Cold-active and NaCl-tolerant exo-inulinase from a cold-adapted Arthrobacter sp. MN8 and its potential for use in the production of fructose at low temperatures

Zhou, Junpei; Lu, Qian; Peng, Mozhen; Zhang, Rui; Mo, Ming-He; Tang, Xianghua; Li, Junjun; Xu, Baojun; Ding, Junmei; Huang, Zunxi

doi:10.1016/j.jbiosc.2014.08.003

Cited by 18 publications

(25 citation statements)

References 39 publications

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“…Compared with these inulinases, the salt-tolerant exo-inulinases InuAMN8 (JQ863111, 29.5%) 5 and InuAHJ7 (30.0%) present higher proportions of amino acid residues G, A, and V. The results suggest that amino acid residues G, A, and V may contribute to the salt tolerances of inulinases.…”

Section: Discussionmentioning

confidence: 92%

“…168, 25 Penicillium sp TN-88, 22 and InuAMN8. 5 Like the salt-tolerant exo-inulinase InuAMN8, which also shows resistance to both lead and zinc, 5 rInuAHJ7 retained 99.6% and 90.8% activity in the presence of 10.0 mM Zn 2C and Pb 2C , respectively. -NTA chelating affinity chromatography with imidazole gradient of 100, 200, 300, and 500 mM, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…Several studies have been published on salt-tolerant enzymes, 5,7,8 including the salt-tolerant exo-inulinase InuAMN8 from Arthrobacter sp MN8, which shows 127.9%-88.4% activity at concentrations between 3.5% and 15.0% (w/v) NaCl and 49.8% activity at 20.0% (w/v) NaCl. 5 However, among the published studies to date, salt-tolerant inulinases have rarely been reported.…”

Section: Discussionmentioning

confidence: 99%

“…5 However, among the published studies to date, salt-tolerant inulinases have rarely been reported. 5 The inulinase from Aspergillus fumigatus MTCC 3009 retains 77% activity in the presence of approximately 0.006% (w/v) NaCl, 12 and the inulinase from Kluyveromyces marxianus var bulgaricus retains 50% activity in the presence of approximately 0.3% (w/v) NaCl. 13 In this study, rInuAHJ7 retained even higher relative activity (98.8%) at high NaCl concentration of 20.0% (w/v) than the salt-tolerant exo-inulinase InuAMN8.…”

Section: Discussionmentioning

confidence: 99%

“…4 In addition, many exo-inulinases from bacteria also hydrolyze levan, sucrose, raffinose, stachyose, and starch. 1,2,5 Based on amino acid sequence similarities, exo-inulinases are classified into the glycoside hydrolase (GH) family 32. 6 Enzymes obtained from extremophilic sources have numerous potential applications.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of an exo-inulinase fromArthrobacter: A novel NaCl-tolerant exo-inulinase with high molecular mass

Shen

Zhang

et al. 2015

Bioengineered

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(2015) Characterization of an exo-inulinase from Arthrobacter: A novel NaCl-tolerant exo-inulinase with high molecular mass, Bioengineered, 6:2, 99-105, DOI: 10.1080/21655979.2015 Keywords: Arthrobacter, exo-inulinase, lead, NaCl, zinc 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 40-45C. The addition of 1.0 and 10.0 mM Zn 2C and Pb 2C 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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Section: Discussionmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Characterization of an exo-inulinase fromArthrobacter: A novel NaCl-tolerant exo-inulinase with high molecular mass

Shen

Zhang

et al. 2015

Bioengineered

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Characterization of inulolytic enzymes from the Jerusalem artichoke–derived Glutamicibacter mishrai NJAU-1

Lian

Zhuang

Shui

et al. 2022

Appl Microbiol Biotechnol

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Characterization of a NaCl-tolerant β-N-acetylglucosaminidase from Sphingobacterium sp. HWLB1

et al. 2016

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β-N-Acetylglucosaminidases serve important biological functions and various industrial applications. A glycoside hydrolase family 3 β-N-acetylglucosaminidase gene was cloned from Sphingobacterium sp. HWLB1 and expressed in Escherichia coli BL21 (DE3). The purified recombinant enzyme (rNag3HWLB1) showed apparent optimal activity at pH 7.0 and 40 °C. In the presence of 0.5-20.0 % (w/v) NaCl, the activity and stability of rNag3HWLB1 were slightly affected or not affected. The enzyme could even retain 73.6 % activity when 30.0 % (w/v) NaCl was added to the reaction mixture. The half-life of the enzyme was approximately 10 min at 37 °C without the addition of NaCl. However, the enzyme was stable at 37 °C in the presence of 3.0 % (w/v) NaCl. A large negatively charged surface in the catalytic pocket of the enzyme was observed and might contribute to NaCl tolerance and thermostability improvement. The degree of synergy between a commercial endochitinase and rNag3HWLB1 on chitin enzymatic degradation ranged from 3.11 to 3.74. This study is the first to report the molecular and biochemical properties of a NaCl-tolerant β-N-acetylglucosaminidase.

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Cold-active and NaCl-tolerant exo-inulinase from a cold-adapted Arthrobacter sp. MN8 and its potential for use in the production of fructose at low temperatures

Cited by 18 publications

References 39 publications

Characterization of an exo-inulinase fromArthrobacter: A novel NaCl-tolerant exo-inulinase with high molecular mass

Characterization of an exo-inulinase fromArthrobacter: A novel NaCl-tolerant exo-inulinase with high molecular mass

Characterization of inulolytic enzymes from the Jerusalem artichoke–derived Glutamicibacter mishrai NJAU-1

Characterization of a NaCl-tolerant β-N-acetylglucosaminidase from Sphingobacterium sp. HWLB1

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