Improving the properties of chitosan supprt for the covalent immobilization of L-arabinose isomerase

MANZO, RICARDO; FENOGLIO, CECILIA; RUBIOLO, AMELIA; MAMMARELLA, ENRIQUE

Foz de Iguazú

Simposio; XIX Simpósio Nacional de Bioprocessos - SINAFERM y X Simpósio de Hidrólise Enzimática de Biomassas - SHEB; 2013

Associação Brasileira de Engenharia Química

Changing gel structure led to a significant improvement in the covalent multipoint attachment of L-arabinose isomerase (L-AI) on chitosan. The use of D-lactose, D-fructose, polyvinyl alcohol, sodium tripolyphosphate, aluminium polychloride, dimethylformamide or 2,4,6-trinitrobenzene sulfonic acid and the activation with glutaraldehyde allowed the modification of the gel structure. Immobilization yields and recovered activities were evaluated and compared with commercial supports of glyoxyl activated agarose gel. Enzyme immobilization in N-alkyl chitosan derivative produced by fructose addition has conducted to the best chitosan derivative. This support allowed an enzyme load up to 9.3 mg L-AI per ggel with a specific activity of 88.4 U ggel-1, while the best commercial glyoxyl activated agarose support allowed an enzyme load up to 28.9 mg L-AI per ggel with a specific activity of 153.8 U ggel-1.