Identification of two α-glucosidase activities in Clostridium acetobutylicum NCIB 8052

K. A. Albasheri, W. J. Mitchell

Research output: Contribution to journalArticle

Abstract

Maltose metabolism in the obligate anaerobe Clostridium acetobutylicum was studied. The sugar is accumulated via an energy-dependent transport process which is not a phosphotransferase. Cell extracts we}e incapable of phosphorylating maltose in the presence or absence of phosphoenolpyruvate or ATP, but exhibited hydrolytic activity against a range of glucoside substrates. The activity was predominantly in the soluble fraction of cell extracts, indicating a cytoplasmic location in the cell. Gel filtration on Sephadex G100 indicated the presence of at least two a-glucosidases. One enzyme (maltase) was active with maltose and maltotriose, while the other (pNPGase) hydrolysed isomaltose and several glucoside analogues, but neither showed activity against starch. Both glucosidases were induced by isomaltose, maltose, glucose and starch, but not by xylose, sucrose or cellobiose. In the presence of both glucose and maltose, growing cells showed a preference for glucose, apparently due to regulation of maltose transport, which did not occur in glucose-grown cells.

Original languageEnglish
Pages (from-to)149-156
Number of pages8
JournalJournal of Applied Bacteriology
Volume78
Issue number2
Publication statusPublished - 1995

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Clostridium acetobutylicum
glucosidases
maltose
isomaltose
glucose
glucosides
cells
starch
maltotriose
cellobiose
anaerobes
extracts
alpha-glucosidase
xylose
phosphotransferases (kinases)
gels
sucrose
sugars
metabolism
energy

Cite this

Albasheri, K. A. ; Mitchell, W. J. / Identification of two α-glucosidase activities in Clostridium acetobutylicum NCIB 8052. In: Journal of Applied Bacteriology. 1995 ; Vol. 78, No. 2. pp. 149-156.
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Identification of two α-glucosidase activities in Clostridium acetobutylicum NCIB 8052. / Albasheri, K. A.; Mitchell, W. J.

In: Journal of Applied Bacteriology, Vol. 78, No. 2, 1995, p. 149-156.

Research output: Contribution to journalArticle

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AU - Albasheri, K. A.

AU - Mitchell, W. J.

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AB - Maltose metabolism in the obligate anaerobe Clostridium acetobutylicum was studied. The sugar is accumulated via an energy-dependent transport process which is not a phosphotransferase. Cell extracts we}e incapable of phosphorylating maltose in the presence or absence of phosphoenolpyruvate or ATP, but exhibited hydrolytic activity against a range of glucoside substrates. The activity was predominantly in the soluble fraction of cell extracts, indicating a cytoplasmic location in the cell. Gel filtration on Sephadex G100 indicated the presence of at least two a-glucosidases. One enzyme (maltase) was active with maltose and maltotriose, while the other (pNPGase) hydrolysed isomaltose and several glucoside analogues, but neither showed activity against starch. Both glucosidases were induced by isomaltose, maltose, glucose and starch, but not by xylose, sucrose or cellobiose. In the presence of both glucose and maltose, growing cells showed a preference for glucose, apparently due to regulation of maltose transport, which did not occur in glucose-grown cells.

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