Rajeswari Mayavan Veeramuthu - Academia.edu (original) (raw)
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Papers by Rajeswari Mayavan Veeramuthu
Your article is protected by copyright and all rights are held exclusively by Springer-Verlag. Th... more Your article is protected by copyright and all rights are held exclusively by Springer-Verlag. This e-offprint is for personal use only and shall not be self-archived in electronic repositories. If you wish to self-archive your article, please use the accepted manuscript version for posting on your own website. You may further deposit the accepted manuscript version in any repository, provided it is only made publicly available 12 months after official publication or later and provided acknowledgement is given to the original source of publication and a link is inserted to the published article on Springer's website. The link must be accompanied by the following text: "The final publication is available at link.springer.com".
Bioprocess and …, Jan 1, 2012
Waste and Biomass …, Jan 1, 2012
Bacillus stearothermophilus secretes ,-mannanase and oa-galactosidase enzymatic activities capabl... more Bacillus stearothermophilus secretes ,-mannanase and oa-galactosidase enzymatic activities capable of hydrolyzing galactomannan substrates. Expression of the hemicellulase activities in the presence of locust bean gum was sequential, with mannanase activity preceding expression of aL-galactosidase activity. The hemicellulase activities were purified to homogeneity by a combination of ammonium sulfate fractionation, gel filtration, hydrophobic interaction chromatography, and ion-exchange and chromatofocusing techniques. The purified P-D-mannanase is a dimeric enzyme (162 kilodaltons) composed of subunits having identical molecular weight (73,000). Maximal activity did not vary between pH 5.5 and 7.5. The P-D-mannanase activity exhibited thermostabiity, retaining nearly full activity after incubation for 24 h at 70°C and pH 6.5. The enzyme displayed high specificity for galactomannan substrates, with no secondary xylanase or cellulase activity detected. Hydrolysis of locust bean gum yielded short oligosaccharides compatible with an endo mode of substrate depolymerization. Initial rate velocities of the mannanase activity displayed substrate inhibition and * Corresponding author. nents . This article describes the purification and characterization of two thermostable hemicellulases from Bacillus stearothermophilus. In the presence of galactomannan, B. stearothermophilus produces both a P-D-mannanase and an a-D-galactosidase activity. Both enzymes retain activity for more than 24 h at temperatures in excess of 60°C.
Your article is protected by copyright and all rights are held exclusively by Springer-Verlag. Th... more Your article is protected by copyright and all rights are held exclusively by Springer-Verlag. This e-offprint is for personal use only and shall not be self-archived in electronic repositories. If you wish to self-archive your article, please use the accepted manuscript version for posting on your own website. You may further deposit the accepted manuscript version in any repository, provided it is only made publicly available 12 months after official publication or later and provided acknowledgement is given to the original source of publication and a link is inserted to the published article on Springer's website. The link must be accompanied by the following text: "The final publication is available at link.springer.com".
Bioprocess and …, Jan 1, 2012
Waste and Biomass …, Jan 1, 2012
Bacillus stearothermophilus secretes ,-mannanase and oa-galactosidase enzymatic activities capabl... more Bacillus stearothermophilus secretes ,-mannanase and oa-galactosidase enzymatic activities capable of hydrolyzing galactomannan substrates. Expression of the hemicellulase activities in the presence of locust bean gum was sequential, with mannanase activity preceding expression of aL-galactosidase activity. The hemicellulase activities were purified to homogeneity by a combination of ammonium sulfate fractionation, gel filtration, hydrophobic interaction chromatography, and ion-exchange and chromatofocusing techniques. The purified P-D-mannanase is a dimeric enzyme (162 kilodaltons) composed of subunits having identical molecular weight (73,000). Maximal activity did not vary between pH 5.5 and 7.5. The P-D-mannanase activity exhibited thermostabiity, retaining nearly full activity after incubation for 24 h at 70°C and pH 6.5. The enzyme displayed high specificity for galactomannan substrates, with no secondary xylanase or cellulase activity detected. Hydrolysis of locust bean gum yielded short oligosaccharides compatible with an endo mode of substrate depolymerization. Initial rate velocities of the mannanase activity displayed substrate inhibition and * Corresponding author. nents . This article describes the purification and characterization of two thermostable hemicellulases from Bacillus stearothermophilus. In the presence of galactomannan, B. stearothermophilus produces both a P-D-mannanase and an a-D-galactosidase activity. Both enzymes retain activity for more than 24 h at temperatures in excess of 60°C.