@article { ISI:000252406100012, title = {CdS quantum dots: enzyme mediated in vitro synthesis, characterization and conjugation with plant lectins}, journal = {Journal of Biomedical Nanotechnology}, volume = {3}, number = {4}, year = {2007}, month = {DEC}, pages = {406-413}, publisher = {AMER SCIENTIFIC PUBLISHERS}, type = {Article}, address = {25650 NORTH LEWIS WAY, STEVENSON RANCH, CA 91381-1439 USA}, abstract = {

This paper presents the in vitro synthesis of CdS quantum dot nanoparticles using sulphite reductase and capping peptide in the presence of a co-factor alpha-NADPH, their characterization and conjugation with plant lectins, Jacalin and Chick pea lectin. Incubation of sulphite reductase with aqueous CdCl2, Na2SO3, and capping peptide in the presence of a-NADPH, which acts as a co-factor, resulted in the formation of CdS nanoparticles of dimensions 5-20 nm. These CdS nanoparticles were conjugated with plant lectins by EDAC mediated coupling. These observations are of significance, as it will help in the development of eco-friendly process for the formation of CdS nanoparticles and their application as fluorescent biolabels. Moreover the above studies will also help in designing a rational enzymatic strategy for the synthesis of nanomaterials of different chemical composition, shapes and sizes as well as their separation.

}, keywords = {bio-label, CdS quantum dots, conjugation, Enzyme, in vitro synthesis, Nanoparticles}, issn = {1550-7033}, doi = {10.1166/jbn.2007.045}, author = {Ansary, Abu Ayoobul and Kumar, S. Anil and Krishnasastry, M. V. and Abyaneh, Majid Kazemian and Kulkarni, Sulabha K. and Ahmad, Absar and Khan, Mohammad Islam} } @article { ISI:000303281200026, title = {In vitro enzyme mediated synthesis of metal sulfide nanoparticles: control of particle size of CdS, Ni7S6, PbS, Co3S4 nanoparticles using synthetic peptides}, journal = {Science of Advanced Materials}, volume = {4}, number = {1}, year = {2012}, month = {JAN}, pages = {179-186}, publisher = {AMER SCIENTIFIC PUBLISHERS}, type = {Article}, address = {26650 THE OLD RD, STE 208, VALENCIA, CA 91381-0751 USA}, abstract = {

We report the use of enzyme sulfite reductase for the in vitro synthesis of technologically important metal sulfide quantum dots viz. Co3S4, PbS and Ni7S6. Also we report the use of synthetic peptides to control the particle size of the above metal sulfide quantum dots in addition to CdS, synthesized using enzyme. Sulfite reductase when incubated with aqueous CdCl2, or Co(NO3)(3) or NiCl2 or Pb(NO3)(2), and Na2SO3 in the presence of the appropriate capping peptide resulted in the synthesis of particle size controlled CdS, Co3S4, Ni7S6, or PbS quantum dots respectively. These, enzyme mediated synthesized and size controlled metal sulfide quantum dots, were characterized using Absorbance and photoluminescence spectrometry, X-ray diffraction, X-ray photoelectron spectroscopy and High resolution-transmission electron microscopy.

}, keywords = {Capping Peptide, Enzyme, Metal Sulfide Nanoparticles, quantum dots, Size Control, Sulfite Reductase}, issn = {1947-2935}, doi = {10.1166/sam.2012.1270}, author = {Ansary, Abu Ayoobul and Khan, Muhammed I. and Gaikwad, Sushama M.} } @article { ISI:000316636600004, title = {Biodegradation of phenol by the yeast candida tropicalis: an investigation by NMR spectroscopy}, journal = {Applied Biochemistry and Biotechnology}, volume = {169}, number = {7}, year = {2013}, month = {APR}, pages = {2029-2037}, publisher = {HUMANA PRESS INC}, address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA}, abstract = {

The process of phenol biodegradation by the yeast Candida tropicalis NCIM 3556 in aqueous medium was studied by H-1, C-13, and DOSY NMR techniques. Samples at regular intervals were centrifuged to separate the cells, and H-1 spectral data were collected at 400 MHz. Though a gradual decrease in the concentration of phenol was observed, after an incubation period of similar to 8 h, formation of any intermediate products could not be detected. Experiments carried out with uniformly C-13-labeled phenol also failed to detect formation of any carboxylic acid intermediates during degradation. The studies indicated that the phenol was completely degraded to carbon dioxide and water in approximately 20 h. Self-diffusion coefficient measurements showed that the lifetime of phenol in the bound form is too small to impart any change in its diffusion behavior and the intermediates formed are converted to carbon dioxide and water at a very fast rate.

}, keywords = {biocatalysis, Carboxylic acid, Diffusion, Enzyme, NMR spectroscopy, phenol}, issn = {0273-2289}, doi = {10.1007/s12010-013-0119-0}, author = {Phalgune, U. D. and Rajamohanan, P. R. and Gaikwad, B. G. and Varma, R. J. and George, S.} } @article { ISI:000336464400074, title = {Protein mediated synthesis of Au-Ag bimetallic nanoparticles}, journal = {Materials Letters}, volume = {124}, year = {2014}, month = {JUN}, pages = {271-274}, publisher = {ELSEVIER SCIENCE BV}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, abstract = {

There is growing need to develop environment friendly method for synthesis of bimetallic nanoparticle that do not use toxic chemicals during their synthesis process. Here, we report synthesis of Au-Ag bimetallic nanoparticles by using macerase enzyme as reducing agent at different temperatures. Bimetallic nanoparticles were synthesized at 80 and 90 degrees C. The intensity of formation of nanoparticles was more at 80 degrees C. The bimetallic nanoparticles are characterized by using UV-vis, TEM and EDAX. The TEM study shows the inner gold and outer silver bimetallic nanoparticles. The formed nanoparticles are 4-20 nm in size and spherical in shape. EDAX confirms the formed bimetallic nanoparticles are of gold and silver. (C) 2014 Elsevier B.V. All rights reserved.

}, keywords = {Enzyme, Gold, Macerase, Particles, Silver, synthesis}, issn = {0167-577X}, doi = {10.1016/j.matlet.2014.03.087}, author = {Raju, D. and Mendapara, Ritul and Mehta, Urmil J.} } @article {47499, title = {Diversity in chemical structures and biological properties of plant alkaloids}, journal = {Molecules}, volume = {26}, year = {2021}, month = {JUN}, pages = {3374}, type = {Review}, abstract = {Phytochemicals belonging to the group of alkaloids are signature specialized metabolites endowed with countless biological activities. Plants are armored with these naturally produced nitrogenous compounds to combat numerous challenging environmental stress conditions. Traditional and modern healthcare systems have harnessed the potential of these organic compounds for the treatment of many ailments. Various chemical entities (functional groups) attached to the central moiety are responsible for their diverse range of biological properties. The development of the characterization of these plant metabolites and the enzymes involved in their biosynthesis is of an utmost priority to deliver enhanced advantages in terms of biological properties and productivity. Further, the incorporation of whole/partial metabolic pathways in the heterologous system and/or the overexpression of biosynthetic steps in homologous systems have both become alternative and lucrative methods over chemical synthesis in recent times. Moreover, in-depth research on alkaloid biosynthetic pathways has revealed numerous chemical modifications that occur during alkaloidal conversions. These chemical reactions involve glycosylation, acylation, reduction, oxidation, and methylation steps, and they are usually responsible for conferring the biological activities possessed by alkaloids. In this review, we aim to discuss the alkaloidal group of plant specialized metabolites and their brief classification covering major categories. We also emphasize the diversity in the basic structures of plant alkaloids arising through enzymatically catalyzed structural modifications in certain plant species, as well as their emerging diverse biological activities. The role of alkaloids in plant defense and their mechanisms of action are also briefly discussed. Moreover, the commercial utilization of plant alkaloids in the marketplace displaying various applications has been enumerated.}, keywords = {alkaloid, Biological activity, classification, defense, Enzyme, modification}, doi = {10.3390/molecules26113374}, author = {Bhambhani, Sweta and Kondhare, Kirtikumar R. and Giri, Ashok P.} }