01734nas a2200241   4500008004100000020002200041022001400063245006700077210006600144260009900210300001400309490000800323520094300331100001801274700001601292700002101308700002001329700001001349700001201359700001201371700001101383856009801394       2007                        eng d  a978-0-444-53068-4  a0167-299100aImmobilization of Ntn hydrolases on APTES fuctionalized SBA-150 aImmobilization of Ntn hydrolases on APTES fuctionalized SBA15  aSara Burgerhartstraat 25, Po Box 211, 1000 AE Amsterdam, NetherlandsbElsevier Science BVcAUG  a1891-18980 v1703 a<p>APTES Functionalized mesoporous silica SBA-15 molecular sieves have been prepared and used for immobilization of Penicillin G acylase. Physico chemical characterization was done by nitrogen adsorption, powder XRD and TEM methods to understand the nature of immobilized PGA enzyme. XRD data indicate a good mesoscopic order. The characteristic hexagonal features of SBA-15 were maintained in PGA immobilized SBA-15 samples. Incorporation of PGA does not affect the original pore structure of the parent SBA-15. The adsorption of PGA on SBA-15 from buffered solutions with a pH value, 7.8 has been studied as a model protein adsorption system. The maximum activity of the immobilized 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 stability of Penicillin G acylase was enhanced by the physical entrapment in SBA-15.</p>1 aShah, Pallavi1 aSridevi, N.1 aPrabhune, Asmita1 aRamaswamy, Veda1 aXu, R1 aGao, Z.1 aChen, J1 aYan, W  uhttps://library.ncl.res.in/content/immobilization-ntn-hydrolases-aptes-fuctionalized-sba-15-0