National Chemical Laboratory

About: National Chemical Laboratory is a facility organization based out in Pune, Maharashtra, India. It is known for research contribution in the topics: Catalysis & Enantioselective synthesis. The organization has 8891 authors who have published 14837 publications receiving 387600 citations.

Temperature dependent Raman spectroscopy of chemically derived few layer MoS2 and WS2 nanosheets

Abstract: We have systematically investigated the temperature dependent Raman spectroscopy behavior of a few layered MoS2 and WS2 nanosheets synthesized using simple hydrothermal method. Our result reveals A1g and E12g modes soften as temperature increases from 77 K to 623 K. This behavior can be explained in terms of a double resonance process which is active in single- and few layer thick nanosheets. The frequency shifts and peak broadening can provide unambiguous, nondestructive, and accurate information of a few layered MoS2 and WS2. This mechanism can also be applicable in characterizing the structural, optical, electronic, and vibrational properties of other emerging layered materials.

Insect trehalase: physiological significance and potential applications.

Abstract: Trehalose, a non-reducing disaccharide, is widespread throughout the biological world. It is the major blood sugar in insects playing a crucial role as an instant source of energy and in dealing with abiotic stresses. The hydrolysis of trehalose is under the enzymatic control of trehalase. The enzyme trehalase is gaining interest in insect physiology as it regulates energy metabolism and glucose generation via trehalose catabolism. The two forms of insect trehalase namely, Tre-1 and Tre-2, are important in energy supply, growth, metamorphosis, stress recovery, chitin synthesis and insect flight. Insect trehalase has not been reviewed in depth and the information available is quite scattered. The present mini review discusses our recent understanding of the regulation, mechanism and biochemical characterization of insect trehalase with respect to its physiological role in vital life functions. We also highlight the molecular and biochemical properties of insect trehalase that makes it amenable to competitive inhibition by most glycosidase inhibitors. Due to its crucial role in carbon metabolism in insects, application of inhibitors against trehalose can form a promising area towards formulating strategies for insect pest control.

Structural and functional diversities in lepidopteran serine proteases

Abstract: Primary protein-digestion in Lepidopteran larvae relies on serine proteases like trypsin and chymotrypsin. Efforts toward the classification and characterization of digestive proteases have unraveled a considerable diversity in the specificity and mechanistic classes of gut proteases. Though the evolutionary significance of mutations that lead to structural diversity in serine proteases has been well characterized, detailing the resultant functional diversity has continually posed a challenge to researchers. Functional diversity can be correlated to the adaptation of insects to various host-plants as well as to exposure of insects to naturally occurring antagonistic biomolecules such as plant-derived protease inhibitors (PIs) and lectins. Current research is focused on deciphering the changes in protease specificities and activities arising from altered amino acids at the active site, specificity-determining pockets and other regions, which influence activity. Some insight has been gained through in silico modeling and simulation experiments, aided by the limited availability of characterized proteases. We examine the structurally and functionally diverse Lepidopteran serine proteases, and assess their influence on larval digestive processes and on overall insect physiology.