Bacillus agaradhaerens LS-3C cyclodextrin glycosyltransferase: activity and stability features

Martins, Rita; Hatti‐Kaul, Rajni

doi:10.1016/s0141-0229(03)00215-1

Cited by 33 publications

(37 citation statements)

References 41 publications

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“…There are only several reports on the effect of reaction temperature on the β-CD formation. In the study of Martins and Hatti-Kaul (2002) and Martins and Hatti-Kaul (2003), the β-CD formation by the CGTase from B. agaradhaerens LS-3C was also found highest at 50ºC. Although the maximum activity of CGTase was found at 55ºC, the β-CD formation drastically decreased at 55ºC and 60ºC.…”

Section: Resultsmentioning

confidence: 94%

“…According to the literature data, the CGTase can directly cyclize oligosaccharides consisting of at least eight glucose units. The shorter oligosaccharide chain has to be first lengthened by disproportion action of the enzyme and then cyclized (Martins and Hatti-Kaul, 2003). The longer the chain, the higher the amount of cyclodextrin formed (Brunet et al 1998).…”

Section: Resultsmentioning

confidence: 99%

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Kinetic characteristics of β-cyclodextrin production by cyclodextrin glycosyltransferase from newly isolated Bacillus sp. C26

Cheirsilp

Kitcha

Maneerat

2010

Electron. J. Biotechnol.

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The kinetic characteristics of β-cyclodextrin production by a cyclodextrin glycosyltransferase (CGTase) produced by Bacillus sp. C26, a new isolate from a soil sample was investigated. Considering highest yield and initial production rate of β-cyclodextrin, among the starches examined, soluble starch, tapioca starch, sago starch, corn starch and rice starch, tapioca starch was the best substrate for this CGTase. The optimum temperature for tapioca starch gelatinization prior to its use as a substrate for β-cyclodextrin production was 65ºC. The yield and initial production rate of β-cyclodextrin increased with increasing starch concentration up to 6% and an enzyme concentration up to 48 U/g-starch. The kinetic parameters of V max and K m of β-cyclodextrin production from tapioca starch by CGTase were 1.59 mg/mL/h and 22.3 mg/mL, respectively. Considering high initial production rate and high yield of β-cyclodextrin, the optimum reaction temperature was at 50ºC. This study provided the necessary kinetic information that may be useful to define the most suitable condition for industrialized production of β-cyclodextrin with the high yield and productivity.

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Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Kinetic characteristics of β-cyclodextrin production by cyclodextrin glycosyltransferase from newly isolated Bacillus sp. C26

Cheirsilp

Kitcha

Maneerat

2010

Electron. J. Biotechnol.

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“…However, low cyclization activities have also been reported for CGTases from thermophilic Thermoanaerobacter sp. P4 (Avci and Donmez, 2009), Bacillus agaradhaerens LS-3C (Martins and Hatti-Kaul, 2003) and Bacillus sphaericus (Moriwaki et al, 2009). As shown in Figure 1, within 12 h of fermentation, the amount of CGTase production was very small and could hardly be detected.…”

Section: Sk13002mentioning

confidence: 98%

“…However, it increased steadily until it reached the maximum of 0.141 U/ml after 66 h. There was also significant starch hydrolysis or amylolytic activity that proceeded alongside CGTase production which also reached the highest value of 4.38 U/ml at 66 h. The cell growth and the production of CGTase did not occur at the same rate as the CGTase production lagged behind. Although hydrolysis and cyclization are all performed at a unique active site in the enzyme, they proceed via different kinetic mechanisms (Martins and Hatti-Kaul, 2003;Van der Veen et al, 2000). This hydrolysis side reaction is undesirable, since it produces short saccharides that are responsible for accelerating the breakdown of the cyclodextrins during the coupling reaction, thus limiting the final product yields (Kelly et al, 2008).…”

Section: Sk13002mentioning

confidence: 99%

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Sun¹,

Letsididi²,

Pan³

2013

Afr. J. Microbiol. Res.

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A β-cyclodextrin glycosyltransferase (β-CGTase) from a new alkalitolerant Bacillus sp. SK 13.002 strain which can significantly hydrolyze starch into short linear saccharides, in addition to production of cyclodextrins (CDs) was produced. The hydrolytic activity of this CGTase as a side reaction is thought to be due to partial retention of ancestral enzyme function from evolution over time. This CGTase is therefore another example of an enzyme at an intermediary stage in between ''true'' α-amylases and ''true'' CGTases. The strain also produced two CGTase isozymes which were purified to homogeneity using DEAE-Sepharose anion exchange chromatography and Superdex 75 gel filtration chromatography to show Molecular masses of 67.5 and 46.8 kDa on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) respectively, which were confirmed by liquid chromatography/mass spectrometry (LC/MS) analysis to be 67.6 and 47.3 kDa, respectively. Both CGTase isozymes formed CDs from soluble starch. Most of the reported CGTases were composed of one single enzyme with only a few strains having CGTase isozymes showing different isoelectric points. Therefore, Bacillus sp. SK 13.002 strain is another Bacillus capable of producing CGTase isozymes which were individually purified to homogeneity.

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“…CGTases are produced by various bacteria, mainly by mesophilic bacteria such as Bacillus macerans (Stavn and Granum, 1979), Bacillus circulans (Szerman et al, 2007), Bacillus firmus (Saverage et al, 2008), Bacillus agaradhaerens LS-3C (Martins and Hatti Kaul, 2003), Paenibacillus pabuli US132 (Jemli et al, 2007) Klebsiella pneumoniae AS-22 (Gawande and Patkar, 2001) and Brevibacterium sp 9605 (Mori et al, 1994). In general, B. macerans is used in the commercial productions (Biwer et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a thermostable cyclodextrin glycosyltransferase from Thermoanaerobacter sp. P4

Avcı¹,

Dönmez²

2012

Afr. J. Biotechnol.

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Cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19) from a thermophilic anaerobic bacterium, Thermoanaerobacter sp. P4, was purified by ammonium sulfate precipitation followed by α-cyclodextrin epoxy activated-sepharose 6B column chromatography. Enzyme was purified 141 fold and had the specific activity of 143.8 U/mg proteins. Purification yields after ammonium sulfate precipitation and affinity chromatography were 25.8 and 17.8%, respectively. SDS-PAGE analysis showed that enzyme was purified successfully and had a single band. Molecular weight of the enzyme was determined as 68.7 kDa. The enzyme had optimum cyclization activity at 80 to 90°C and hydrolyzing activity at 90°C and maintained 87 and 95% of these activities at 95°C, respectively. Optimal pH was found as 7.0. It retained full activity at 80°C for 4 h. Enzyme was strongly inhibited by HgSO 4 and AgNO 3 . Addition of 1 mM CaCl 2 increased the enzymatic activity up to 7%. This novel enzyme could be a good candidate for industrial applications according to its characteristic found in the current study.

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Bacillus agaradhaerens LS-3C cyclodextrin glycosyltransferase: activity and stability features

Cited by 33 publications

References 41 publications

Kinetic characteristics of β-cyclodextrin production by cyclodextrin glycosyltransferase from newly isolated Bacillus sp. C26

Kinetic characteristics of β-cyclodextrin production by cyclodextrin glycosyltransferase from newly isolated Bacillus sp. C26

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Purification and characterization of a thermostable cyclodextrin glycosyltransferase from Thermoanaerobacter sp. P4

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