@article { ISI:000327915300016,
	title = {Calcium oxide supported gold nanoparticles as catalysts for the selective epoxidation of styrene by t-butyl hydroperoxide},
	journal = {Journal of Colloid and Interface Science},
	volume = {415},
	year = {2014},
	month = {FEB},
	pages = {111-116},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	type = {Article},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>Gold nanoparticles are deposited on basic CaO supports as catalysts for the selective conversion of styrene into styrene oxide. Synthetic methods, gold loading and calcination temperatures are varied to permit an understanding of their influence on gold nanoparticle size, the presence of cationic gold species and the nature of interaction between the gold nanoparticles and the CaO support. Based on these studies, optimal conditions are designed to make the Au/CaO catalyst efficient for the selective epoxidation of styrene. (C) 2013 Elsevier Inc. All rights reserved.</p>},
	keywords = {Au/CaO, Epoxidation of styrene, gold nanoparticles, Homogenous deposition precipitation method, Styrene oxide},
	issn = {0021-9797},
	doi = {10.1016/j.jcis.2013.10.016},
	author = {Dumbre, Deepa K. and Choudhary, Vasant R. and Patil, Nilesh S. and Uphade, Balu S. and Bhargava, Suresh Kumar}
}
@article { ISI:000359596600058,
	title = {Charge-switchable gold nanoparticles for enhanced enzymatic thermostability},
	journal = {Physical Chemistry Chemical Physics},
	volume = {17},
	number = {33},
	year = {2015},
	month = {JUL},
	pages = {21517-21524},
	publisher = {ROYAL SOC CHEMISTRY},
	address = {THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND},
	abstract = {<p>This study illustrates a facile strategy for efficient immobilization of enzymes on a metal nanoparticle surface. The strategy proposed here enables the enzymatic activity to be retained while increasing the enzyme thermostability. It is demonstrated that the use of a zwitterionic amino acid tyrosine as a reducing and capping agent to synthesise gold nanoparticles allows efficient immobilization of phytase enzyme through charge-switchable electrostatic interactions. The detailed kinetic and thermodynamic studies reveal that the proposed enzyme immobilization strategy improves the overall quality of phytase by reducing the activation energy required for substrate hydrolysis and broadening the temperature window in which immobilized enzyme is able to operate. The outcomes of this study indicate that the underlying zwitterionic nature of 20 natural amino acids along with significant variability in their isoelectric points and hydropathy indices as well the ability of some of the amino acids to reduce metal ions is likely to offer significant opportunities for tailoring nano-bio interfaces in a rational manner for a range of biological applications.</p>},
	issn = {1463-9076},
	doi = {10.1039/c5cp03021h},
	author = {Shankar, Shiv and Soni, Sarvesh K. and Daima, Hemant K. and Selvakannan, P. R. and Khire, Jayant Malhar and Bhargava, Suresh Kumar and Bansal, Vipul}
}
