Next Article in Journal
Time Course Exo-Metabolomic Profiling in the Green Marine Macroalga Ulva (Chlorophyta) for Identification of Growth Phase-Dependent Biomarkers
Next Article in Special Issue
Preparation of Antioxidant Peptides from Salmon Byproducts with Bacterial Extracellular Proteases
Previous Article in Journal
Trichophycin A, a Cytotoxic Linear Polyketide Isolated from a Trichodesmium thiebautii Bloom
Previous Article in Special Issue
In vitro Anti-Thrombotic Activity of Extracts from Blacklip Abalone (Haliotis rubra) Processing Waste
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle
Mar. Drugs 2017, 15(1), 13;

Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414

SOA Key Laboratory for Polar Science, Polar Research Institute of China, Shanghai 200136, China
Author to whom correspondence should be addressed.
Academic Editor: Se-Kwon Kim
Received: 1 November 2016 / Revised: 20 December 2016 / Accepted: 24 December 2016 / Published: 8 January 2017
(This article belongs to the Special Issue Marine Proteins and Peptides)
Full-Text   |   PDF [3812 KB, uploaded 8 January 2017]   |  


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. View Full-Text
Keywords: β-galactosidase; Marinomonas; thermostable; purification; gene cloning; linkage selectivity β-galactosidase; Marinomonas; thermostable; purification; gene cloning; linkage selectivity

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Ding, H.; Zeng, Q.; Zhou, L.; Yu, Y.; Chen, B. Biochemical and Structural Insights into a Novel Thermostable β-1,3-Galactosidase from Marinomonas sp. BSi20414. Mar. Drugs 2017, 15, 13.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Mar. Drugs EISSN 1660-3397 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top