01904nas a2200193   4500008004100000245011500041210006900156260000800225300001400233490000700247520120900254100001301463700002601476700001701502700002101519700002101540700001701561856013201578       2017                        eng d00aIdentification of biomolecules involved in the biosynthesis of gold nanoparticles from living peanut seedlings0 aIdentification of biomolecules involved in the biosynthesis of g  cMAR  a1787-17950 v173 aIn present work, we have fabricated gold nanoparticles by treating an aqueous solution of 10(-4) M HAuCl4 with the proteins extracted from roots of in vitro raised peanut seedlings and purified them by FPLC at room temperature. These proteins which tested positive for the reduction of 10(-4) M HAuCl4 were identified as Mannose glucose binding lectin and Ara h 8 allergen isoforms by ESI MS/MS. It is a well known fact that aromatic amino acids possess delocalized pi electrons in their ring structures, rendering them as the best electron donors which can transfer electrons and reduce the acceptor. These results suggest that the aromatic amino acids present in the proteins from the peanut seedlings are the primary biomolecules involved in the reduction of Au (III) to Au (0). We isolated different protein of molecular weight 16.4, 28.3 and 30 kDa involved in the formation of nanoparticles. The protein with molecular weight 16.4 kDa (allergens) yielded NPs of 25-60 nm whereas, the proteins with molecular weight 28.3 kDa and 30 kDa (lectins) yielded highly monodispersed NPs of 5-20 nm in size. The results clearly indicate that the size of nanoparticles can be controlled by different proteins.1 aRaju, D.1 aSiddiqui, Ejaz, Ahmad1 aPrasanth, S.1 aKhan, Bashir, M.1 aMehta, Urmil, J.1 aAhmad, Absar  uhttps://library.ncl.res.in/content/identification-biomolecules-involved-biosynthesis-gold-nanoparticles-living-peanut-seedlings02232nas a2200181   4500008004100000022001500041245010100056210006900157260000800226490000700234520156800241100001801809700002201827700002701849700002701876700002101903856012601924       2018                        eng d  a 0959-399300a Enhanced activity of Withania somnifera family-1 glycosyltransferase (UGT73A16) via mutagenesis0 aEnhanced activity of Withania somnifera family1 glycosyltransfer  cOCT0 v343 aThis work used an approach of enzyme engineering towards the improved production of baicalin as well as alteration of acceptor and donor substrate preferences in UGT73A16. The 3D model of Withania somnifera family-1 glycosyltransferase (UGT73A16) was constructed based on the known crystal structures of plant UGTs. Structural and functional properties of UGT73A16 were investigated using docking and mutagenesis. The docking studies were performed to understand the key residues involved in substrate recognition. In the molecular model of UGT73A16, substrates binding pockets are located between N- and C-terminal domains. Modeled UGT73A16 was docked with UDP-glucose, UDP-glucuronic acid (UDPGA), kaempferol, isorhamnetin, 3-hydroxy flavones, naringenin, genistein and baicalein. The protein-ligand interactions showed that His 16, Asp 246, Lys 255, Ala 337, Gln 339, Val 340, Asn 358 and Glu 362 amino acid residues may be important for catalytic activity. The kinetic parameters indicated that mutants A337C and Q339A exhibited 2-3 fold and 6-7 fold more catalytic efficiency, respectively than wild type, and shifted the sugar donor specificity from UDP-glucose to UDPGA. The mutant Q379H displayed large loss of activity with UDP-glucose and UDPGA strongly suggested that last amino acid residue of PSPG box is important for glucuronosylation and glucosylation and highly specific to sugar binding sites. The information obtained from docking and mutational studies could be beneficial in future to engineer this biocatalyst for development of better ones.1 aSingh, Somesh1 aPatel, Krunal, A.1 aSonawane, Prashant, D.1 aVishwakarma, Rishi, K.1 aKhan, Bashir, M.  uhttps://library.ncl.res.in/content/enhanced-activity-withania-somnifera-family-1-glycosyltransferase-ugt73a16-mutagenesis