A novel β-mannanase from Pantoea agglomerans A021: gene cloning, expression, purification and characterization

Jing, Wang; Shao, Zongze; Hong, Yuzhi; Li, Chanjuan; Fu, Xiaoyu; Liu, Ziduo

doi:10.1007/s11274-010-0358-y

Cited by 33 publications

(11 citation statements)

References 33 publications

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“…They reported that the maximum b-mannanase activity was 7.9, 41.1, and 76.1 U/mL, respectively. Wang et al (2010) produced the bmannanase in shake flasks with konjac powder by using Pantoena agglomerans A021 and reported that the maximum b-mannanase activity of purified Man26P was 514 U/mg. It has also been reported that the b-mannanase activity was found to be 2195.5 U/mL in fed-batch bioreactor with corn steep liquor dextrose medium by recombinant Pichia pastoris (Zheng et al 2012).…”

Section: Resultsmentioning

confidence: 99%

Effect of different fermentation strategies on β-mannanase production in fed-batch bioreactor system

et al. 2017

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Mannanases, one of the important enzyme group for industry, are produced by numerous filamentous fungi, especially Aspergillus species with different fermentation methods. The aim of this study was to show the best fermentation method of β-mannanase production for fungal growth in fermenter. Therefore, different fermentation strategies in fed-batch fermentation (suspended, immobilized cell, biofilm and microparticle-enhanced bioreactor) were applied for β-mannanase production from glucose medium (GM) and carob extract medium (CEM) by using recombinant Aspergillus sojae. The highest β-mannanase activities were obtained from microparticle-enhanced bioreactor strategy. It was found to be 347.47 U/mL by adding 10 g/L of AlO to GM and 439.13 U/mL by adding 1 g/L of talcum into CEM. The maximum β-mannanase activities for suspended, immobilization, and biofilm reactor remained at 72.55 U/mL in GM, 148.81 U/mL in CEM, and 194.09 U/mL in GM, respectively. The reason for that is the excessive, and irregular shaped growth and bulk formation, inadequate oxygen transfer or substrate diffusion in bioreactor. Consequently, the enzyme activity was significantly enhanced by addition of microparticles compared to other fed-batch fermentation strategies. Also, repeatable β-mannanase activities were obtained by controlling of the cell morphology by adding microparticle inside the fermenter.

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Section: Resultsmentioning

confidence: 99%

Effect of different fermentation strategies on β-mannanase production in fed-batch bioreactor system

et al. 2017

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“…A novel mannanase gene ( A021 ) was isolated from marine bacterium Pantoea agglomerans and was cloned in E. coli . Maximum activity of enzyme was observed at pH 6 at 55 o C that enhanced in correlation to the increase of NaCl concentration up to 0.75 M (Wang et al 2010a ).…”

Section: Xylanasesmentioning

confidence: 94%

Halophilic Bacteria: Potentials and Applications in Biotechnology

Mohammadipanah

Hamedi

Dehhaghi

2015

Sustainable Development and Biodiversity

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Halophilic bacteria are categorized based on their requirements to salt. They apply some strategies in adaptation to the high saline environment. Their low nutritional requirements and resistance to high concentrations of salt, introduce as potent agents in wide range of biotechnological applications. Halophilic bacteria are very divergent and more than 150 species introduce in 70 genera of halophilic bacteria are reported. Use of resistant microorganisms and their metabolites under harsh industrially conditions is a strikingly important subject. Various halophilic enzymes in different enzymatically processes, compatible solutes as macromolecule stabilizers, biopolymers, biofertilizers and pharmaceutically active molecules from halophilic bacteria are among the important applications of these group. Additionally, they have many potential in bioremediation of various organic and inorganic pollutants from environment. This chapter covers the different aspects of potential applications of halophilic bacteria in biotechnology. Keywords IntroductionMicrobial life exists in hypersaline habitat refl ects the adaption of microorganisms to high concentration of salts. Halophilic and halotolerant organisms are found in all three domains of life: Archaea , Bacteria , and Eukarya . According to the requirement

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“…Man1E presented higher expression after IPTG induction for16 h (Fig. 7 e), the mannanase activity was 642.25 U/mL, however, there was no significant difference in soluble expression and activity between 12 and 16 h. By comparison, the optimal inductive temperature and time for Man1E gene expression similar to those of β-mannanase genes from Bacillus circulans NT 6.7 (for 16 h at 18 °C) [ 56 ] and Pantoea agglomerans A021 (for 15 h at 18 °C) [ 57 ]. However, for the expression of three β mannanase genes, the IPTG concentrations were different, which were 0.6 mm, 1.0 mm and 0.05–0.15 mm, respectively.…”

Section: Resultsmentioning

confidence: 99%

Expression, homology modeling and enzymatic characterization of a new β-mannanase belonging to glycoside hydrolase family 1 from Enterobacter aerogenes B19

2020

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Background: β-mannanase can hydrolyze β-1,4 glycosidic bond of mannan by the manner of endoglycosidase to generate mannan-oligosaccharides. Currently, β-mannanase has been widely applied in food, medicine, textile, paper and petroleum exploitation industries. β-mannanase is widespread in various organisms, however, microorganisms are the main source of β-mannanases. Microbial β-mannanases display wider pH range, temperature range and better thermostability, acid and alkali resistance, and substrate specificity than those from animals and plants. Therefore microbial β-mannanases are highly valued by researchers. Recombinant bacteria constructed by gene engineering and modified by protein engineering have been widely applied to produce β-mannanase, which shows more advantages than traditional microbial fermentation in various aspects. Results: A β-mannanase gene (Man1E), which encoded 731 amino acid residues, was cloned from Enterobacter aerogenes. Man1E was classified as Glycoside Hydrolase family 1. The bSiteFinder prediction showed that there were eight essential residues in the catalytic center of Man1E as Trp166, Trp168, Asn229, Glu230, Tyr281, Glu309, Trp341 and Lys374. The catalytic module and carbohydrate binding module (CBM) of Man1E were homologously modeled. Superposition analysis and molecular docking revealed the residues located in the catalytic module of Man1E and the CBM of Man1E. The recombinant enzyme was successfully expressed, purified, and detected about 82.5 kDa by SDS-PAGE. The optimal reaction condition was 55 °C and pH 6.5. The enzyme exhibited high stability below 60 °C, and in the range of pH 3.5-8.5. The β-mannanase activity was activated by low concentration of Co 2+ , Mn 2+ , Zn 2+ , Ba 2+ and Ca 2+. Man1E showed the highest affinity for Locust bean gum (LBG). The K m and V max values for LBG were 3.09 ± 0.16 mg/mL and 909.10 ± 3.85 μmol/(mL min), respectively. Conclusions: A new type of β-mannanase with high activity from E. aerogenes is heterologously expressed and characterized. The enzyme belongs to an unreported β-mannanase family (CH1 family). It displays good pH and temperature features and excellent catalysis capacity for LBG and KGM. This study lays the foundation for future application and molecular modification to improve its catalytic efficiency and substrate specificity.

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A novel β-mannanase from Pantoea agglomerans A021: gene cloning, expression, purification and characterization

Cited by 33 publications

References 33 publications

Effect of different fermentation strategies on β-mannanase production in fed-batch bioreactor system

Effect of different fermentation strategies on β-mannanase production in fed-batch bioreactor system

Halophilic Bacteria: Potentials and Applications in Biotechnology

Expression, homology modeling and enzymatic characterization of a new β-mannanase belonging to glycoside hydrolase family 1 from Enterobacter aerogenes B19

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