Konjac-mannanase from the Tubers of Amorphophallus konjac C. Koch

Sugiyama, Noboru; Shimahara, Hideo; Andoh, Tetsuo; Takemoto, Motoko

doi:10.1271/bbb1961.37.9

Cited by 10 publications

(5 citation statements)

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“…The present pI is higher than that of other sources like actinomycetes and fungi [16] where it was reported to be 3.4 and 4.1. The determined K m (0.91%) and V mx (2935 U mg 3I ) for GM of the present mannanase were higher than those of other L-mannanases [6,8,9]. The enzyme was strongly inhibited by Hg P , Cr P , Mn P , Ag P , Cu P .…”

Section: Discussionmentioning

confidence: 58%

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

Zakaria¹

1998

FEMS Microbiology Letters

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Endo-1,4-L-mannanase was purified to homogeneity from the culture supernatant of Bacillus subtilis KU-1 by ammonium sulfate precipitation, DEAE-Toyopearl, phenyl-Sepharose and FPLC Mono Q column chromatography by 810-fold with 39% yield. The molecular mass of the enzyme was estimated to be 39 kDa by SDS-PAGE and 40 kDa by gel filtration. It had a pI of 4.5 with maximum activity at pH 7.0 and 50^55³C. It was stable for 48 h between pH 4.5 and 9.0, and for 1 h up to 60³C. The enzyme activity was strongly inhibited by Hg P , Ag P , Cu P , Mn P , and Cr P . The amino acid composition of the enzyme was in the order Asx s Glx s Leu s Try s Ser. ß 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V.

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Section: Discussionmentioning

confidence: 58%

“…Recently, more attention has been focused on ex-traction and utilization of L-mannanases from various sources including plants [6,7], bacteria [8^13], fungi [14^17], actinomycetes [18] and even molluscs [19]. Bacterial sources are preferred when large amounts of enzyme are required.…”

Section: Introductionmentioning

confidence: 99%

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

Zakaria¹

1998

FEMS Microbiology Letters

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“…The present p I is higher than that of other sources like actinomycetes and fungi [16] where it was reported to be 3.4 and 4.1. The determined K m (0.91%) and V max (2935 U mg −1 ) for GM of the present mannanase were higher than those of other β‐mannanases [6, 8, 9]. The enzyme was strongly inhibited by Hg 2+ , Cr 2+ , Mn 2+ , Ag 2+ , Cu 2+ .…”

Section: Discussionmentioning

confidence: 61%

“…Recently, more attention has been focused on extraction and utilization of β‐mannanases from various sources including plants [6, 7], bacteria [8–13], fungi [14–17], actinomycetes [18] and even molluscs [19]. Bacterial sources are preferred when large amounts of enzyme are required.…”

Section: Introductionmentioning

confidence: 99%

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

Zakaria

Yamamoto

Yagi

1998

FEMS Microbiology Letters

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Endo‐1,4‐β‐mannanase was purified to homogeneity from the culture supernatant of Bacillus subtilis KU‐1 by ammonium sulfate precipitation, DEAE‐Toyopearl, phenyl‐Sepharose and FPLC Mono Q column chromatography by 810‐fold with 39% yield. The molecular mass of the enzyme was estimated to be 39 kDa by SDS‐PAGE and 40 kDa by gel filtration. It had a pI of 4.5 with maximum activity at pH 7.0 and 50–55°C. It was stable for 48 h between pH 4.5 and 9.0, and for 1 h up to 60°C. The enzyme activity was strongly inhibited by Hg2+, Ag2+, Cu2+, Mn2+, and Cr2+. The amino acid composition of the enzyme was in the order Asx>Glx>Leu>Try>Ser.

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“…Hydrolysis of locust bean gum by 100 mM CoCl 2 treated mannanase S1 yielded galactose and unknown compounds which moved further than mannotriose and mannotetraose on TLC. Sugiyama et al 35 reported that hydrolysis of mannan can result in various kinds of unknown oligosaccharides and unknown substances. These unknown compounds may be mannooligosaccharides carrying side chains that can result from transferase activity of the hydrolase.…”

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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Konjac-mannanase from the Tubers of Amorphophallus konjac C. Koch

Abstract: A crude enzyme preparation hydrolyzing konjac mannan was extracted from germinating konjac tubers, and purified by chromatography with DEAE-cellulose and alkali-swollen cellulose, and by gel-filtration on Sephadex G-100. The purified enzyme preparation showed

Cited by 10 publications

References 0 publications

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

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

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

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

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