Purification and characterization of an endo-1,4-β-mannanase from Bacillus subtilis KU-1

Zakaria, M

doi:10.1016/s0378-1097(97)00494-1

Cited by 13 publications

(26 citation statements)

References 20 publications

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“…The specific activity of Man26P (514 U mg -1 ) is higher than that of MANB48 from Bacillus circulans strain K-1 (481.55 U mg -1 ) (Li et al 2008), MAN5C from Paecilomyces lilacinus (14.5 U mg -1 ) (Sugino et al 2004), Man26A from Bacillus sp. strain JAMB-750 (36.3 U mg -1 ) (Hatada et al 2005) and the b-mannanase from Bacillus subtilis KU-1 (407.7 U mg -1 ) (Zakakaria and Yagi 1998). It is similar that of Man26B from Clostridium thermocellum (520 U mg -1 ) (Kurokawa et al 2001), but lower than that of the b-mannanase from Streptomyces lividans 66 (876 U mg -1 ) (Arcand et al 1993) or ManA from alkaliphilic Bacillus sp.…”

Section: Discussionmentioning

confidence: 90%

“…Cu 2? has been shown to inhibit some mannanases (Zakakaria and Yagi 1998;Tamaru et al 1995). EDTA showed negative effects on the activity of Man26P, which indicates that it does not require divalent ions to function.…”

Section: Discussionmentioning

confidence: 99%

“…To date, numerous endo-b-1,4-mannanases and their respective genes have been identified and isolated from microorganisms such as Bacillus sp. (Zakakaria and Yagi 1998), Aspergillus sp. (Kanamasa et al 2001), Clostridium sp.…”

Section: Introductionmentioning

confidence: 99%

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

Jing

Shao

Hong

et al. 2010

World J Microbiol Biotechnol

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This paper describes the construction of a genomic library from the bacterium Pantoea agglomerans A021 and the subsequent cloning and expression of a novel mannanase gene (man26P). The gene consists of 1,047 bp and encodes a peptide (Man26P) of 348 amino acids with a calculated molecular mass of 38.5 kDa. Man26P is 63% identical with mannanase from Pectobacterium carotovorum at protein level and considered to be a member of the glycoside hydrolase family 26 (GH26). Man26P was expressed efficiently in E.coli BL21 (DE3) after induction with isopropylthiogalactoside (IPTG) and purified with a GST Bind Purification Kit. Maximum activity of purified Man26P was 514 U mg -1 , which was seen at pH 6.0 and a temperature of 55°C. Man26P was stable on exposure to buffers ranging from pH 4.0-10.0, and tolerant of temperature below 60°C. Zn 2? , Mg 2? and Co 2? enhanced the activity, while Mn 2? , Cu 2? and Hg ? had a negative effect. b-mercaptoethanol (1%) increased the activity twofold, while SDS (1%) inhibited it significantly. The enzyme showed optimal activity in a NaCl solution. The properties make it a candidate for various industrial applications.

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Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

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

Jing

Shao

Hong

et al. 2010

World J Microbiol Biotechnol

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“…Bacillus spp. mannanases have a molecular mass in the range of 37-40 kDa [20][21][22] . Nevertheless, Takeda et al 23 reported that the purified mannanase from Bacillus sp.…”

Section: Discussionmentioning

confidence: 99%

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Chantorn¹,

Pongsapipatana²,

Keawsompong³

et al. 2013

ScienceAsia

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The mannanase S1 from Klebsiella oxytoca KUB-CW2-3 was purified by a single anion exchange chromatography to electrophoretic homogeneity. S1 is a protein with a molecular mass of approximately 165 kDa and a pI value of 3.5. The optimum pH and temperature of mannanase activity were 4.0 and 40°C, respectively. The enzyme exhibited good stability over the broad pH range of 3-6. The mannanase S1 exhibited specific activity for different mannan substrates including galactomannan from locust bean gum (LBG), copra meal, and glucomannan from konjac, while neither xylanase nor cellulase activity were detectable. The Michaelis-Menten constants (Km), maximum velocity (Vmax), and the catalytic constant (kcat) values of S1 against LBG and konjac mannan were 1.038-1.056 mg/ml, 6.149-6.183 µU ml −1 min −1 , and 0.047 s −1 , respectively. In addition, mannanase activity was activated by Co 2+ (129%) but completely inhibited by EDTA and Zn 2+ . The N-terminal amino acid sequence (GRVGEAGPHGPHGPH) of mannanase S1is different from the N-terminal region of other bacterial mannanases belonging to the glycoside hydrolase family GH5. The degradation products of mannanase S1 from LBG hydrolysis were galactose and unknown oligosaccharides with a different molecular structure to mannobiose, triose, and tetraose indicating the cleavages of α-1,6-galactosidic and β-1,4-mannosidic linkages. Its hydrolysis of 100 mM CoCl2-treated copra mannan enhanced the growth of Lactobacillus reuteri KUB-AC5 but inhibited that of Salmonella serovar Enteritidis S003, indicating potential prebiotic properties by the action of mannanase from K. oxytoca.

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“…Mannanases are produced mainly by members of the genus Bacillus. Bacillus subtilis is recommended because of its safety, fast growth, and ability to secrete high levels of mannanase into the medium (Khanongnuch et al 1998;Zakaria et al 1998;Jiang et al 2006;Dhawan and Kaur 2007). Despite having high practical potential, the use of mannanase is still limited, due to low yields and high production costs (Dhawan and Kaur 2007;Zhang et al 2000).…”

Section: Introductionmentioning

confidence: 99%

Enhanced production of a thermostable mannanase by immobilized cells of Bacillus subtilis on various membranes

Yan

Jiang

et al. 2009

World J Microbiol Biotechnol

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Cells of the thermophilic Bacillus subtilis WY34 were immobilized on various formaldehyde-activated polymer membranes and the immobilized cells were used for the production of thermostable mannanase in flasks. The results showed that polyethersulfone membranes (PES) and nylon-6 membranes were the most suitable supports for cell immobilization to produce the mannanase. Moreover, PES and nylon-6 membranes immobilized cells provided 1.78-and 1.74-fold higher mannanase activity compared to the control after 4 days of cultivation, respectively. The immobilized cells on PES and nylon-6 membranes had good stability and retained 131.5 and 114.3% of ability of enzyme production even after six cycles of repeated batch fermentation, respectively. Active cell growth was observed by scanning electron microscopy (SEM) after 16 days (four cycles) repeated batch cultivation. Therefore, the membrane-immobilized cells of B. subtilis WY34 can be proposed as an effective biocatalyst for repeated usage for production of the thermostable mannanase.

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Purification and characterization of an endo-1,4-β-mannanase from Bacillus subtilis KU-1

Cited by 13 publications

References 20 publications

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

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

Characterization of mannanase S1 from Klebsiella oxytoca KUB-CW2-3 and its application in copra mannan hydrolysis

Enhanced production of a thermostable mannanase by immobilized cells of Bacillus subtilis on various membranes

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