Abstract
Inulinase is widely used in the food industry as it can digest inulin derived from various sources and is effective in producing high yield fructose. Inulin from Jerusalem artichoke is the choice of substrates for food industries using inulinase. Inulinase was purified and characterized from an endophytic Rossellomorea aquimaris 3.13 isolated from Jerusalem artichoke. The purified inulinase had molecular mass of 58 kDa as assessed by SDS-PAGE. The optimum temperature and pH were 60°C and pH 5.0, respectively. Enzyme was stable at 60°C and retained 60% residual activity after 90 min. It was also stable in a pH range of 5–7 for 12 h. This inulinase showed greatest substrate specificity, to levan, inulin and raffinose in this order. Thin layer chromatography analysis of the end product revealed that inulinase hydrolyzed inulin extracted from chicory and Jerusalem artichoke, giving only fructose; therefore, the purified enzyme was verified as an exo-inulinase. This study indicated that inulinase from R. aquimaris 3.13 can be used in fructose production from inulin and levan substrates in food technology.