Purification and Characterization of Cycloinulooligosaccharide Fructanotransferase (CFTase) from<i>Bacillus circulans</i>MCI-2554

Kushibe, Sachiko; Mitsui, Kaori; Yamagishi, M; Yamada, Kazunori; Morimoto, Yuuki

doi:10.1271/bbb.59.31

Cited by 12 publications

(13 citation statements)

References 3 publications

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“…TN88 (Nakamura et al, 1997), Aspergillus species (Vandamme and Derycke, 1993;Nakamura et al, 1994;Ettalibi and Barotti, 1987) and Fusarium oxysporum (Kaur et al, 1992), yeasts, e.g., Kluyveromyces marxianus CDBB-L-278 (Guerrero et al, 1995), Kluyveromyces fragilis and Debaryomyces cantarelli (Barthomeuf et al, 1991), Candida kefyr (Negoro and Kito, 1973), and bacteria, e.g., Bacillus circulans (Kushibe et al, 1995), Clostridium acetobutylicum ABKn8 (Efstahion et al, 1986), Pseudomonas sp. (Kim et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Parameters optimization for enzymatic assays using experimental design

Burkert

Kalil

Filho

et al. 2006

Braz. J. Chem. Eng.

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-The conditions for maximization enzymatic activity were determined using experimental design and inulinase from Kluyveromyces marxianus ATCC 16045. The effects of substrate concentration (sucrose and inulin), pH and temperature on inulinase activity were verified using four factorial design and surface response analysis. Using sucrose as substrate. It has bean shown that the effects sucrose on enzymatic activity is not statistically significant and the best condition for the highest activity (110 U/mL) was achieved with temperature between 60°C and 68°C and pH between 4.5 and 5.0. Using inulin as substrate it was verified that temperature is the only variable statistically significant and the maximum activity was 7.3 U/mL at temperature between 50°C and 51°C.

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Section: Introductionmentioning

confidence: 99%

Parameters optimization for enzymatic assays using experimental design

Burkert

Kalil

Filho

et al. 2006

Braz. J. Chem. Eng.

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“…Accordingly, cyclofructans are considered to have potential capacities as a novel host molecule in bioorganic chemistry, an ionophore, and an effective protectant of liposome. To date, three CFTases have been isolated and characterized, one each from Bacillus circulans OKUMZ31B (5), B. circulans MCI-2554 (10), and Bacillus macerans CFC1 (8). Only the CFTase gene (cft) from B. circulans MCI-2554 has been cloned and sequenced (GenBank/EMBL/DDBJ accession no.…”

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confidence: 99%

“…The CFTase of B. circulans MCI-2554 was deduced to consist of 1,503 amino acids with a calculated molecular mass of 167 kDa. Interestingly, the molecular mass of the purified CFTase from the culture supernatant of the Bacillus strain was reported to be 110 kDa (10). However, there was no report to explain why the calculated molecular mass of the cloned CFTase is different from that of the purified CFTase.…”

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confidence: 99%

Molecular Characterization of Cycloinulooligosaccharide Fructanotransferase from Bacillus macerans

Kim

Choi

2001

Appl Environ Microbiol

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Cycloinulooligosaccharide fructanotransferase (CFTase) converts inulin into cyclooligosaccharides of ␤-(231)-linked D-fructofuranose by catalyzing an intramolecular transfructosylation reaction. The CFTase gene was cloned and characterized from Bacillus macerans CFC1. The CFTase gene encoded a polypeptide of 1,333 amino acids with a calculated M r of 149,563. Western blot and zymography analyses revealed that the CFTase with a molecular mass of 150 kDa (CFT150) was processed (between Ser389 and Phe390 residue) to form a 107-kDa protein (CFT107) in the B. macerans CFC1 cells. The processed CFT107 was similar in its mass to the previously purified CFTase from B. macerans CFC1. The CFT107 enzyme was produced by B. macerans CFC1 but was not detected from the recombinant Escherichia coli cells, indicating that the processing event occurred in a host-specific manner. The two CFTases (CFT150 and CFT107) exhibited the same enzymatic properties, such as influences of pH and temperature on the enzyme activity, the intermolecular transfructosylation ability, and the ability of hydrolysis of cycloinulooligosaccharides produced by the cyclization reaction. However, the thermal stability of CFT107 was slightly higher than that of CFT150. The most striking difference between the two enzymes was observed in their K m values; the value for CFT150 (1.56 mM) was threefold lower than that for CFT107 (4.76 mM). Thus, the specificity constant (k cat /K m ) of CFT150 was about fourfold higher than that of CFT107. These results indicated that the N-terminal 358-residue region of CFT150 played a role in increasing the enzyme's binding affinity to the inulin substrate.

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“…9) With respect to the enzymes from P. polymyxa MGL21, the 148 kDa CFTase is reported to be inhibited by Cu 2+ ion 10) whereas no inhibition was observed either in the 108 kDa CFTase 11) or the enzyme in this study. The most remarkable difference between this enzyme and the enzymes from B. circulans OKUMZ31B, 2) B. circulans MCI 2554 7) and B. macerans CFC1 9) was the production ratio of cycloinulohexaose (CF 6) and cycloinuloheptaose (CF7) as shown in Table 3, indicating that the enzyme from P. polymyxa MG CF6 is capable of producing larger amounts of CF7 than the other enzymes. In this connection, crude enzyme prepared from culture broth of P. polymyxa MGL21 was found to produce CF6 and CF7 in a ratio of 2.7:1, 10) which was similar to that (2.5:1) in our purified enzyme.…”

Section: )mentioning

confidence: 93%

“…The enzyme was hardly inhibited by Cu 2+ ion, which inhibited both the enzymes from B. circulans MCI 2554 7) and B. macerans CFC1. 9) With respect to the enzymes from P. polymyxa MGL21, the 148 kDa CFTase is reported to be inhibited by Cu 2+ ion 10) whereas no inhibition was observed either in the 108 kDa CFTase 11) or the enzyme in this study.…”

Section: )mentioning

confidence: 96%