Refolding of a recombinant organic solvent-stable lipase, which is overexpressed and forms an inclusion body, and activation with lipase-specific foldase

Ogino, Hiroyasu; Inoue, Sosuke; Akagi, Rieko; Yasuda, Masahiro; Doukyu, Noriyuki; Ishimi, Kosaku

doi:10.1016/j.bej.2008.01.022

Cited by 8 publications

(2 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Numerous studies have examined the molecular interaction between lipases and their Lifs. These studies focused mainly on the function of Lifs and indicated that they assist with the correct folding of their cognate lipases both in vitro and in vivo [8][9][10][11]. Although the three-dimensional (3D) structure of the Lif-LipA complex from B. glumae has been solved [12], few studies have examined the reaction mechanism of Lifs.…”

Section: Introductionmentioning

confidence: 99%

Probing the molecular determinant of the lipase-specific foldase Lif26 for the interaction with its cognate Lip26

Zheng

Tian

et al. 2013

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 99%

Probing the molecular determinant of the lipase-specific foldase Lif26 for the interaction with its cognate Lip26

Zheng

Tian

et al. 2013

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

“…Escherichia coli can accumulate recombinant proteins up to 80% of its dry weight and survives in a variety of environmental conditions (Demain and Vaishnav 2009). Escherichia coli has been used widely as host for lipase gene expression (Nthangeni et al 2001;Oginoa et al 2008;Gao et al 2009). However, development of lipase production by recombinant E. coli is focused more toward cloning, expression and characterization of the enzymes.…”

Section: Introductionmentioning

confidence: 99%

Sequential optimization of production of a thermostable and organic solvent tolerant lipase by recombinant Escherichia coli

et al. 2010

View full text Add to dashboard Cite

Several medium formulations were screened for the production of a thermostable and organic solvent tolerant lipase by a recombinant Escherichia coli BL21. The highest lipase production (28.9±4.1 IU/mL) was obtained in Luria Bertani medium with the addition of 1% (w/v) glucose. The medium formulation and fermentation conditions were then subjected to sequential optimization. Using a Plackett-Burman design, glucose, NaCl, temperature and induction time were found to be the most significant variables affecting lipase production, and these were then optimized using response surface methodology (RSM). The large value of R 2 (0.979) showed that the quadratic model used for the prediction is highly significant. The optimum levels of these four significant variables (glucose, NaCl, temperature and induction time) as predicted by RSM were 32.4 g/L, 5 g/L, 31.7°C and 2.1 h, respectively. The amount of lipase activity (50.2±4.5 IU/ mL) produced under these optimal conditions fitted well to the value (48.9 IU/mL) predicted by RSM. Production of lipase in optimized fermentation was about 2.5-fold higher than in non-optimized fermentation.

show abstract

Primary recovery of lipase derived from Burkholderia cenocepacia strain ST8 and recycling of phase components in an aqueous two-phase system

Show

Tan

Anuar

et al. 2012

Biochemical Engineering Journal

View full text Add to dashboard Cite

Refolding of a recombinant organic solvent-stable lipase, which is overexpressed and forms an inclusion body, and activation with lipase-specific foldase

Cited by 8 publications

References 28 publications

Probing the molecular determinant of the lipase-specific foldase Lif26 for the interaction with its cognate Lip26

Probing the molecular determinant of the lipase-specific foldase Lif26 for the interaction with its cognate Lip26

Sequential optimization of production of a thermostable and organic solvent tolerant lipase by recombinant Escherichia coli

Primary recovery of lipase derived from Burkholderia cenocepacia strain ST8 and recycling of phase components in an aqueous two-phase system

Contact Info

Product

Resources

About