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Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry
Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry
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Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry
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Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry
Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry

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Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry
Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry
Journal Article

Production of CGTase by a Bacillus alkalophilic CGII strain isolated from wastewater of a manioc flour industry

2004
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Overview
GCTase production by a new strain of Bacillus alkalophilic CGII isolated from Brazilian wastewater of manioc flour industry was examined. The growth medium used was composed by 1.5% starch, 1.5% nitrogen and 1% Na2CO3. Higher activity was obtained with starch, maltodextrin and galactose. When glucose was added to the medium, no enzyme production was observed. High enzyme activity and growth were reached when aeration was increased (88.6 U/mL). The enzyme characterization showed an optimum pH and temperature 8.0 and 55ºC for starch hydrolyses, respectively. Mg+ and Ca++ showed small activation; however, Hg+ and Cu+ showed a strong enzyme inhibition. Estudou-se a produção de CGTase por uma nova cepa de Bacillus alkalophilic CGII, isolada de água residuária de uma fecularia de mandioca, durante cultivo em meio composto de 1,5% de amido, 1,5% de fonte de nitrogênio e 1% Na2CO3. A atividade enzimática foi alta quando se utilizou amido, maltodextrina e galactose como fontes de carbono. Quando se utilizou glicose no meio de cultivo não se observou produção da enzima. Atividade enzimática alta (88,6 U/mL) e melhor crescimento foram obtidos quando se aumentou a aeração. A caracterização da enzima mostrou um pH ótimo de 8,0 e temperatura ótima de 55ºC sendo que a enzima sofreu uma pequena ativação por Mg+ e Ca++. A enzima foi fortemente inibida por Hg+ e Cu+.

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