Characterization of three .BETA.-mannanases of an alkalophilic Bacillus sp.

Akino, Toshiro; Nakamura, Nobuyuki; Horikoshi, Koki

doi:10.1271/bbb1961.52.773

Cited by 46 publications

(38 citation statements)

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“…strain no. 17 hydrolyzed mannooligosaccharides larger than mannobiose, 40,41) and those from Aeromonas sp. F-25, Bacillus subtilis, Enterococcus casseliflavus FL2121, Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of a β-1,4-Mannanase 5C Possessing a Family 27 Carbohydrate-Binding Module from a Marine Bacterium,Vibriosp. Strain MA-138

Tanaka

Umemoto

Okamura

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…strain no. 17 hydrolyzed mannooligosaccharides larger than mannobiose, 40,41) and those from Aeromonas sp. F-25, Bacillus subtilis, Enterococcus casseliflavus FL2121, Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

Cloning and Characterization of a β-1,4-Mannanase 5C Possessing a Family 27 Carbohydrate-Binding Module from a Marine Bacterium,Vibriosp. Strain MA-138

Tanaka

Umemoto

Okamura

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…AM-001. 28) To examine the pH stability of the enzyme, the enzyme was preincubated at 30°C for 30 min in the various buffers (10 mM) of different pH values, and residual activity was assayed. The enzyme was stable at pH 5.0-10.0, where more than 90% of the maximum activity at pH 8.0 was remained, as shown in Fig.…”

Section: Substrate Specificitymentioning

confidence: 99%

Purification and characterization of β-Mannanase from Reinekea sp. KIT-YO10 with transglycosylation activity

Hakamada

Ohkubo²,

Ohashi

2014

Bioscience, Biotechnology, and Biochemistry

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Marine bacterium Reinekea sp. KIT-YO10 was isolated from the seashore of Kanazawa Port in Japan as a seaweed-degrading bacterium. Homology between KIT-YO10 16S rDNA and the 16S rDNA of Reinekea blandensis and Reinekea marinisedimentorum was 96.4 and 95.4%, respectively. Endo-1,4-β-D-mannanase (β-mannanase, EC 3.2.1.78) from Reinekea sp. KIT-YO10 was purified 29.4-fold to a 21% yield using anion exchange chromatography. The purified enzyme had a molecular mass of 44.3 kDa, as estimated by SDS-PAGE. Furthermore, the purified enzyme displayed high specificity for konjac glucomannan, with no secondary agarase and arginase activity detected. Hydrolysis of konjac glucomannan and locust bean gum yielded oligosaccharides, compatible with an endo mode of substrate depolymerization. The purified enzyme possessed transglycosylation activity when mannooligosaccharides (mannotriose or mannotetraose) were used as substrates. Optimal pH and temperature were determined to be 8.0 and 70 °C, respectively. It showed thermostability at temperatures from 20 to 50 °C and alkaline stability up to pH 10.0. The current enzyme was thermostable and thermophile compared to the β-mannanase of other marine bacteria.

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“…Known mannanase-producing bacteria described to date include Bacillus spp. (Araujo and Ward 1990a, b;Akino et al 1988;Ethier et al 1998;Jiang et al 2006;Zakaria et al 1998;Zhang et al 2000), Streptomyces sp. (Takahashi et al 1984), Enterococcus sp.…”

Section: Identification Of Mannanase-producing Isolatesmentioning

confidence: 99%

Selection and characterization of mannanase-producing bacteria useful for the formation of prebiotic manno-oligosaccharides from copra meal

Titapoka

Keawsompong

Haltrich

et al. 2007

World J Microbiol Biotechnol

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In order to select bacterial strains effectively secreting mannanase activity for the production of prebiotic mannooligosaccharides, a two-step screening procedure was performed. Enriched cultures from isolation medium containing copra meal were primary screened on an isolation agar medium containing 1% locust bean gum (LBG), which resulted in 48 mannanase-producing bacterial isolates with significant clearing zones on the mannan-containing agar. However, only nine isolates showed appreciable mannanase activities against copra meal in their culture supernatants (0.054-0.185 U/mg of protein) as determined in a standard assay based on the detection of reducing sugars released from this substrate. The isolates CW2-3 and ST1-1 displayed the highest activity against LBG and copra meal, respectively. Copra mannan hydrolysates that were obtained by using crude mannanase from these nine isolates were further used for a secondary screening towards a growth-enhancing activity on Lactobacillus reuteri and inhibitory activity against Escherichia coli as well as Salmonella Enteritidis, resulting in 0.09-2.15 log CFU/ml enhancing activity and low inhibitory activity of 0.46-1.78 log CFU/ml as well as 0.37-1.72 log CFU/ml, respectively. The hydrolysate of CW2-3 mannanase showed the highest enhancing activity of 2.15 log CFU/ml while isolate ST1-1 was most effective with respect to growth inhibition against E. coli E010 and S. Enteritidis S003 with 0.76 and 1.61 log CFU/ml, respectively. Based on morphological, physical, biochemical and genetics properties, isolates CW2-3 and ST1-1 were identified as Klebsiella oxytoca and Acinetobacter sp., respectively. Crude mannanase activity from these two strains was characterized preliminarily. The pH optima of mannanase activity from Klebsiella oxytoca CW2-3 and Acinetobacter sp. ST1-1 were 7 and 6, respectively. The enzymes were stable at 4°C over a pH range of 3-6 and 3-10, respectively.

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Characterization of three .BETA.-mannanases of an alkalophilic Bacillus sp.

Cited by 46 publications

References 0 publications

Cloning and Characterization of a β-1,4-Mannanase 5C Possessing a Family 27 Carbohydrate-Binding Module from a Marine Bacterium,Vibriosp. Strain MA-138

Cloning and Characterization of a β-1,4-Mannanase 5C Possessing a Family 27 Carbohydrate-Binding Module from a Marine Bacterium,Vibriosp. Strain MA-138

Purification and characterization of β-Mannanase from Reinekea sp. KIT-YO10 with transglycosylation activity

Selection and characterization of mannanase-producing bacteria useful for the formation of prebiotic manno-oligosaccharides from copra meal

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