Expression and Characterization of Levansucrase from Clostridium acetobutylicum.

Abstract : The Clostridium acetobutylicum gene Ca-SacB encoding levansucrase was cloned and expressed in Escherichia coli. Ca-SacB is composed of 1287 bp and encodes 428 amino acid residues, which could convert 150 mmol/L sucrose to levan with the liberation of glucose. The optimum pH and temperature of this enzyme for levan formation were pH 6 and 60 °C, respectively. Levansucrase activity of Ca-SacB was completely abolished by 5 mmol/L Ag(+) and Hg(2+). The Km and Vmax values for levansucrase were calculated to be 64 mmol/L and 190 μmol/min/mg, respectively. Interestingly, Ca-SacB was found to have high product specificity, and no fructooligosaccharide was identified in the product, indicating that Ca-SacB may be valuable for industrial production of levan. In addition, Ca-SacB is the first characterized levansucrase isolated from an anaerobic bacterium, which should be valuable for exploring new enzyme resources and deepening the understanding of the catalytic mechanisms of levansucrases.
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Journal of Agricultural and Food Chemistry, American Chemical Society, 2017, 65 (4), pp.867-871. 〈10.1021/acs.jafc.6b05165〉
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Soumis le : mercredi 29 mars 2017 - 10:21:51
Dernière modification le : lundi 19 février 2018 - 14:34:04

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Song Gao, Xianghui Qi, Darren J Hart, Herui Gao, Yingfeng An. Expression and Characterization of Levansucrase from Clostridium acetobutylicum.. Journal of Agricultural and Food Chemistry, American Chemical Society, 2017, 65 (4), pp.867-871. 〈10.1021/acs.jafc.6b05165〉. 〈hal-01497700〉

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