Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase

Ademark, Pia; Varga, Arthur; Medve, József; Harjunpää, Vesa; Drakenberg, Torbjörn; Tjerneld, Folke; Stålbrand, Henrik

doi:10.1016/s0168-1656(98)00086-8

Cited by 132 publications

(95 citation statements)

References 24 publications

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“…Aspergillus mannanases range from 30-110 kDa 24 while those of Trichoderma range from 32-46 kDa 25,26 . The optimum pH of mannanase S1 was similar to those of some bacterial and fungal mannanases which are in the range of 3.0-6.0 22,[26][27][28][29] . With regard to stability of mannanase S1, the results obtained suggest that mannanase S1 is quite stable at higher temperature with half life times of several hours in the temperature range of 50-70°C.…”

Section: Discussionsupporting

confidence: 52%

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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Section: Discussionsupporting

confidence: 52%

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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“…Similar degradation products were produced from ivory nut's mannan by -1,4-mannanases from Mytilus, T. reesei and A. niger (Xu et al, 2002a, Stalbrand et al, 1993Ademark et al, 1998).…”

Section: Discussionmentioning

confidence: 77%

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

Zahura¹,

Rahman²,

Inoue³

et al. 2010

Comparative Biochemistry and Physiology Part B: Biochemistry an

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“…The presence of galactose residues on the mannan backbone significantly hinders the activity of ␤-mannanase (252), but this effect is small if the galactose residues in the vicinity of the cleavage point are all on the same side of the main chain (251). ␤-Mannanases release predominantly mannobiose and mannotriose from mannan, confirming that they are true endohydrolases (4,64,105,306). It has been shown that A. niger ␤-mannanase binds to four mannose residues during catalysis (249).…”

Section: Degradation Of the Galacto(gluco)mannan Backbonementioning

confidence: 99%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

879

585

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SUMMARY Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.

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Softwood hemicellulose-degrading enzymes from Aspergillus niger: Purification and properties of a β-mannanase

Cited by 132 publications

References 24 publications

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

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

An endo-β-1,4-mannanase, AkMan, from the common sea hare Aplysia kurodai

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

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