A multi-tolerant low molecular weight mannanase from Bacillus sp. CSB39 and its compatibility as an industrial biocatalyst

Regmi, Sudip; Pradeep, G C; Choi, Yun Hee; Choi, Yoon Seok; Choi, Ji Eun; Cho, Seung‐Sik; Yoo, Jin Cheol

doi:10.1016/j.enzmictec.2016.06.018

Cited by 25 publications

(12 citation statements)

References 40 publications

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“…S27 (Shi et al, 2011) and for DturCelB (Fusco et al, 2018). However, there are many reports where β-mannanase activity was either reduced to greater extent or completely halted in the presence of EDTA (Liu et al, 2015;Regmi et al, 2016;Singh et al, 2019). In this study, only SDS and CTAB drastically inhibited enzyme activity.…”

Section: Discussionmentioning

confidence: 47%

Man/Cel5B, a Bifunctional Enzyme Having the Highest Mannanase Activity in the Hyperthermic Environment

Sadaqat

Chen

Rupani

et al. 2021

Front. Bioeng. Biotechnol.

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Thermotoga maritima (Tma) contains genes encoding various hyperthermophilic enzymes with great potential for industrial applications. The gene TM1752 in Tma genome has been annotated as cellulase gene encoding protein Cel5B. In this work, the gene TM1752 was cloned and expressed in Escherichia coli, and the recombinant enzyme was purified and characterized. Interestingly, the purified enzyme exhibited specific activities of 416 and 215 U/mg on substrates galactomannan and carboxy methyl cellulose, which is the highest among thermophilic mannanases. However, the putative enzyme did not show sequence homology with any of the previously reported mannanases; therefore, the enzyme Cel5B was identified as bifunctional mannanase and cellulase and renamed as Man/Cel5B. Man/Cel5B exhibited maximum activity at 85°C and pH 5.5. This enzyme retained more than 50% activity after 5 h of incubation at 85°C, and retained up to 80% activity after incubated for 1 h at pH 5–8. The Km and Vmax of Man/Cel5B were observed to be 4.5 mg/mL galactomannan and 769 U/mg, respectively. Thin layer chromatography depicted that locust bean gum could be efficiently degraded to mannobiose, mannotriose, and mannooligosaccharides by Man/Cel5B. These characteristics suggest that Man/Cel5B has attractive applications for future food, feed, and biofuel industries.

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Section: Discussionmentioning

confidence: 47%

Man/Cel5B, a Bifunctional Enzyme Having the Highest Mannanase Activity in the Hyperthermic Environment

Sadaqat

Chen

Rupani

et al. 2021

Front. Bioeng. Biotechnol.

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“…One example is Man5A that has been shown to retain more than 97% of its catalytic activity after 60 or 30 min of proteolytic treatment with trypsin, α-chymotrypsin, collagenase, subtilisin A, and proteinase K (Luo et al 2012). Worth mentioning are also the multi-stress tolerant enzymes isolated from Neosartorya fischeri P1 (Man5P1) and Bacillus subtilis CSB39 (MnCSB39), which are resistant to the presence of SDS, Ag + ions, surfactants, NaCl and urea, as well as to the action of proteases (Regmi et al 2016;Yang et al 2015b). Altogether, the above-mentioned features make these enzymes very interesting candidates for various industrial applications.…”

Section: β-Mannanasesmentioning

confidence: 99%

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Aulitto

Fusco

Limauro

et al. 2019

World J Microbiol Biotechnol

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Extremophilic microorganisms are valuable sources of enzymes for various industrial applications. In fact, given their optimal catalytic activity and operational stability under harsh physical and chemical conditions, they represent a suitable alternative to their mesophilic counterparts. For instance, extremophilic enzymes are important to foster the switch from fossil-based to lignocellulose-based industrial processes. Indeed, more stable enzymes are needed, because the conversion of the lignocellulosic biomass to a wide palette of value-added products requires extreme chemo-physical pre-treatments. Galactomannans are part of the hemicellulose fraction in lignocellulosic biomass. They are heteropolymers constituted by a β-1,4-linked mannan backbone substituted with side chains of α-1,6-linked galactose residues. Therefore, the joint action of different hydrolytic enzymes (i.e. β-mannanase, β-mannosidase and α-galactosidase) is needed to accomplish their complete hydrolysis. So far, numerous galactomannan-degrading enzymes have been isolated and characterized from extremophilic microorganisms. Besides applications in biorefinery, these biocatalysts are also useful to improve the quality (i.e. digestibility and prebiotic properties) of food and feed as well as in paper industries to aid the pulp bleaching process. In this review, an overview about the structure, function and applications of galactomannans is provided. Moreover, a survey of (hyper)-thermophilic galactomannans-degrading enzymes, mainly characterized in the last decade, has been carried out. These extremozymes are described in the light of their biotechnological application in industrial processes requiring harsh conditions.

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“…AM-001 58 9.0 60 8.0–9.0 ≤ 50 NA NA [ 74 ] B. nealsonii PN-11 50 8.8 65 5.0–10.0 ≤ 70 LBG 2288.9 [ 13 ] B. circulans CGMCC1554 32 7.6 60 6.0–10.0 ≤ 50 LBG 4839.0 [ 51 ] B. circulans CGMCC1416 31 7.6 58 7.0–9.0 ≤ 50 LBG 481.6 [ 12 ] Bacillus sp. CSB39 30 7.5 70 4.6–11.0 ≤ 70 LBG 1063.9 [ 68 ] Bacillus sp. W-2 36 7.0 70 5.0–10.0 ≤ 60 LBG 710.0 [ 7 ] B. subtilis BCC41051 38 7.0 60 5.0–11.5 …”

Section: Resultsmentioning

confidence: 99%

“…inaquosorum CSB31 (0.043 g l −1 ) [ 53 ], Bacillus sp. CSB39 (0.082 g l −1 ) [ 68 ], Bacillus sp. MG-33 (0.20 g l −1 ) [ 69 ], N. fischeri P1 (0.83 g l −1 ) [ 32 ], A. nidulans XZ3 (0.90 g l −1 ) [ 25 ], Streptomyces sp.…”

Section: Resultsmentioning

confidence: 99%

Characterization and high-efficiency secreted expression in Bacillus subtilis of a thermo-alkaline β-mannanase from an alkaliphilic Bacillus clausii strain S10

Zhou

Xue

2018

Microb Cell Fact

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Backgroundβ-Mannanase catalyzes the cleavage of β-1,4-linked internal linkages of mannan backbone randomly to produce new chain ends. Alkaline and thermostable β-mannanases provide obvious advantages for many applications in biobleaching of pulp and paper, detergent industry, oil grilling operation and enzymatic production of mannooligosaccharides. However, only a few of them are commercially exploited as wild or recombinant enzymes, and none heterologous and secretory expression of alkaline β-mannanase in Bacillus subtilis expression system was reported. Alkaliphilic Bacillus clausii S10 showed high β-mannanase activity at alkaline condition. In this study, this β-mannanase was cloned, purified and characterized. The high-level secretory expression in B. subtilis was also studied.ResultsA thermo-alkaline β-mannanase (BcManA) gene encoding a 317-amino acid protein from alkaliphilic Bacillus clausii strain was cloned and expressed in Escherichia coli. The purified mature BcManA exhibited maximum activity at pH 9.5 and 75 °C with good stability at pH 7.0–11.5 and below 80 °C. BcManA demonstrated high cleavage capability on polysaccharides containing β-1,4-mannosidic linkages, such as konjac glucomannan, locust bean gum, guar gum and sesbania gum. The highest specific activity of 2366.2 U mg−1 was observed on konjac glucomannan with the Km and kcat value of 0.62 g l−1 and 1238.9 s−1, respectively. The hydrolysis products were mainly oligosaccharides with a higher degree of polymerization than biose. BcManA also cleaved manno-oligosaccharides with polymerization degree more than 3 without transglycosylation. Furthermore, six signal peptides and two strong promoters were used for efficiently secreted expression optimization in B. subtilis WB600 and the highest extracellular activity of 2374 U ml−1 with secretory rate of 98.5% was obtained using SPlipA and P43 after 72 h cultivation in 2 × SR medium. By medium optimization using cheap nitrogen and carbon source of peanut meal and glucose, the extracellular activity reached 6041 U ml−1 after 72 h cultivation with 6% inoculum size by shake flask fermentation.ConclusionsThe thermo-alkaline β-mannanase BcManA showed good thermal and pH stability and high catalytic efficiency towards konjac glucomannan and locust bean gum, which distinguished from other reported β-mannanases and was a promising thermo-alkaline β-mannanase for potential industrial application. The extracellular BcManA yield of 6041 U ml−1, which was to date the highest reported yield by flask shake, was obtained in B. subtilis with constitutive expression vector. This is the first report for secretory expression of alkaline β-mannanase in B. subtilis protein expression system, which would significantly cut down the production cost of this enzyme. Also this research would be helpful for secretory expression of other β-mannanases in B. subtilis.Electronic supplementary materialThe online version of this article (10.1186/s12934-018-0973-0) contains supplementary material, which is available to authorized users.

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A multi-tolerant low molecular weight mannanase from Bacillus sp. CSB39 and its compatibility as an industrial biocatalyst

Cited by 25 publications

References 40 publications

Man/Cel5B, a Bifunctional Enzyme Having the Highest Mannanase Activity in the Hyperthermic Environment

Man/Cel5B, a Bifunctional Enzyme Having the Highest Mannanase Activity in the Hyperthermic Environment

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Characterization and high-efficiency secreted expression in Bacillus subtilis of a thermo-alkaline β-mannanase from an alkaliphilic Bacillus clausii strain S10

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