Modification of chitin properties for enzymatic deacetylation

✍ Scribed by Paul D. Beaney; Quan Gan; Thomas R. A. Magee; Michael Healy; Jaime Lizardi-Mendoza

• Publisher: Wiley (John Wiley & Sons)
• Year: 2007
• Tongue: English
• Weight: 637 KB
• Volume: 82
• Category: Article
• ISSN: 0268-2575
• DOI: 10.1002/jctb.1647

✦ Synopsis

Abstract

Chitins produced via a conventional chemical route as well as from a new biological process were modified to increase the efficiency of enzymatic deacetylation reactions for the production of novel biological chitosan. These modified chitins were reacted for 24 h with extracellular fungal enzymes from Colletotrichum lindemuthianum. The chemical and physical properties of the various substrates were analysed and their properties related to the effectiveness in the deacetylation reaction. Modifications of the chitins affected the degree of deacetylation with varied effects. Without further modification to reduce crystallinity and to open up the solid substrate structure, the chitins were found to be poor substrates for the heterogeneous solid‐liquid enzymatic catalysis. It was found that the solvent and drying method used in modifying the chitins had significant impact on the final efficiency of the enzymatic deacetylation reaction. The most successful modifications through freeze drying of a colloidal chitin suspension increased the degree of enzymatic deacetylation by 20 fold. These processes reduce the crystallinity of the chitin making it easier for the enzymes to access their internal structure. X‐ray diffraction, scanning electron microscopy, thermogravimetric analysis, and BET isotherm analysis are employed to characterise the modified chitins to ascertain the degree of crystallinity, porous structure, surface area, and morphology. Copyright © 2007 Society of Chemical Industry