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https://www.selleckchem.com/products/Y-27632.html In this comparative study, Cellulose Dialdehyde (CDA) immobilized enzyme depicts high reusability, good enzyme loading, storage capacity up to 49 days, optimum pH 6, optimum temperature 95 °C, good pH and thermal stability as compared to native enzyme having optimum pH and temperature of 7 and 37 °C. On the contrary, nanocellulose - Cetyl Trimethyl Ammonium Bromide (NC-CTAB) matrix shows good enzyme loading and optimum pH shift of about 3 units but poor recyclability. Outcome of this study presents the promising nature of covalent mode of immobilization for industrial use.Lentinan, a β-1,3-D-glucan, is clinically used as an immune enhancement drug for tumor therapy. Dectin-1 is a cell-surface immune receptor, which plays an important role in immunological defense against fungal pathogens and β-glucan-mediated immune modulation. Herein we attempted to study the advanced structure of lentinan and how lentinan interacts with dectin-1 for its immune enhancement effect. We firstly used MD simulation and rigid macromolecule docking, combining some spectral techniques, to uncover the complex 3D conformation of a typical polysaccharide - lentinan, and the detailed interaction mode of lentinan with dectin-1. We proved by computational simulation that lentinan can maintain its triple-helix through hydrogen network and disclosed some structural properties of lentinan. We also characterized the affinity of lentinan to dectin-1 by LSPR and binding free energy calculation, and we found out that hydrogen bonds and CH-π interaction are the major contributors for lentinan's binding to dectin-1. Besides, after bound with lentinan, dectin-1 might surprisingly go through a conformational change. In summary, our work provided insights into lentinan's advanced structure and β-glucan recognition by dectin-1.In this study, a comparative efficacy of Cananga odorata EO (CoEO) and its nanoencapsulated formulation into chitosan nanoemulsion (Co

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