Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414
A novel β-1,3-galactosidase, designated as MaBGA (β-galactosidase from Marinomonas sp. BSi20414), was successfully purified to homogeneity from Marinomonas sp. BSi20414 isolated from Arctic sea ice by ammonium sulfate precipitation and anion exchange chromatography, resulting in an 8.12-fold increas...
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ftmdpi:oai:mdpi.com:/1660-3397/15/1/13/ 2023-08-20T04:04:42+02:00 Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 Haitao Ding Qian Zeng Lili Zhou Yong Yu Bo Chen agris 2017-01-08 application/pdf https://doi.org/10.3390/md15010013 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/md15010013 https://creativecommons.org/licenses/by/4.0/ Marine Drugs; Volume 15; Issue 1; Pages: 13 β-galactosidase Marinomonas thermostable purification gene cloning linkage selectivity Text 2017 ftmdpi https://doi.org/10.3390/md15010013 2023-07-31T21:01:31Z A novel β-1,3-galactosidase, designated as MaBGA (β-galactosidase from Marinomonas sp. BSi20414), was successfully purified to homogeneity from Marinomonas sp. BSi20414 isolated from Arctic sea ice by ammonium sulfate precipitation and anion exchange chromatography, resulting in an 8.12-fold increase in specific activity and 9.9% recovery in total activity. MaBGA displayed its maximum activity at pH 6.0 and 60 °C, and maintained at least 90% of its initial activity over the pH range of 5.0–8.0 after incubating for 1 h. It also exhibited considerable thermal stability, which retained 76% of its initial activity after incubating at 50 °C for 6 h. In contrast to other β-galactosidases, MaBGA displayed strict substrate specificity, not only for the glycosyl group, but also for the linkage type. To better understand the structure–function relationship, the encoding gene of MaBGA was obtained and subject to bioinformatics analysis. Multiple alignments and phylogenetic analysis revealed that MaBGA belonged to the glycoside hydrolase family 42 and had closer genetic relationships with thermophilic β-galactosidases of extremophiles. With the aid of homology modeling and molecular docking, we proposed a reasonable explanation for the linkage selectivity of MaBGA from a structural perspective. On account of the robust stability and 1,3-linkage selectivity, MaBGA would be a promising candidate in the biosynthesis of galacto-oligosaccharide with β1–3 linkage. Text Arctic Sea ice MDPI Open Access Publishing Arctic Marine Drugs 15 1 13 |
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English |
topic |
β-galactosidase Marinomonas thermostable purification gene cloning linkage selectivity |
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β-galactosidase Marinomonas thermostable purification gene cloning linkage selectivity Haitao Ding Qian Zeng Lili Zhou Yong Yu Bo Chen Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 |
topic_facet |
β-galactosidase Marinomonas thermostable purification gene cloning linkage selectivity |
description |
A novel β-1,3-galactosidase, designated as MaBGA (β-galactosidase from Marinomonas sp. BSi20414), was successfully purified to homogeneity from Marinomonas sp. BSi20414 isolated from Arctic sea ice by ammonium sulfate precipitation and anion exchange chromatography, resulting in an 8.12-fold increase in specific activity and 9.9% recovery in total activity. MaBGA displayed its maximum activity at pH 6.0 and 60 °C, and maintained at least 90% of its initial activity over the pH range of 5.0–8.0 after incubating for 1 h. It also exhibited considerable thermal stability, which retained 76% of its initial activity after incubating at 50 °C for 6 h. In contrast to other β-galactosidases, MaBGA displayed strict substrate specificity, not only for the glycosyl group, but also for the linkage type. To better understand the structure–function relationship, the encoding gene of MaBGA was obtained and subject to bioinformatics analysis. Multiple alignments and phylogenetic analysis revealed that MaBGA belonged to the glycoside hydrolase family 42 and had closer genetic relationships with thermophilic β-galactosidases of extremophiles. With the aid of homology modeling and molecular docking, we proposed a reasonable explanation for the linkage selectivity of MaBGA from a structural perspective. On account of the robust stability and 1,3-linkage selectivity, MaBGA would be a promising candidate in the biosynthesis of galacto-oligosaccharide with β1–3 linkage. |
format |
Text |
author |
Haitao Ding Qian Zeng Lili Zhou Yong Yu Bo Chen |
author_facet |
Haitao Ding Qian Zeng Lili Zhou Yong Yu Bo Chen |
author_sort |
Haitao Ding |
title |
Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 |
title_short |
Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 |
title_full |
Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 |
title_fullStr |
Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 |
title_full_unstemmed |
Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 |
title_sort |
biochemical and structural insights into a novel thermostable β-1,3-galactosidase from marinomonas sp. bsi20414 |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2017 |
url |
https://doi.org/10.3390/md15010013 |
op_coverage |
agris |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic Sea ice |
genre_facet |
Arctic Sea ice |
op_source |
Marine Drugs; Volume 15; Issue 1; Pages: 13 |
op_relation |
https://dx.doi.org/10.3390/md15010013 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/md15010013 |
container_title |
Marine Drugs |
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15 |
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1 |
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13 |
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1774715080816984064 |