Biochemical characterization of the cutinases from Thermobifida fusca

Chen, Sheng; Su, Lingqia; Billig, Susan; Zimmermann, Wolfgang; Chen, Jian; Wu, Jing

doi:10.1016/j.molcatb.2010.01.001

Cited by 83 publications

(56 citation statements)

References 31 publications

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“…This property is similar to that of the cutinase from A. brassicicola (Koschorreck et al, 2010). TtcutB from T. terrestris showed a strong preference for substrates with short acyl chain length, which is a typical characteristic of cutinases (Chen et al, 2010;Rubio et al, 2008). Though the substrate specificity of TtcutB toward pNP esters is similar to that of TtcutA from T. terrestris CAU709 , the specific activities of TtcutB for triglycerides are approximately 2-3 times higher than that of TtcutA (Table 2).…”

Section: Discussionsupporting

confidence: 52%

Characterization of an acidic cold-adapted cutinase from Thielavia terrestris and its application in flavor ester synthesis

Yan

Duan

et al. 2015

Food Chemistry

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Section: Discussionsupporting

confidence: 52%

Characterization of an acidic cold-adapted cutinase from Thielavia terrestris and its application in flavor ester synthesis

Yan

Duan

et al. 2015

Food Chemistry

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“…harzanum [42] and Cryptococcus magnus [55], and the bacteria T. fusca [56], T. alba [57] and T. cellulosilytica [58]. Similarly, activity and efficiency of FoCut5a (i.e.…”

Section: Kinetic Studies Of the Recombinant Cutinasementioning

confidence: 99%

Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

Dimarogona

Nikolaivits

Kanelli

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

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“…In the present work, TDOC that does not inhibit the activity of cutinase [29], was used to increase the leakage of recombinant cutinase from periplasm to culture medium [30]. TDOC was added into the culture after 16 h of cultivation when the value of OD 600 reached about 4.0.…”

Section: Effect Of Surfactant On Translocation Of Recombinant Cutinasmentioning

confidence: 99%

Study on Improvement of Extracellular Production of Recombinant Thermobifida fusca Cutinase by Escherichia coli

Chen

Liu

Chen

et al. 2011

Appl Biochem Biotechnol

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Escherichia coli is one of the most commonly used host strains for recombinant protein production. More and more research works on the production of recombinant protein indicate that extracellular production throughout a culture medium is more convenient and attractive compared to intracellular production. In present work, inducing temperature and isopropyl β-D: -1-thiogalactopyranoside (IPTG) concentration were investigated to decrease the formation of inclusion body and increase the amount of soluble recombinant cutinase initially. Enzyme activity in the culture medium reached to 118.9 U/ml at 64 h of culture, and no inclusion body was detected in cytoplasm under the inducement condition of 0.2 mM IPTG and 30°C. In addition, it was found that a large amount of cutinase had been accumulated in periplasm since 16-h cultivation under the same inducement condition. Therefore, glycine and surfactant sodium taurodeoxycholate (TDOC) were further used to promote the leakage of recombinant cutinase from periplasm. Supplied with 100 mM glycine and 1 mM TDOC, the amount of cutinase in periplasm decreased remarkably, and the activity in the culture medium reached to 146.2 and 149.2 U/ml after 54 h of culturing, respectively.

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Biochemical characterization of the cutinases from Thermobifida fusca

Cited by 83 publications

References 31 publications

Characterization of an acidic cold-adapted cutinase from Thielavia terrestris and its application in flavor ester synthesis

Characterization of an acidic cold-adapted cutinase from Thielavia terrestris and its application in flavor ester synthesis

Structural and functional studies of a Fusarium oxysporum cutinase with polyethylene terephthalate modification potential

Study on Improvement of Extracellular Production of Recombinant Thermobifida fusca Cutinase by Escherichia coli

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