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Title: Efficient enzymatic hydrolysis of ionic liquid pretreated chitin and its dissolution mechanism. Author: Li J, Huang WC, Gao L, Sun J, Liu Z, Mao X. Journal: Carbohydr Polym; 2019 May 01; 211():329-335. PubMed ID: 30824097. Abstract: Colloidal chitin, the substrate of chitinase with an open hydrated gel-like structure, can be obtained by treatment using either traditional hydrochloric acid (HCl) or ionic liquid (IL) 1-ethyl-3-methylimidazolium acetate ([Emim][OAc]). IL-pretreated chitin provided an efficient production of N-acetylglucosamine (175.62 mg g chitin) and N,N'-diacetylchitobiose (341.70 mg g chitin) with a conversion of 61.49% at 48 h catalyzed by chitinase from Streptomyces albolongus ATCC 27414. A short time second homogenization treatment after IL pretreatment can increase the conversion to 76.11%. A comprehensive characterization and comparison of chitin with different pretreatments suggested that enzymatic performances were correlated with the structural changes (size of the grains and porosity), high decrease in crystallinity, and high enzyme adsorption. The NMR spectroscopy studies of N-acetylglucosamine solvation in [Emim][OAc] clearly suggest that hydrogen bonding is formed between the hydroxyls of N-acetylglucosamine and both the anions and cations of the IL.[Abstract] [Full Text] [Related] [New Search]