000168158 001__ 168158
000168158 005__ 20260127160850.0
000168158 0247_ $$2doi$$a10.1021/bm500333v
000168158 0248_ $$2sideral$$a147686
000168158 037__ $$aART-2014-147686
000168158 041__ $$aeng
000168158 100__ $$0(orcid)0000-0001-9478-6750$$aVelasco-Lozano, Susana
000168158 245__ $$aCarrier-Free Immobilization of Lipase from <i>Candida rugosa</i> with Polyethyleneimines by Carboxyl-Activated Cross-Linking
000168158 260__ $$c2014
000168158 5060_ $$aAccess copy available to the general public$$fUnrestricted
000168158 5203_ $$aCarrier-free immobilization of Candida rugosa lipase (CRL) and polymers containing primary amino groups were cross-linked using carbodiimide. To accomplish this, the free carboxyl groups of the enzyme were activated with carbodiimide-succinimide in organic medium, and then the activated proteins were cross-linked with different polyethyleneimines (PEIs). The effect of the cross-linker chain length, the amount of added bovine serum albumin (BSA), and carbodiimide concentration on the catalytic properties of resulting cross-linked enzyme aggregates (CLEAs) was investigated. The CLEAs’ size, shape, specific activity, activity recovery, thermostability and enantioselectivity significantly varied according to the preparation procedure. The highest thermostable CRL-CLEA preparation was obtained with 1.3 kDa polyethyleneimine as cross-linker, 10 mg of BSA and 28 mM of carbodiimide. This preparation is 1.3-fold more active and thermostable than CLEAs prepared by the traditional method of amino cross-linking with glutaraldehyde, and retains 60% of residual activity after 22 h at 50°C. Additionally, the CRL-CLEA preparation showed an enantioselectivity of 91% enantiomeric excess (ee). This immobilization procedure provides an alternative strategy for CLEA production, particularly for enzymes where the traditional method of cross-linking via lysine residues leads to enzyme inactivation.
000168158 540__ $$9info:eu-repo/semantics/openAccess$$aAll rights reserved$$uhttp://www.europeana.eu/rights/rr-f/
000168158 590__ $$a5.75$$b2014
000168158 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b39 / 290 = 0.134$$c2014$$dQ1$$eT1
000168158 591__ $$aPOLYMER SCIENCE$$b5 / 82 = 0.061$$c2014$$dQ1$$eT1
000168158 591__ $$aCHEMISTRY, ORGANIC$$b5 / 58 = 0.086$$c2014$$dQ1$$eT1
000168158 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/acceptedVersion
000168158 700__ $$aLópez-Gallego, Fernando
000168158 700__ $$aVázquez-Duhalt, Rafael
000168158 700__ $$aMateos-Díaz, Juan C.
000168158 700__ $$aGuisán, José M.
000168158 700__ $$aFavela-Torres, Ernesto
000168158 773__ $$g15, 5 (2014), 1896-1903$$pBiomacromolecules$$tBIOMACROMOLECULES$$x1525-7797
000168158 8564_ $$s693387$$uhttps://zaguan.unizar.es/record/168158/files/texto_completo.pdf$$yPostprint
000168158 8564_ $$s1174917$$uhttps://zaguan.unizar.es/record/168158/files/texto_completo.jpg?subformat=icon$$xicon$$yPostprint
000168158 909CO $$ooai:zaguan.unizar.es:168158$$particulos$$pdriver
000168158 951__ $$a2026-01-27-15:01:33
000168158 980__ $$aARTICLE