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PMID:20372022
| Citation |
Fu, X, Huang, X, Liu, P, Lin, L, Wu, G, Li, C, Feng, C and Hong, Y (2010) Cloning and characterization of a novel mannanase from Paenibacillus sp. BME-14. J. Microbiol. Biotechnol. 20:518-24 |
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| Abstract |
A mannanase gene (man26B) was obtained from a sea bacterium, Paenibacillus sp. BME-14, through the constructed genomic library and inverse PCR. The gene of man26B had an open reading frame of 1,428 bp that encoded a peptide of 475- amino acid residues with a calculated molecular mass of 53 kDa. Man26B possessed two domains, a carbohydrate binding module (CBM) belonging to family 6 and a family 26 catalytic domain (CD) of glycosyl hydrolases, which showed the highest homology to Cel44C of P. polymyxa (60% identity). The optimum pH and temperature for enzymatic activity of Man26B were 4.5 and 60 degrees C, respectively. The activity of Man26B was not affected by Mg(2+) and Co(2+), but was inhibited by Hg(2+), Ca(2+), Cu(2+), Mn(2+), K(+), Na(+), and beta-mercaptoethanol, and slightly enhanced by Pb(2+) and Zn(2+). EDTA did not affect the activity of Man26B, which indicates that it does not require divalent ions to function. Man26B showed a high specific activity for LBG and konjac glucomannan, with K(m), V(max), and k(cat) values of 3.80 mg/ml, 91.70 micromol/min/mg protein, and 77.08/s, respectively, being observed when LBG was the substrate. Furthermore, deletion of the CBM6 domain increased the enzyme stability while enabling it to retain 80% and 60% of its initial activity after treatment at 80 degrees C and 90 degrees C for 30 min, respectively. This finding will be useful in industrial applications of Man26B, because of the harsh circumstances associated with such processes. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Cations/metabolism; Cloning, Molecular; DNA, Bacterial/chemistry; DNA, Bacterial/genetics; Electrophoresis, Polyacrylamide Gel; Enzyme Stability/physiology; Hydrogen-Ion Concentration; Molecular Sequence Data; Molecular Weight; Paenibacillus/enzymology; Paenibacillus/genetics; Polymerase Chain Reaction; Sequence Alignment; Substrate Specificity; beta-Mannosidase/chemistry; beta-Mannosidase/genetics; beta-Mannosidase/isolation & purification; beta-Mannosidase/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0016985: mannan endo-1,4-beta-mannosidase activity |
ECO:0000314: |
F |
Table 2. "...these data demonstrate that Man26B is a mannanase with narrow substrate specificity. Specifically, these results indicate that the enzyme does not hydrolyze other polysaccharides and that it specifically cleaves the β-1,4-glycosidic linkages between mannopyranosyl residues." |
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See also
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