000095557 001__ 95557
000095557 005__ 20210902121735.0
000095557 0247_ $$2doi$$a10.3390/catal10060669
000095557 0248_ $$2sideral$$a119685
000095557 037__ $$aART-2020-119685
000095557 041__ $$aeng
000095557 100__ $$aCorrea, S.
000095557 245__ $$aStabilization of b-Glucuronidase by Immobilization in Magnetic-Silica Hybrid Supports
000095557 260__ $$c2020
000095557 5060_ $$aAccess copy available to the general public$$fUnrestricted
000095557 5203_ $$abeta-Glucuronidases are a class of enzymes that catalyze the breakdown of complex carbohydrates. They have well documented biocatalytic applications in synthesis, therapeutics, and analytics that could benefit from enzyme immobilization and stabilization. In this work, we have explored a number of immobilization strategies for Patella vulgata beta-Glucuronidase that comprised a tailored combination of biomimetic silica (Si) and magnetic nanoparticles (MNPs). The individual effect of each material on the enzyme upon immobilization was first tested. Three different immobilization strategies for covalent attachment on MNPs and different three catalysts for the deposition of Si particles were tested. We produced nine different immobilized preparations and only two of them presented negligible activity. All the preparations were in the micro-sized range (from 1299 +/- 52 nm to 2101 +/- 67 nm of hydrodynamic diameter). Their values for polydispersity index varied around 0.3, indicating homogeneous populations of particles with low probability of agglomeration. Storage, thermal, and operational stability were superior for the enzyme immobilized in the composite material. At 80 degrees C different preparations with Si and MNPs retained 40% of their initial activity after 6 h of incubation whereas the soluble enzyme lost 90% of its initial activity within 11 min. Integration of MNPs provided the advantage of reusing the biocatalyst via magnetic separation up to six times with residual activity. The hybrid material produced herein demonstrated its versatility and robustness as a support for beta-Glucuronidases immobilization.
000095557 536__ $$9info:eu-repo/grantAgreement/ES/DGA/E15-20R$$9info:eu-repo/grantAgreement/EC/H2020/829162/EU/Redesigning biocatalysis: Thermal-tuning of one-pot multienzymatic cascades by nanoactuation/HOTZYMES$$9This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No H2020 829162-HOTZYMES$$9info:eu-repo/grantAgreement/ES/MINECO/BIO2017-84246-C2-1-R
000095557 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000095557 590__ $$a4.146$$b2020
000095557 591__ $$aCHEMISTRY, PHYSICAL$$b67 / 162 = 0.414$$c2020$$dQ2$$eT2
000095557 592__ $$a0.8$$b2020
000095557 593__ $$aPhysical and Theoretical Chemistry$$c2020$$dQ2
000095557 593__ $$aCatalysis$$c2020$$dQ2
000095557 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000095557 700__ $$aRipoll, M.
000095557 700__ $$aJackson, E.
000095557 700__ $$0(orcid)0000-0001-6170-4237$$aGrazu, V.$$uUniversidad de Zaragoza
000095557 700__ $$aBetancor, L.
000095557 7102_ $$12013$$2765$$aUniversidad de Zaragoza$$bDpto. Química Orgánica$$cÁrea Química Orgánica
000095557 773__ $$g10, 6 (2020), 669 [15 pp]$$pCatalysts$$tCATALYSTS$$x2073-4344
000095557 8564_ $$s700333$$uhttps://zaguan.unizar.es/record/95557/files/texto_completo.pdf$$yVersión publicada
000095557 8564_ $$s480328$$uhttps://zaguan.unizar.es/record/95557/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000095557 909CO $$ooai:zaguan.unizar.es:95557$$particulos$$pdriver
000095557 951__ $$a2021-09-02-09:38:47
000095557 980__ $$aARTICLE