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090			_aB-11132
245	1	0	_aFunctional fusion mutant of Candida antarctica lipase B (CalB)expressed in Escherichia coli
490	0		_vBiochimica et Biophysica Acta, 1794(3), p.519-525, 2009
520	3		_aCandida antarctica lipase B (CalB)was functionally expressed in the cytoplasm of Escherichia coli Origami (DE3)with the N-terminus fusion of E. coli endogenous proteins. The previously-identified stress responsive proteins through comparative proteome analyses such as malate dehydrogenase (Mdh), spermidine/ putrescine-binding periplasmic protein (PotD), and FKBP-type peptidyl-prolyl cis-trans isomerase (PPIases)(SlyD)dramatically increased the solubility of CalB in E. coli cytoplasm when used as N-terminus fusion partners. We demonstrated that Mdh, PotD, and SlyD were powerful solubility enhancers that presumably facilitated the protein folding of CalB. Moreover, among the various fusion mutants, Mdh-CalB showed the highest hydrolytic activity and was as biologically active as standard CalB. Similarly to the previous report, the electrophoretic properties of CalB indicate that CalB seems to form dimer-based oligomer structures. We evaluated the structural compatibility between the fusion partner protein and CalB, which seems to be of crucial importance upon the bioactive dimer formation of CalB and might affect the substrate accessibility to the enzyme active site, thereby determining the biological activities of the fusion mutants.
650	1	4	_aCALB
650	1	4	_aFUNCTIONAL EXPRESSION
650	1	4	_aFUSION MUTANT
650	1	4	_aBIOACTIVITY
650	1	4	_aESCHERICHIA COLI
700	1	2	_aSeo, H.S.
700	1	2	_aKim, S.E.
700	1	2	_aHan, K.Y.
700	1	2	_aPark, J.
700	1	2	_aKim, Y.
700	1	2	_aSim, S.J.
700	1	2	_aLee, J.
856	4	0	_uhttps://drive.google.com/file/d/1C4KY4_F6g_ApDOMjhe0InTgfS4W17HBx/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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