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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ftpubmed:oai:pubmedcentral.nih.gov:5295233 2023-05-15T15:08:53+02:00 Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 Ding, Haitao Zeng, Qian Zhou, Lili Yu, Yong Chen, Bo 2017-01-08 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5295233/ http://www.ncbi.nlm.nih.gov/pubmed/28075353 https://doi.org/10.3390/md15010013 en eng MDPI http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5295233/ http://www.ncbi.nlm.nih.gov/pubmed/28075353 http://dx.doi.org/10.3390/md15010013 © 2017 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). CC-BY Article Text 2017 ftpubmed https://doi.org/10.3390/md15010013 2017-02-12T01:14:06Z 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 PubMed Central (PMC) Arctic Marine Drugs 15 1 13 |
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Article Ding, Haitao Zeng, Qian Zhou, Lili Yu, Yong Chen, Bo Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414 |
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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 |
Ding, Haitao Zeng, Qian Zhou, Lili Yu, Yong Chen, Bo |
author_facet |
Ding, Haitao Zeng, Qian Zhou, Lili Yu, Yong Chen, Bo |
author_sort |
Ding, Haitao |
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 |
MDPI |
publishDate |
2017 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5295233/ http://www.ncbi.nlm.nih.gov/pubmed/28075353 https://doi.org/10.3390/md15010013 |
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Arctic |
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Arctic |
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Arctic Sea ice |
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Arctic Sea ice |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5295233/ http://www.ncbi.nlm.nih.gov/pubmed/28075353 http://dx.doi.org/10.3390/md15010013 |
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© 2017 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/). |
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CC-BY |
op_doi |
https://doi.org/10.3390/md15010013 |
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Marine Drugs |
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15 |
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13 |
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