01521nas a2200217   4500008004100000022001400041245008500055210006900140260011700209300001000326490000600336520066800342653004301010653001901053653002501072653003501097100001601132700001801148700002101166856011601187       2008                        eng d  a0973-626300aImmobilization of penicillin G acylase on amino functionalized mesoporous silica0 aImmobilization of penicillin G acylase on amino functionalized m  aSECTOR A-80, SCHEME NO 54, VIJAY NAGAR, A B ROAD, INDORE, 452 010 MP, INDIAbRESEARCH JOURNAL BIOTECHNOLOGYcNOV  a18-210 v33 a<p>Penicillin G acylase was immobilized on Amino functionalized mesoporous silica by adsorption method. In this paper we present the effect of penicillin G acylase immobilization on amino-functionalized mesoporous silica and the effect of silica as host matrix on enzyme kinetics. The loading capacity of immobilized Penicillin G acylase is 34 mg protein per 0.5 g of SBA-15. About 65% of the protein was adsorbed on mesoporous silica. The stability of penicillin acylase was enhanced after immobilization on mesoporous silica. The adsorbed enzyme is more stable than the soluble form, both to temperature and pH environments and retained 73% of its activity.</p>10aAmino functionalized mesoporous silica10aImmobilization10aPenicillin G acylase10apH and temperature stabilities1 aSridevi, N.1 aPallavi, Shah1 aAsmita, Prabhune  uhttps://library.ncl.res.in/content/immobilization-penicillin-g-acylase-amino-functionalized-mesoporous-silica-002419nas a2200229   4500008004100000022001400041245008800055210006900143260007300212300001200285490000800297520159300305653002501898653002701923653003401950653001101984100001801995700001602013700002102029700002002050856011902070       2008                        eng d  a1387-181100aStructural features of Penicillin acylase adsorption on APTES functionalized SBA-150 aStructural features of Penicillin acylase adsorption on APTES fu  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcDEC  a157-1650 v1163 a<p>The immobilization of Penicillin acylase (PGA) enzyme (which belongs to the Ntn hydrolase super family) into the amino-functionalized SBA-15 mesoporous molecular sieve is carried out to see the effect of silica as a host matrix on the enzyme kinetics. Physicochemical characterization by nitrogen adsorption, powder XRD and TEM methods indicate that the characteristic hexagonal features and the original pore structure of the parent SBA-15 is retained even after the incorporation of PGA. The adsorption of PGA on SBA15 shows a dependence on the pore volume and the composition of the adsorbent. The maximum loading of the enzyme was observed at pH 7.8, slightly below the isoelectric point of the enzyme. The loading capacity of immobilized PGA is 34 mg protein per 0.5 g of SBA-15. The trapped enzyme is more stable than the soluble form to temperature and pH environments and retained 73% of its activity after immobilization. This enhanced stability is attributed to the protective nature of the cage itself and to the rigidity of the SiO(2) matrix, which reduces the freedom of peptide-chain refolding of molecular motions that occur in denaturation processes. The strength of binding is very strong; however, the activity of the immobilized enzyme is then simply restored with very little leakage of enzyme from the support. An important feature of the immobilized PGA enzyme is the excellent reusability without significant loss in activity, which indicates potentially exciting industrial/biomedical application of this support. (C) 2008 Elsevier Inc. All rights reserved.</p>10aPenicillin G acylase10aPGA immobilized SBA-1510apH and temperatures stability10aSBA-151 aShah, Pallavi1 aSridevi, N.1 aPrabhune, Asmita1 aRamaswamy, Veda  uhttps://library.ncl.res.in/content/structural-features-penicillin-acylase-adsorption-aptes-functionalized-sba-15-0