Purification and characterization of an endo-1,4-Î²-mannanase from<i>Bacillus subtilis</i>KU-1

Zakaria, M; Yamamoto, Satoshi; Yagi, Toshiharu

doi:10.1111/j.1574-6968.1998.tb12795.x

Cited by 19 publications

(5 citation statements)

References 28 publications

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“…The pH 6.0 was the best pH for mannanase production from Bacillus circulans NT 6.7. The result was similar to mannanase production from Sclerotium rolfsii, pH 6.0 (Gübitz et al, 1996), but lower than that reported for mannanase production from Aspergillus niger, pH 7.0 (Ademark et al, 1998) and Bacillus subtilis KU-1, pH 7.0 (Zakaria et al, 1998). This study used locus bean gum because it's a common substrate used in mannanase industrial production.…”

Section: Effect Of Temperature and Ph On Mannanase Productionsupporting

confidence: 79%

TR OPTIMAL CONDITIONS FOR Β-Mannanase PRODUCTION BY BACILLUS CIRCULANS NT 6.7

Rungruangsaphakun

Keawsompong²

2019

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Optimum medium for mannanase production is very important and producing medium has been shown effective for mannanase production from Bacillus circulans NT 6.7 but expensive. This work aim to find low cost medium and optimum condition for mannanase production from Bacillus circulans NT 6.7. 1.5% concentration of defatted copra meal as carbon source in shake flask resulted in highest growth and enzyme activities of 10.51±0.53 Log CFU/ml and 12.84±4.38 U/ml at 18 hours accordingly. Also, 2% defatted copra meal in fermenter produced highest growth of 7.94±0.41 Log CFU/ml and enzyme activities of 32.07±2.94 U/ml at 15 hours. Using taguchi design, optimal conditions for inoculum, agitation and aeration were 1%, 600 rpm and 0.75 vvm, respectively. Under this optimized condition, the mannanase experimental yield (29.57±4.81U/ml) closely matched the yield predicted by the statistical model (24.15U/ml) with R2 = 0.75. Using mineral salts medium, slightly increased in mannanase product was observed compare to previously used producing medium. Also, the cost of using mineral salts medium (cost per liter) is 27 time lower than the cost of producing medium. Suggesting that, mineral salt medium provides an economically feasible medium for producing mannanase from Bacillus circulans NT 6.7.

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Section: Effect Of Temperature and Ph On Mannanase Productionsupporting

confidence: 79%

TR OPTIMAL CONDITIONS FOR Β-Mannanase PRODUCTION BY BACILLUS CIRCULANS NT 6.7

Rungruangsaphakun

Keawsompong²

2019

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“…N16-5 sourced β-mannanase [26] showed the optimal temperature and pH at 70°C and 10.0 respectively, which was a basic functioning enzyme. A B. subtilis KU-1 sourced β-mannanase functions in the range of 50 to 55°C, and optimally catalyzes in pH 7.0 [27]. A β-mannanase from B. subtilis NM-39 was optimal at 50°C and pH 5.5 [28], which showed the most similar property as our β-mannanase at this point.…”

Section: Discussionmentioning

confidence: 50%

“…A β-mannanase from B. subtilis NM-39 was optimal at 50°C and pH 5.5 [28], which showed the most similar property as our β-mannanase at this point. Our β-mannanase expressed in P. pastoris X-33 optimally functions at 50ºC, which is the closest temperature to the body temperature compared to other reported β-mannanases [25][26][27][28]. Its optimal pH 6.0 is also in the pH range of gastric intestinal tract.…”

Section: Discussionmentioning

confidence: 93%

Expression of Bacillus subtilis MA139 β-mannanase in Pichia pastoris and the Enzyme Characterization

Qiao

Rao

Dong

et al. 2009

Appl Biochem Biotechnol

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The 1014 nucleotides long gene-encoding beta-mannanase from Bacillus subtilis strain MA139 was cloned using PCR. To obtain high expression levels in Pichia pastoris, the beta-mannanase gene was optimized according to the codon usage bias of P. pastoris and fused downstream of GAP promoter. The reconstituted plasmid pGAP-mann was transformed into P. pastoris X-33 strain to constitutively express beta-mannanase. When cultured at 28 degrees Celsius for 3 days protein yields up to 2.7 mg/mL was obtained with the enzyme activity of up to 230 U/mL. In comparison, wild-type gene product yielded 1.9 mg/mL and 170 U/mL, respectively indicating that the protein yield and enzyme activity were significantly improved by codon modification. After purification, the enzyme properties were characterized. The optimal activity was at pH 6.0 and 50 degrees Celsius. In the pH range of 3.0 to 9.0, beta-mannanase showed above 60% of its peak activity. Among the numerous ions tested copper significantly inhibited the enzyme activity. These results suggested that codon-optimized beta-mannanase expressed in P. pastoris could potentially be used as an additive in the feed for monogastric animals.

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“…Based on the 3D structure and H1A-23A mutation, the thermal stability of mannanase BCman from Bacillus subtilis was affected by its disulfide bond and metal-bonding site (His1-Glu336-His23); however, the mechanisms were not determined in details [31]. The specific activity of the purified MAN5A was 4,839 U/mg, which was higher than that of MANB48 (481.55 U/mg) [19] and of the β-mannanase from B. subtilis KU-1 (407.7 U/mg) [32], and only lower than that of β-mannanase purified from B. subtilis WY34 (8302.4 U/mg) [33]. MAN5A contains the acidic residues Glu-110 and Asp-149, in contrast to Gly and Asn, respectively, in MANB48.…”

Section: Discussionmentioning

confidence: 99%

A Novel β-mannanase with High Specific Activity from Bacillus circulans CGMCC1554: Gene Cloning, Expression and Enzymatic Characterization

Yang

Wang

et al. 2008

Appl Biochem Biotechnol

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A DNA fragment of 2,042 bp containing a novel beta-mannanase gene, man5A, was identified from the genome of the mannan-degrading bacterium Bacillus circulans CGMCC1554. The open reading frame of man5A comprised 978 bp encoding a protein of 326 amino acids with a predicted molecular weight of 32 kDa. The amino acid sequence of the encoded mannanase, MAN5A, showed the highest identity (78.5%) to beta-mannanases belonging to glycosyl hydrolases family 5. The gene man5A was efficiently expressed in Escherichia coli and Pichia pastoris with the highest activity of 541 U/ml in a 3-L fermenter. Recombinant MAN5A purified from E. coli had a high specific activity of 4,839 U/mg, which is much higher than that of enzymes that showed high sequence identity. The enzyme showed maximum activity at pH 7.6 and 60 degrees C and resistance to trypsin. After hydrolysis of LBG, oligomannosides accounted for 76% of the hydrolysis products. All these properties collectively make MAN5A a better candidate than current mannanases for use in the food and feed industry.

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Purification and characterization of an endo-1,4-Î²-mannanase fromBacillus subtilisKU-1

Cited by 19 publications

References 28 publications

TR OPTIMAL CONDITIONS FOR Β-Mannanase PRODUCTION BY BACILLUS CIRCULANS NT 6.7

TR OPTIMAL CONDITIONS FOR Β-Mannanase PRODUCTION BY BACILLUS CIRCULANS NT 6.7

Expression of Bacillus subtilis MA139 β-mannanase in Pichia pastoris and the Enzyme Characterization

A Novel β-mannanase with High Specific Activity from Bacillus circulans CGMCC1554: Gene Cloning, Expression and Enzymatic Characterization

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