High-level production, purification and characterization of a thermostable β-mannanase from the newly isolated Bacillus subtilis WY34

Jiang, Zhengqiang; Wang, Yun; Li, Daoyi; Li-te, LI; Chai, Pingping; Kusakabe, Isao

doi:10.1016/j.carbpol.2006.02.030

Cited by 138 publications

(110 citation statements)

References 27 publications

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“…Different ability to degrade mannan substrate has been shown by isolate RA05 which was not able to degrade mannan of sugar palm but it had the activity on PKC (Meryandini et al, 2010). Bacillus subtilis WY34 exhibited high activity on galactomannan from LBG (100%), but just 56.8% in Konjac powder, 20.4% in copra mannan and 10.7% in guar gum galactomannan (Jiang et al, 2006). The optimum time of mannanase production was then used as the standard for the harvesting time of bacterial cells crude extract in the following mannanase production.…”

Section: Resultsmentioning

confidence: 99%

Characterization of Bacterial Mannanase for Hydrolyzing Palm Kernel Cake to Produce Manno-oligosaccharides Prebiotics

Utami¹,

Meryandini²,

Wiryawan³

2013

Med Pet

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Palm kernel cake (PKC) is a promising source of prebiotics, since it contains high amount of β-mannan which can be further hydrolyzed to manno-oligasaccharides (MOS), a prebiotic. Therefore, this research was carried out to analyze the capability of a bacterial isolate (A2 isolates) previously isolated from soils sample from around IPB campus to hydrolyze PKC. Based on 16S-DNA analysis, isolate A2 was identified as Brevibacillus borstelensis. Mannanase of A2 isolate had an optimum condition at 90 o C and pH 7. Mannanase activity of crude extracts using Locust Bean Gum (LBG) and PKC as substrates were 0.37U/mL and 0.032U/mL, respectively. However, the most favorable production of oligosaccharides based on the degree of polymerization was obtained after 72-h of incubation with the ratio of substrate:enzyme, 1.2:1, on 1.5% PKC as substrate. The manno-oligosaccharides prebiotic obtained was found to interfere the growth of both lactic acid bacteria (Lactobacillus casei) and pathogenic microflora (Escherichia coli). E. coli apparently could not use this prebiotic as the carbon sources, in contrast to L. casei. Substitution of carbon source in medium with prebiotics reduced the capability of L. casei to produce organic acids. It is concluded that local A2 isolate (B. borstelensis) produces mannanase which can be used to produce prebiotics from PKC. Key words: Brevibacillus borstelensis, mannanase, Lactobacillus casei, PKC ABSTRAKKomponen utama dari bungkil inti sawit (BIS) adalah β-manan yang dapat digunakan dalam produksi prebiotik Manno-oligosakarida (MOS). Penelitian ini bertujuan mengkarakterisasi kemampuan isolat bakteri A2 yang diisolasi dari sampel tanah di sekitar kampus IPB dalam mendegradasi BIS. Berdasarkan analisis 16S-DNA isolat A2 teridentifikasi sebagai Brevibacillus borstelensis. Mananase isolat A2 memiliki kondisi optimum pada suhu 90 o C dan pH 7. Aktivitas mananase isolat A2 pada media dengan Locust Bean Gum (LBG) dan BIS berturut turut adalah 0.37U/ml dan 0.032U/ml. Perbandingan substrat:enzyme: 1.2:1, pada substrat BIS 1.5% memberikan derajat polimerisasi terbaik bagi produksi oligosakarida. Prebiotik MOS ini dapat mempengaruhi pertumbuhan Escherichia coli patogen dan Lactobacillus casei. E. coli tidak dapat menggunakan prebiotik ini sebagai sumber karbon dibandingkan L. casei. Substitusi sumber karbon dengan prebiotik menurunkan kemampuan L. casei dalam memproduksi asam organik. Disimpulkan bahwa isolat lokal A2 (B. borstelensis) menghasilkan mananase yang dapat digunakan untuk menghasilkan prebiotik dari BIS. Kata kunci: Brevibacillus borstelensis, mananase, Lactobacillus casei, PKC

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Section: Resultsmentioning

confidence: 99%

Characterization of Bacterial Mannanase for Hydrolyzing Palm Kernel Cake to Produce Manno-oligosaccharides Prebiotics

Utami¹,

Meryandini²,

Wiryawan³

2013

Med Pet

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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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“…At optimum pH, the structure and active site of an enzyme are in the most suitable condition to bind substrate, resulting in a maximum activity. Microorganism has high diversity in the sensitivity to pH changes, i.e., Streptomyces galbus NR has an optimum pH of 6.5 (Kansoh & Nagieb, 2004), whereas for bacterias, Bacillussubtilis WY34 the optimum pH was 6 (Jiang, 2006). For fungal, Aspergillus niger and Trichoderma spp,the highest activity was found at pH of 5 (Adesina et al, 2013).…”

Section: Mannanase Characterizationmentioning

confidence: 99%

“…It indicates that mannanase belongs to endo-mannanase type. Endo-mananase can degrade mannan polysaccharide to mannotetraose, mannotriose, and mannobiose (Jiang et al, 2006). The gure 3 The effect of temperature on the activity of mannanase Streptomyces violascensBF 3.10 measured at pH 6. gure 4 Mannanase stability of Streptomyces violascensBF 3.10 at different storage temperatures measured at pH 6.…”

Section: Analyzing Mannooligosaccharides By Using Tlc and Hplcmentioning

confidence: 99%

Enzymatic Hydrolysis of Porang by Streptomyces violascens BF 3.10 Mannanase for the Production of Mannooligosaccharides

Safitri

Meryandini

Yopi

2014

Med Pet

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Porang (Amorphophallus muelleriBlumeo C dengan aktivitas enzim sebesar 16.38 U/mL dan stabil pada suhu 4 °C selama 48 jam. Selama 5 jam waktu hidrolisis, reaksi dengan konsentrasi substrat 0,25%, 0,5%, dan 1% glukomanan porang yang dilarutkan dalam 10 mL enzim menghasilkan manooligosakarida dengan derajat polimerisasi 2-3. Visualisasi produk hidrolisis mengggunakan metode thin layer chromatography (TLC) dan high performance liquid chromatography (HPLC) menunjukkan bahwa jenis manooligosakarida yang dihasilkan adalah glukosa, manobiosa, manotriosa, dan manotetrosa. Derajat polimerisasi dan gula-gula sederhana yang terbentuk menunjukkan bahwa mananase S. violascens bekerja secara aktif mengatalisis reaksi hidrolisis ikatan 1,4-β-D-manosida dari rantai utama β-1,4-mannan sehingga menghasilkan gula-gula sederhana manooligosakarida.

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High-level production, purification and characterization of a thermostable β-mannanase from the newly isolated Bacillus subtilis WY34

Cited by 138 publications

References 27 publications

Characterization of Bacterial Mannanase for Hydrolyzing Palm Kernel Cake to Produce Manno-oligosaccharides Prebiotics

Characterization of Bacterial Mannanase for Hydrolyzing Palm Kernel Cake to Produce Manno-oligosaccharides Prebiotics

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

Enzymatic Hydrolysis of Porang by Streptomyces violascens BF 3.10 Mannanase for the Production of Mannooligosaccharides

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