Potential of insect endogenous cellulases for lignocellulosic break down deciphered using molecular docking studies.

Insects possess cellulolytic system capable of producing variegate enzymes with multifarious specificities to break down complex lignocellulosic products. Astonishingly, endoglucanases, exoglucanases and β-glycosidases act sequentially in a synergistic system to facilitate the breakdown of cellulose to utilisable energy source glucose. docking studies of endo-β-1,4-glucanase from 19 different insects belonging to six different orders identified that it possesses high affinity for all the six substrates, including CMC, cellulose, cellotriose, cellotetraose, cellopentose and cellohexaose.

Fucose-binding lectins: purification, characterization and potential biomedical applications.

The property of lectins to specifically recognize and bind carbohydrates makes them an excellent candidate in biomedical research. Among them are fucose-binding lectins possessing the capacity to bind fucose are taxonomically, evolutionarily and ecologically significant class of lectins that are identified in a wide range of taxa. Purification of fucose-binding lectins dates back to 1967 when L-fucose binding protein from Lotus tetragonolobus was isolated using a dye that contained three α-L-fucopyranosyl residues.

Evaluation of haemolymph phenoloxidase activity from the grub of Zophobas morio as a predictor of immune response.

In insects, enzyme phenoloxidase plays a critical role in cuticular sclerotisation and defensive functions. In the present investigation, haemolymph phenoloxidase activity from the grub of Zophobas morio was attempted to evaluate as a reliable predictor of insect's immunological response. Among the various substrates tested, L-DOPA was chosen as an appropriate substrate due to its high oxidation.

Predominant contribution of an endogenous cellulase (OlCel) to the cellulolysis in the digestive system of larvae of banana pseudostem weevil, Odoiporus longicollis (Coleoptera: Curculionidae).

Insects have evolved with effective strategies to utilize cellulose as an energy source by possessing cellulolytic enzymes which can be used as an optimal resource in the bioenergy sector. The study was aimed at evaluating the cellulolytic enzyme in the larval gut of the banana pseudostem weevil, Odoiporus longicollis Olivier (Coleoptera: Curculionidae). Primarily, cellulase activity was localized along the gut, in which the midgut showed the highest activity (2858 U/mg).

Purification, characterization and larvicidal activity of a potent bioactive compound asarone from leaves of Acorus calamus against the culician larval mosquitoes.

Mosquitoes are potent vectors by serving as agents to life-threatening diseases in humans. Increasing resistance in mosquitoes against existing insecticides and repellents brings new challenges and an opportunity to explore sustainable compounds. We chose six medicinal plants to screen potential bioactive compounds that could act as an insecticide.

Cloning, expression and characterization of arcelin and its impact on digestive enzymes of the stored product insect pest, Callosobruchus maculatus (F.).

The pulse beetle Callosobruchus maculatus causes potential damage to legume crops by infesting the seeds, leading to a reduction of total protein content. Arcelin found in the wild accessions of the common bean, is an insecticidal protein that has the potency to hamper the metabolism of the bruchid beetle. The arcelin gene from the wild accession of Phaseolus lunatus was isolated and the ORF encoding 158 amino acids was cloned in pET-45b (+) vector.

In silico analysis of carbohydrate-binding pockets in the lectin genes from various species of Canavalia.

Legumes are endowed with an opulent class of proteins called lectins that can detect tenuous variations in carbohydrate structures and bind them reversibly with high affinity and specificity. The genus Canavalia, in the family of Leguminosae, is considered to be an affluent source of lectin. An effort has been made to analyse the sequences encoded by the lectin gene and its carbohydrate binding pockets from three species of Canavalia, including C.