The β-fructofuranosidase activities of a strain of Clostridium acetobutylicum grown on inulin

Looten, Ph.; Blanchet, Denis; Vandecasteele, J. P.

doi:10.1007/bf00253311

Cited by 30 publications

(8 citation statements)

References 9 publications

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“…From these results, it can be concluded that inulinase production from strain LS-A18 is inducible, and not constitutive. Similarly, production of extracellular exoinulinase from Clostridium acetobutylicum was significantly inhibited in the presence of glucose, fructose and sucrose (Looten et al 1987). Of the various concentrations of inulin tested, the maximum inulinase activity was observed at 4% (Fig.…”

Section: Effects Of Carbon Sources On Inulinase Productionmentioning

confidence: 85%

Alkaline inulinase production by a newly isolated bacterium Marinimicrobium sp. LS–A18 and inulin hydrolysis by the enzyme

Guo

2011

World J Microbiol Biotechnol

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To date, all of microbial inulinases reported showed optimal activity at pH values ranging from 3.5 to 7.0. A bacterial strain, Marinimicrobium sp. LS-A18, showing high extracellular inulinolytic activity was isolated from a marine solar saltern of the Yellow Sea in China. Maximum enzyme activity was obtained at 55°C and pH 9.0, respectively. The inulinase activity was induced by inulin, but not by the other carbon sources employed. Under the optimal medium and culture condition, the highest inulinase activity, 14.6 U/ml, was obtained after 96 h of incubation at shake flask level. The optimal medium for inulinase production was MHI medium containing 4% inulin, 1% peptone and 5% NaCl, while the optimal culture condition for inulinase production were pH 7.5, temperature 37°C, agitation speed 210 rpm, medium volume 40 ml in 250 ml shake flask, and incubation time 96 h. A large amount of monosaccharides was released after inulin hydrolysis by the inulinase from strain LS-A18. This is the first report on alkaline inulinase production from microorganism.

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Section: Effects Of Carbon Sources On Inulinase Productionmentioning

confidence: 85%

Alkaline inulinase production by a newly isolated bacterium Marinimicrobium sp. LS–A18 and inulin hydrolysis by the enzyme

Guo

2011

World J Microbiol Biotechnol

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“…This has also forced interest towards the microbial inulinases. Inulinases are produced by yeasts (Vandamme & Derycke 1983;Rouwenhorst et al 1990;Laloux et al 1991), filamentous fungi (Laloux et al 1991) and bacteria (Kunst et al 1977;Efstathiou et al 1986;Burne et al 1987;Looten et al 1987;Vullo et al 1991;Burne & Penders 1992).…”

Section: Introductionmentioning

confidence: 96%

Optimization of Process Parameters for the Production of Inulinase from a Newly Isolated Aspergillus niger AUP19

Kumar

Kunamneni

Prabhakar

et al. 2005

World J Microbiol Biotechnol

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Fifty strains were isolated from different soil samples on synthetic medium containing inulin as a sole carbon source for the production of extracellular inulinase. Of them, five isolates showed high inulinase activity and one of them was selected for identification and medium optimization studies. The isolate was identified as Aspergillus niger. Various physical and chemical parameters were optimized for inulinase production. Maximum productivity of inulinase (176 U ml )1 ) was achieved by employing medium containing 5% (w/v) inulin, galactose as additional carbon source, corn steep liquor and (NH 4 )H 2 PO 4 as nitrogen sources, incubation period of 72 h, incubation temperature of 28°C, pH 6.5, inoculum load at 10% (v/v) level and medium volume to flask volume ratio of 1:20 (v/v) with indented flasks.

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“…Levan-type fructans consist of P(2-*6)-linked fructosyl units with branching at the 2-1 position, while inulin-type fructans consist exclusively of 3(2-41)-linked fructosyl units with a terminal glucose unit (50). These fructanases (inulinases or levanases) are produced by yeasts (25,37,50), filamentous fungi (50), and bacteria such as Streptococcus mutans (6,7), Clostridium acetobutylicum (10,28), and B. subtilis (23,53). Inulinase (or levanase) activity is often compared with sucrase (or invertase) activity displayed by the same strain or enzyme preparation; the ratio of total sucrase units to total inulinase units is commonly expressed as the S/I ratio (50).…”

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confidence: 99%

Molecular characterization of a fructanase produced by Bacteroides fragilis BF-1

Blatch

Woods

1993

J Bacteriol

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The Bacteroidesfragilis BF-1 fructanase-encoding gene (fruA) was cloned and expressed in Escherichia coli from the recombinant plasmid pBS100. Expression of the fiuA gene was constitutive in E. coli(pBS100) and B. fragilis BF-1. The ratio of sucrase activity to inulinase activity (S/I ratio) was constant for enzyme preparations from E. coli(pBS100), indicating that both activities were associated with the fructanase. For B. fragilis BF-1, the S/I ratio varied considerably depending on the carbon source used for growth, suggesting that a separate sucrase is produced in addition to the fructanase in B. fragilis BF-1. Localization experiments and TnphoA mutagenesis indicated that the fructanase was exported to the periplasm. Sequence analysis of the N-terminal region of the fructanase revealed a putative 30-amino-acid signal peptide. The enzymatic properties of the purified fructanase were investigated. The enzyme was able to hydrolyze sucrose, raffinose, inulin, and levan but not melezitose, indicating that it was a 13-D-fructofuranosidase which was able to hydrolyze 10(2-4)-linked and 0(2-6)-linked fructans.The microbial hydrolysis of fructose-containing disaccharides, trisaccharides, and polymers involves two types of P-D-fructofuranosidase enzymes. The first type is able to efficiently hydrolyze low-molecular-weight, fructose-containing sugars such as sucrose and raffinose, but it has relatively low or nonexistent activity toward fructose polymers. Examples are the Saccharomyces cerevisiae invertase (26) and sucrases of Bacillus subtilis (11), Vbrio alginolyticus (42), Salmonella typhimurium (41), and Klebsiella pneumoniae (46). The second type of enzyme is able to hydrolyze fructose polymers such as levan and inulin in addition to sugars such as sucrose and raffinose. Levan-type fructans consist of P(2-*6)-linked fructosyl units with branching at the 2-1 position, while inulin-type fructans consist exclusively of 3(2-41)-linked fructosyl units with a terminal glucose unit (50). These fructanases (inulinases or levanases) are produced by yeasts (25,37,50), filamentous fungi (50), and bacteria such as Streptococcus mutans (6, 7), Clostridium acetobutylicum (10, 28), and B. subtilis (23, 53). Inulinase (or levanase) activity is often compared with sucrase (or invertase) activity displayed by the same strain or enzyme preparation; the ratio of total sucrase units to total inulinase units is commonly expressed as the S/I ratio (50). S/I values for real sucrases are relatively high numbers ranging from 1,600 to 28,300, while those for real fructanases are relatively low numbers ranging from 0.51 to 18.5.

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The β-fructofuranosidase activities of a strain of Clostridium acetobutylicum grown on inulin

Cited by 30 publications

References 9 publications

Alkaline inulinase production by a newly isolated bacterium Marinimicrobium sp. LS–A18 and inulin hydrolysis by the enzyme

Alkaline inulinase production by a newly isolated bacterium Marinimicrobium sp. LS–A18 and inulin hydrolysis by the enzyme

Optimization of Process Parameters for the Production of Inulinase from a Newly Isolated Aspergillus niger AUP19

Molecular characterization of a fructanase produced by Bacteroides fragilis BF-1

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