah Diba, Ramli, Norhayati
Format: Article
Language:English
Published: Multidisciplinary Digital Publishing Institute 2020
Online Access:http://psasir.upm.edu.my/id/eprint/89405/1/SILICO.pdf
http://psasir.upm.edu.my/id/eprint/89405/
https://www.mdpi.com/1422-0067/21/11/4035
Tags: Add Tag
No Tags, Be the first to tag this record!
id my.upm.eprints.89405
record_format eprints
spelling my.upm.eprints.894052021-08-19T08:26:25Z http://psasir.upm.edu.my/id/eprint/89405/ In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1 Mohamad Sobri, Mohamad Farhan Abd Aziz, Suraini Abu Bakar, Farah Diba Ramli, Norhayati β-glucosidases (Bgl) are widely utilized for releasing non-reducing terminal glucosyl residues. Nevertheless, feedback inhibition by glucose end product has limited its application. A noticeable exception has been found for β-glucosidases of the glycoside hydrolase (GH) family 1, which exhibit tolerance and even stimulation by glucose. In this study, using local isolate Trichoderma asperellum UPM1, the gene encoding β-glucosidase from GH family 1, hereafter designated as TaBgl2, was isolated and characterized via in-silico analyses. A comparison of enzyme activity was subsequently made by heterologous expression in Escherichia coli BL21(DE3). The presence of N-terminal signature, cis-peptide bonds, conserved active site motifs, non-proline cis peptide bonds, substrate binding, and a lone conserved stabilizing tryptophan (W) residue confirms the identity of Trichoderma sp. GH family 1 β-glucosidase isolated. Glucose tolerance was suggested by the presence of 14 of 22 known consensus residues, along with corresponding residues L167 and P172, crucial in the retention of the active site’s narrow cavity. Retention of 40% of relative hydrolytic activity on ρ-nitrophenyl-β-D-glucopyranoside (ρNPG) in a concentration of 0.2 M glucose was comparable to that of GH family 1 β-glucosidase (Cel1A) from Trichoderma reesei. This research thus underlines the potential in the prediction of enzymatic function, and of industrial importance, glucose tolerance of family 1 β-glucosidases following relevant in-silico analyses. Multidisciplinary Digital Publishing Institute 2020 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/89405/1/SILICO.pdf Mohamad Sobri, Mohamad Farhan and Abd Aziz, Suraini and Abu Bakar, Farah Diba and Ramli, Norhayati (2020) In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1. International Journal of Molecular Sciences, 21 (11). art. no. 4035. pp. 1-23. ISSN 1661-6596; ESSN: 1422-0067 https://www.mdpi.com/1422-0067/21/11/4035 10.3390/ijms21114035
institution Universiti Putra Malaysia
building UPM Library
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Putra Malaysia
content_source UPM Institutional Repository
url_provider http://psasir.upm.edu.my/
language English
description β-glucosidases (Bgl) are widely utilized for releasing non-reducing terminal glucosyl residues. Nevertheless, feedback inhibition by glucose end product has limited its application. A noticeable exception has been found for β-glucosidases of the glycoside hydrolase (GH) family 1, which exhibit tolerance and even stimulation by glucose. In this study, using local isolate Trichoderma asperellum UPM1, the gene encoding β-glucosidase from GH family 1, hereafter designated as TaBgl2, was isolated and characterized via in-silico analyses. A comparison of enzyme activity was subsequently made by heterologous expression in Escherichia coli BL21(DE3). The presence of N-terminal signature, cis-peptide bonds, conserved active site motifs, non-proline cis peptide bonds, substrate binding, and a lone conserved stabilizing tryptophan (W) residue confirms the identity of Trichoderma sp. GH family 1 β-glucosidase isolated. Glucose tolerance was suggested by the presence of 14 of 22 known consensus residues, along with corresponding residues L167 and P172, crucial in the retention of the active site’s narrow cavity. Retention of 40% of relative hydrolytic activity on ρ-nitrophenyl-β-D-glucopyranoside (ρNPG) in a concentration of 0.2 M glucose was comparable to that of GH family 1 β-glucosidase (Cel1A) from Trichoderma reesei. This research thus underlines the potential in the prediction of enzymatic function, and of industrial importance, glucose tolerance of family 1 β-glucosidases following relevant in-silico analyses.
format Article
author Mohamad Sobri, Mohamad Farhan
Abd Aziz, Suraini
Abu Bakar, Farah Diba
Ramli, Norhayati
spellingShingle Mohamad Sobri, Mohamad Farhan
Abd Aziz, Suraini
Abu Bakar, Farah Diba
Ramli, Norhayati
In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1
author_facet Mohamad Sobri, Mohamad Farhan
Abd Aziz, Suraini
Abu Bakar, Farah Diba
Ramli, Norhayati
author_sort Mohamad Sobri, Mohamad Farhan
title In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1
title_short In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1
title_full In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1
title_fullStr In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1
title_full_unstemmed In-silico characterization of glycosyl hydrolase family 1 β glucosidase from Trichoderma asperellum UPM1
title_sort in-silico characterization of glycosyl hydrolase family 1 β glucosidase from trichoderma asperellum upm1
publisher Multidisciplinary Digital Publishing Institute
publishDate 2020
url http://psasir.upm.edu.my/id/eprint/89405/1/SILICO.pdf
http://psasir.upm.edu.my/id/eprint/89405/
https://www.mdpi.com/1422-0067/21/11/4035
_version_ 1709669010720686080
score 13.211869

Similar Items