ArticleWorld journal of microbiology & biotechnology2013
A novel cold-adapted β-galactosidase isolated from Halomonas sp. S62: gene cloning, purification and enzymatic characterization.
Article in World journal of microbiology & biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 29 citations in OpenAlex.
- Enzymes from Fishery and Aquaculture Waste: Research Trends in the Era of Artificial Intelligence and Circular Bio-Economy.Marine drugs · 2024Review
- A Review on Psychrophilic β-D-Galactosidases and Their Potential Applications.Applied biochemistry and biotechnology · 2023Review
- Himalayan Microbiomes for Agro-environmental Sustainability: Current Perspectives and Future Challenges.Microbial ecology · 2022Review
- Sustainable Upcycling of Fisheries and Aquaculture Wastes Using Fish-Derived Cold-Adapted Proteases.Frontiers in nutrition · 2022Review
- AntarcticInternational journal of molecular sciences · 2021Article
- Cold-Active β-Galactosidases: Insight into Cold Adaption Mechanisms and Biotechnological Exploitation.Marine drugs · 2021Review
- Cloning and Characterization of a New β-Galactosidase fromMarine drugs · 2020Article
- Cloning, Expression and Characterization of a Novel Cold-adapted β-galactosidase from the Deep-sea BacteriumMarine drugs · 2018Article
- Pitfalls on sample preparation forOncotarget · 2018Article
- Article
- Molecular cloning, expression, and characterization of four novel thermo-alkaliphilic enzymes retrieved from a metagenomic library.Biotechnology for biofuels · 2017Article
- Surgical tissue handling methods to optimize ex vivo fluorescence with the activatable optical probe γ-glutamyl hydroxymethyl rhodamine green.Contrast media & molecular imaging · 2016Article
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6 authors at 1 institution in 1 country.
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Abstract
A novel 1,170 bp β-galactosidase gene sequence from Halomonas sp. S62 (BGalH) was identified through whole genome sequencing and was submitted to GenBank (Accession No. JQ337961). The BGalH gene was heterologously expressed in Escherichia coli BL21(DE3) cells, and the enzymatic properties of recombinant BGalH were studied. According to the polyacrylamide gel electrophoresis results and the sequence alignment analysis, BGalH is a dimeric protein and cannot be classified into one of the known β-galactosidase families (GH1, GH2, GH35, GH42). The optimal pH and temperature were determined to be 7.0 and 45 °C, respectively; the K m and K cat were 2.9 mM and 390.3 s(-1), respectively, for the reaction with the substrate ortho-nitrophenyl-β-D-galactopyranoside. At 0-20 °C, BGalH exhibited 50-70 % activity relative to its activity under the optimal conditions. BGalH was stable over a wide range of pHs (6.0-8.5) after a 1 h incubation (>93 % relative activity) and was thermostable at 50 °C and below (>60 % relative activity). The enzyme hydrolyzes lactose completely in milk over 24 h at 7 °C. The characteristics of this novel β-galactosidase suggest that BGalH may be a good candidate for medical researches and food industry applications.
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