2006
DOI: 10.1016/j.ibiod.2006.07.003
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Culture and characteristics of recombinant protein production of an Escherichia coli strain expressing carboxylesterase B1

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Cited by 7 publications
(3 citation statements)
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“…The probable reason for the low lipase activity with respect to high temperature is due to the aggregation of inclusion bodies. High temperature favours the aggregation of inclusion bodies whereas lower temperature enhances the secretion of recombinant protein in soluble form [24]. At lower temperature, reduced growth of E. coli [2] might be the reason for decreased lipase production.…”
Section: Discussionmentioning
confidence: 99%
“…The probable reason for the low lipase activity with respect to high temperature is due to the aggregation of inclusion bodies. High temperature favours the aggregation of inclusion bodies whereas lower temperature enhances the secretion of recombinant protein in soluble form [24]. At lower temperature, reduced growth of E. coli [2] might be the reason for decreased lipase production.…”
Section: Discussionmentioning
confidence: 99%
“…A low molecular weight SDS calibration kit containing proteins (14.4 -97.0 kDa) was used to provide standard molecular weight markers. Proteins were visualized by silver staining (17).…”
Section: Protein Determination and Electrophoresismentioning
confidence: 99%
“…It has been reported that CarEs are involved in the mediation of metabolic resistance to organophosphate insecticides in several insect species. 15,29,31,33 The enhanced activity of CarEs in insects is frequently correlated with resistance to organophosphate pesticides, including chlorpyrifos and malathion. 15,31,32,34 In our study, a significant increase in CarE activity of B. odoriphaga after exposure to LC 30 of malathion, suggest that enhanced activity of CarE might contribute to detoxification of malathion.…”
Section: ■ Discussionmentioning
confidence: 99%