Characterization of an exo-inulinase from<i>Arthrobacter</i>: A novel NaCl-tolerant exo-inulinase with high molecular mass

Shen, Jidong; Zhang, Rui; Li, Junjun; Tang, Xianghua; Li, Ruixian; Wang, Min; Huang, Zunxi; Zhou, Junpei

doi:10.1080/21655979.2015.1019686

Cited by 12 publications

(5 citation statements)

References 28 publications

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“…The exo-inulinases from Arthrobacter strains HJ7 and MN8 and Sphingomonas sp. JB13 were observed to exhibit considerable salt tolerance, without a clear elucidation of structural characteristics and mechanisms regarding salt tolerance ( Shen et al, 2015 ; Zhou et al, 2015a , b ). Comparisons of biochemical and structural properties among InuAMN8 and its mutants MutG169Δ4 and MutG360Δ9 in this study revealed that salt tolerance showed a positive correlation with the negatively charged surface.…”

Section: Discussionmentioning

confidence: 99%

Deletion of the Loop Linking Two Domains of Exo-Inulinase InuAMN8 Diminished the Enzymatic Thermo-Halo-Alcohol Tolerance

Cen

Zhang

et al. 2022

Front. Microbiol.

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Inulin is the rich water-soluble storage polysaccharide after starch in nature, and utilization of inulin through hydrolysis of exo-inulinases has attracted much attention. Thermo-halo-alcohol tolerance is essential for exo-inulinase applications, while no report reveals the molecular basis involved in halo-alcohol tolerance of exo-inulinases via experimental data. In this study, two loops of exo-inulinase InuAMN8, including the loop built with 360GHVRLGPQP368 linking domains of Glyco_hydro_32N and Glyco_hydro_32C and another loop built with 169GGAG172 in the catalytic domain, were deleted to generate mutants MutG360Δ9 and MutG169Δ4, respectively. After heterologous expression, purification, and dialysis, InuAMN8, MutG169Δ4, and MutG360Δ9 showed half-lives of 144, 151, and 7 min at 50°C, respectively. InuAMN8 and MutG169Δ4 were very stable, while MutG360Δ9 showed a half-life of approximately 60 min in 5.0% (w/v) NaCl, and they showed half-lives of approximately 60 min in 25.0, 25.0, and 5.0% (w/v) ethanol, respectively. Structural analysis indicated that two cation-π bonds, which contributed to thermal properties of InuAMN8 at high temperatures, broke in MutG360Δ9. Four basic amino acid residues were exposed to the structural surface of MutG360Δ9 and formed positive and neutral electrostatic potential that caused detrimental effects on halo-alcohol tolerance. The study may provide a better understanding of the loop-function relationships that are involved in thermo-halo-alcohol adaptation of enzymes in extreme environment.

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Section: Discussionmentioning

confidence: 99%

Deletion of the Loop Linking Two Domains of Exo-Inulinase InuAMN8 Diminished the Enzymatic Thermo-Halo-Alcohol Tolerance

Cen

Zhang

et al. 2022

Front. Microbiol.

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“…This inulinase can sustain 90% of its activity during one hour incubation at 50°С. Shen et al (2015) found that the exoinulinase from Arthrobacter sp. HJ7 has a temperature optimum range of 40-45°С and a pH optimum ranging between pH 5.0 and 5.5.…”

Section: Temperature Optimum and Temperature Stabilitymentioning

confidence: 97%

“…Cu 2+ , Zn 2+ and Ni 2+ also inhibit said inulinase. Shen et al (2015) determined that the exo-inulinase produced by Arthrobacter sp. HJ7 is not affected by 1.0 and 10.0 mМ Zn 2+ and Pb 2+ ions.…”

Section: Effects Of Metal Ions and Reagentsmentioning

confidence: 99%

“…Inulinases from various microbial sources have been isolated and characterized. Unfortunately, only a small part of which have a temperature optimum of 60С and a considerable thermal stability (Ettalibi and Baratti, 1987;Ettalibi and Baratti, 2001;Kwon et al, 2003;Sharma and Gill, 2007;Neagu (Bonciu) and Bahrim, 2011;Shen et al, 2015). It is for these reasons that the matter of thermostable inulinases, produced by thermophillic microorganisms remains relevant.…”

Section: Introductionmentioning

confidence: 99%

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Purification of an Exo-Inulinase From Bacillus Sp. Sg7

Иванова¹,

Gavrailov²,

Pashkoulova³

2018

J microb biotech food sci

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An exo-inulinase from strain Bacillus sp. SG7 was isolated and purified. A two-phase system PEG/Dextran, size-exclusion chromatography and ion-exchange chromatography were used in the purification process. The enzyme was purified to homogeneity with specific inulinase activity 18.47 U/mg protein and specific invertase activity 196.5 U/mg protein, purification fold of 10.44 and 27.4% yield. The molecular mass of the purified enzyme was estimated to be 56 000 Da. Strong inhibitors of enzyme activity are Pb, Hg, Zn and Cu ions with inhibition levels rising up to 55% for Cu and 95% for Pb. SDS totally inhibited the purified inulinase. The kinetic constants Km and Vmax for inulin as substrate were determined to be 1.0 mg/mL and 6.25 mg/mL.h, respectively. The pH optimum is at pH 7.0 and the enzyme is stable between pH 6.0 and pH 7.5, while retaining 100% of its initial activity between pH 6.5 and pH 7.0. The temperature optimum for the purified inulinase from strain Bacillus sp. SG7 was at 60°С. In the presence of inulin the purified inulinase sustains its activity at 100% for 55 minutes at 65°С. After the 70 th minute the residual activity is 63% of the initial. The enzyme showed capacity to hydrolyse sucrose, raffinose and inulin from which it liberated only fructose units showing, therefore, an exo-action mechanism. The inulins from chicory (Cichorium intibus), from dahlia (Dahlia pinnata) and Jerusalem artichoke (Helianthus tuberosus) roots were hydrolysed by the purified enzyme. ARTICLE INFO

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“…The genus Arthrobacter can effectually utilize inorganic and organic compounds as a metabolism substrate, acting as a tool for bioremediation in agriculture [ 75 , 76 , 77 , 78 ]. Certain Arthrobacter species, mainly soil-dwelling rhizobacteria, have been considered as plant growth promoters because of their different growth-promoting activities, such as potassium and phosphate solubilization, nitrogen fixation, and indole acetic acid synthesis [ 79 , 80 ].…”

Section: Arthrobacter Sppmentioning

confidence: 99%

The Roles of Plant-Growth-Promoting Rhizobacteria (PGPR)-Based Biostimulants for Agricultural Production Systems

Sun,

Shahrajabian,

Soleymani

2024

Plants

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The application of biostimulants has been proven to be an advantageous tool and an appropriate form of management towards the effective use of natural resources, food security, and the beneficial effects on plant growth and yield. Plant-growth-promoting rhizobacteria (PGPR) are microbes connected with plant roots that can increase plant growth by different methods such as producing plant hormones and molecules to improve plant growth or providing increased mineral nutrition. They can colonize all ecological niches of roots to all stages of crop development, and they can affect plant growth and development directly by modulating plant hormone levels and enhancing nutrient acquisition such as of potassium, phosphorus, nitrogen, and essential minerals, or indirectly via reducing the inhibitory impacts of different pathogens in the forms of biocontrol parameters. Many plant-associated species such as Pseudomonas, Acinetobacter, Streptomyces, Serratia, Arthrobacter, and Rhodococcus can increase plant growth by improving plant disease resistance, synthesizing growth-stimulating plant hormones, and suppressing pathogenic microorganisms. The application of biostimulants is both an environmentally friendly practice and a promising method that can enhance the sustainability of horticultural and agricultural production systems as well as promote the quantity and quality of foods. They can also reduce the global dependence on hazardous agricultural chemicals. Science Direct, Google Scholar, Springer Link, CAB Direct, Scopus, Springer Link, Taylor and Francis, Web of Science, and Wiley Online Library were checked, and the search was conducted on all manuscript sections in accordance with the terms Acinetobacter, Arthrobacter, Enterobacter, Ochrobactrum, Pseudomonas, Rhodococcus, Serratia, Streptomyces, Biostimulants, Plant growth promoting rhizobactera, and Stenotrophomonas. The aim of this manuscript is to survey the effects of plant-growth-promoting rhizobacteria by presenting case studies and successful paradigms in various agricultural and horticultural crops.

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

Cited by 12 publications

References 28 publications

Deletion of the Loop Linking Two Domains of Exo-Inulinase InuAMN8 Diminished the Enzymatic Thermo-Halo-Alcohol Tolerance

Deletion of the Loop Linking Two Domains of Exo-Inulinase InuAMN8 Diminished the Enzymatic Thermo-Halo-Alcohol Tolerance

Purification of an Exo-Inulinase From Bacillus Sp. Sg7

The Roles of Plant-Growth-Promoting Rhizobacteria (PGPR)-Based Biostimulants for Agricultural Production Systems

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