ArticleBioengineered2015
Characterization of an exo-inulinase from Arthrobacter: a novel NaCl-tolerant exo-inulinase with high molecular mass.
Article in Bioengineered, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Microbial Inulinases: Characterization, Properties, and Potential Contribution to Metabolic and Nutritional Health.Molecules (Basel, Switzerland) · 2026Review
- The Roles of Plant-Growth-Promoting Rhizobacteria (PGPR)-Based Biostimulants for Agricultural Production Systems.Plants (Basel, Switzerland) · 2024Review
- Production of fructan synthesis/hydrolysis of endophytic bacteria involved in inulin production in Jerusalem artichoke.3 Biotech · 2022Article
- Characterization of inulolytic enzymes from the Jerusalem artichoke-derived Glutamicibacter mishrai NJAU-1.Applied microbiology and biotechnology · 2022Article
- Deletion of the Loop Linking Two Domains of Exo-Inulinase InuAMN8 Diminished the Enzymatic Thermo-Halo-Alcohol Tolerance.Frontiers in microbiology · 2022Article
- Examining the molecular characteristics of glycoside hydrolase family 20 β-N-acetylglucosaminidases with high activity.Bioengineered · 2019Article
- Purification and Characterization of Exo-Inulinase from Paenibacillus sp. d9 Strain.The protein journal · 2018Article
- A Shinella β-N-acetylglucosaminidase of glycoside hydrolase family 20 displays novel biochemical and molecular characteristics.Extremophiles : life under extreme conditions · 2017Article
- Distinctive molecular and biochemical characteristics of a glycoside hydrolase family 20 β-N-acetylglucosaminidase and salt tolerance.BMC biotechnology · 2017Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A glycoside hydrolase family 32 exo-inulinase gene was cloned from Arthrobacter sp. HJ7 isolated from saline soil located in Heijing town. The gene encodes an 892-residue polypeptide with a calculated mass of 95.1 kDa and a high total frequency of amino acid residues G, A, and V (30.0%). Escherichia coli BL21 (DE3) cells were used as hosts to express the exo-inulinase gene. The recombinant exo-inulinase (rInuAHJ7) showed an apparently maximal activity at pH 5.0-5.5 and 40-45°C. The addition of 1.0 and 10.0 mM Zn(2+) and Pb(2+) had little or no effect on the enzyme activity. rInuAHJ7 exhibited good salt tolerance, retaining more than 98% inulinase activity at a concentration of 3.0%-20.0% (w/v) NaCl. Fructose was the main product of inulin, levan, and Jerusalem artichoke tubers hydrolyzed by the enzyme. The present study is the first to report the identification and characterization of an Arthrobacter sp exo-inulinase showing a high molecular mass of 95.1 kDa and NaCl tolerance. These results suggest that the exo-inulinase might be an alternative material for potential applications in processing seafood and other foods with high saline contents, such as marine algae, pickles, and sauces.
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