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Regulation and properties of an invertase from Clostridium pasteurianum.
Metadata
Journalcanadian journal of microbiology1.793Date
1975-Nov
Publication Type
Journal Article
Volume
1975-Nov / 21 : 1711-8
Author
Laishley EJ
DoiPMIDMESH
Cell-Free System
Clostridium
Cysteine
Dithionitrobenzoic Acid
Enzyme Induction
Enzyme Repression
Fructose
Glucose
Hot Temperature
Hydrogen-Ion Concentration
Hydroxymercuribenzoates
Phosphates
Sucrase
Sucrose
Abstract
An intracellular invertase was induced in cultures of Clostridium pasteurianum utilizing sucrose as its carbon source for growth. This enzyme synthesis could be repressed by the addition of fructose of a sucrose-growing culture. In contrast, invertase activity was not affected by the addition of glucose to sucrose-growing cells and this enzyme could be induced in a glucose-metabolizing culture by the addition of sucrose. This enzyme was purified 10.5-fold over the induced lese, EC 3.2.1.26) by substrate-specificity studies. Invertase had a pH optimum of 6.5 and an apparent Km of 79.5 mM for sucrose, and required high concentration of potassium phosphate for maximum activity. Invertase was completely inactivated by a 2-min heat treatment at 60 degrees C. This enzyme was strongly inhibited by p-hydroxymercuribenzoate (pCMB) and weakly inhibited by 5,5'-dithiobis(2-nitrobenzoic acid), while cysteine could substantially reverse pCMB) inhibition, suggesting that sulfhydryl group(s) were necessary for invertase activity.
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Can J Microbiolcanadian journal of microbiology
Metadata
LocationCanada
FromCANADIAN SCIENCE PUBLISHING

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