An engineered Aspergillus fumigatus GH3 β-glucosidase with higher glucose tolerance
β-glucosidases (3.2.1.21) are present in all domains of living organisms, and their importance in a number of essential biological processes and industrial applications has been highlighted. They are interesting for biomass conversion because b-glucans are the world’s largest source of biomass. For...
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| Veröffentlicht in: | Bioresources 2022-05, Vol.17 (2), p.3057-3066 |
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| creator | Nazir, Sidrah Asad, Muhammad Javaid Naqvi, Syed Muhammad Saqlan Zainab, Tayyaba Malik, Saad Imran Mehmood, Raja Tahir Khan, Jehangir Sultana, Tasawar Nasir, Nazim Hassan, Atiq |
| description | β-glucosidases (3.2.1.21) are present in all domains of living organisms, and their importance in a number of essential biological processes and industrial applications has been highlighted. They are interesting for biomass conversion because b-glucans are the world’s largest source of biomass. For this reason, several fungal β-glucosidases have been investigated. The β-glucosidase gene of Aspergillus fumigatus, as well as its mutants D262E and W263F, were cloned and expressed in Pichia pastoris in this study. Their optimum temperature, pH, glucose tolerance, metal ion effect, and Vmax, km, and kcat were determined. The optimal temperature for recombinant β-glucosidase was 65 °C. For mutant D262E, there is an improvement in pH stability ranging from 4 to 6. As compared to the D262E mutant and recombinant β-glucosidase, mutant W263F showed a higher glucose tolerance and kcat. |
| doi_str_mv | 10.15376/biores.17.2.3057-3066 |
| format | Article |
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They are interesting for biomass conversion because b-glucans are the world’s largest source of biomass. For this reason, several fungal β-glucosidases have been investigated. The β-glucosidase gene of Aspergillus fumigatus, as well as its mutants D262E and W263F, were cloned and expressed in Pichia pastoris in this study. Their optimum temperature, pH, glucose tolerance, metal ion effect, and Vmax, km, and kcat were determined. The optimal temperature for recombinant β-glucosidase was 65 °C. For mutant D262E, there is an improvement in pH stability ranging from 4 to 6. As compared to the D262E mutant and recombinant β-glucosidase, mutant W263F showed a higher glucose tolerance and kcat.</description><identifier>ISSN: 1930-2126</identifier><identifier>EISSN: 1930-2126</identifier><identifier>DOI: 10.15376/biores.17.2.3057-3066</identifier><language>eng</language><publisher>Raleigh: North Carolina State University</publisher><subject>Amino acids ; Aspergillus fumigatus ; Biological activity ; Biomass ; Cellulase ; Cellulose ; Enzymes ; Genes ; Glucans ; Glucose ; Glucose tolerance ; Glucosidase ; Industrial applications ; Lignocellulose ; Metal ions ; Mutagenesis ; Mutants ; Mutation ; Optimization ; pH effects ; Plasmids ; Proteins ; Temperature tolerance ; β-Glucosidase</subject><ispartof>Bioresources, 2022-05, Vol.17 (2), p.3057-3066</ispartof><rights>2022. 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As compared to the D262E mutant and recombinant β-glucosidase, mutant W263F showed a higher glucose tolerance and kcat.</description><subject>Amino acids</subject><subject>Aspergillus fumigatus</subject><subject>Biological activity</subject><subject>Biomass</subject><subject>Cellulase</subject><subject>Cellulose</subject><subject>Enzymes</subject><subject>Genes</subject><subject>Glucans</subject><subject>Glucose</subject><subject>Glucose tolerance</subject><subject>Glucosidase</subject><subject>Industrial applications</subject><subject>Lignocellulose</subject><subject>Metal ions</subject><subject>Mutagenesis</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Optimization</subject><subject>pH effects</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Temperature tolerance</subject><subject>β-Glucosidase</subject><issn>1930-2126</issn><issn>1930-2126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNpNkM1KxDAUhYMoOI6-ggRct-ZnkrTLMuiMMOBmXIckve1k6LQ1aRFfywfxmexYFy4u93A43Hv4ELqnJKWCK_lofRcgplSlLOVEqIQTKS_QguacJIwyeflPX6ObGI-ErDJOyQLtixZDW_sWIECJi9hDqH3TjBFX48nXZpjUZsvx91dSN6Proi9NBPzhhwM--PoAAc8-4KFrIJjWwS26qkwT4e5vL9Hb89N-vU12r5uXdbFL3FRHJlZZa1cguYS8VCIjpQJwFla5MZnhzGWWMJJzzoQwrKzY5FVOCSYF4WKaJXqY7_ahex8hDvrYjaGdXmqmpKRCUSGnlJxTLnQxBqh0H_zJhE9Nif4lqGeCmirN9JmgPhPkP1RLZus</recordid><startdate>20220514</startdate><enddate>20220514</enddate><creator>Nazir, Sidrah</creator><creator>Asad, Muhammad Javaid</creator><creator>Naqvi, Syed Muhammad Saqlan</creator><creator>Zainab, Tayyaba</creator><creator>Malik, Saad Imran</creator><creator>Mehmood, Raja Tahir</creator><creator>Khan, Jehangir</creator><creator>Sultana, Tasawar</creator><creator>Nasir, Nazim</creator><creator>Hassan, Atiq</creator><general>North Carolina State University</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X2</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>HCIFZ</scope><scope>M0K</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope></search><sort><creationdate>20220514</creationdate><title>An engineered Aspergillus fumigatus GH3 β-glucosidase with higher glucose tolerance</title><author>Nazir, Sidrah ; 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| source | DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals |
| subjects | Amino acids Aspergillus fumigatus Biological activity Biomass Cellulase Cellulose Enzymes Genes Glucans Glucose Glucose tolerance Glucosidase Industrial applications Lignocellulose Metal ions Mutagenesis Mutants Mutation Optimization pH effects Plasmids Proteins Temperature tolerance β-Glucosidase |
| title | An engineered Aspergillus fumigatus GH3 β-glucosidase with higher glucose tolerance |
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