Influence of cofactor concentration in the activity of L-arabinose isomerase immobilized on chitosan

DE SOUSA, MARYLANE; MANZO, RICARDO M.; MAMMARELLA, ENRIQUE J.; ROCHA BARRO GONÇALVES, LUCIANA

Fortaleza

Simposio; VI Simposio Iberoamericano de quitina y en la XII conferencia internacional sobre quitina y quitosano; 2012

Sociedad Iberoamericana de Quitina

L-Arabinose isomerase (LAI) has been of interest and studied intensively in recent years due to its industrial feasibility in D-tagatose production [1]. The production of D-Tagatose has attracted a great deal of attention [2] due to its health benefits and similar properties to sucrose. However, unlike sucrose, it has a low calorific value and it can be used to replace sucrose in various products [3,4]. It is also useful as an intermediate for the synthesis of optically active compounds and as an additive in detergent, cosmetic and pharmaceutical formulation [5]. Aiming costs reduction in D-tagatose production catalyzed by LAI, enzyme immobilization was performed. Among the various natural organic support used in immobilization of enzymes, chitosan may be used due to the presence of different functional groups, such as hydroxyl and amino groups, enabling the use of different methods of activation and immobilization. It is a renewable, low cost and biodegradable natural product that has a great economic and environmental importance. This biopolymer has a molecular structure chemically similar to cellulose, differing only in functional groups [6].Since the removal of metals, including Mn2+, is well described in the literature [7], the effect of Mn2+ concentration, a cofactor, was studied. According to Patrick and Lee [8], L-arabinose isomerase requires Mn2+ as a cofactor to enhance the isomerization rate reaction.