@article { ISI:000261133600023,
	title = {Structural features of Penicillin acylase adsorption on APTES functionalized SBA-15},
	journal = {Microporous and Mesoporous Materials},
	volume = {116},
	number = {1-3},
	year = {2008},
	month = {DEC},
	pages = {157-165},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<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>},
	keywords = {Penicillin G acylase, PGA immobilized SBA-15, pH and temperatures stability, SBA-15},
	issn = {1387-1811},
	doi = {10.1016/j.micromeso.2008.03.030},
	author = {Shah, Pallavi and Sridevi, N. and Prabhune, Asmita and Ramaswamy, Veda}
}
@article { ISI:000330603800033,
	title = {Immobilization of bile salt hydrolase enzyme on mesoporous SBA-15 for co-precipitation of cholesterol},
	journal = {International Journal of Biological Macromolecules},
	volume = {63},
	year = {2014},
	month = {FEB},
	pages = {218-224},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>We describe herein a simple and effective strategy for immobilization of bile salt hydrolase enzyme by grafting glutaraldehyde groups inside channels of APTES functionalized SBA-15. The increase in glutaraldehyde concentration prevents leakage of enzyme but showed a steep decrease in enzyme activity in the immobilized matrix. So the degree of cross-linking should be the minimum possible to ensure sufficient stability without loss of activity. Cross-linking carried out with 0.1\% glutaraldehyde concentration showed the highest activity, so this was used in all further experiments. Physico-chemical characterizations of the immobilized enzyme were carried out by XRD, N-2 adsorption, TEM, FUR and Si-29 CP-MAS NMR techniques. Immobilized BSH exhibits enhanced stability over a wide pH (3-11) and temperature range (40-80 degrees C) and retains an activity even after recycling experiments and six months of storage. From our in vivo research experiment toward co-precipitation of cholesterol, we have shown that immobilized BSH enzyme may be the promising catalyst for the reduction of serum cholesterol levels in our preliminary investigation. Enhancement in pH stability at the extreme side of pH may favor the use of immobilized BSH enzyme for drug delivery purpose to with stand extreme pH conditions in the gastrointestinal conditions. (C) 2013 Elsevier B.V. All rights reserved.</p>},
	keywords = {Bile salt hydrolase, Co-precipitation of cholesterol, SBA-15},
	issn = {0141-8130},
	doi = {10.1016/j.ijbiomac.2013.11.008},
	author = {Bhange, Pallavi and Sridevi, N. and Bhange, Deu S. and Prabhune, Asmita and Ramaswamy, Veda}
}
