화학공학소재연구정보센터
Process Biochemistry, Vol.41, No.6, 1325-1331, 2006
Catalytic performance of invertase immobilized by adsorption on anionic exchange resin
Invertase (E.C.3.2.1.26; K-m = 17.0 mM, V-max = 0.0240 U mL(-1), optimal activity at 55 degrees C and pH 5.0) was adsorbed on DOWEX (R)-anionic resin (types 1X2:100-400, 1X4:50-400 and 1X8:50-400), resulting in the DOWEX (R)-1X4-200 as the best support. One hundred milligrams of DOWEX (R)-1X4-200 were suspended in a 25 mL invertase solution (total activity 35 U) at 32 degrees C, pH 5.5, agitation of a 100 rpm for 4 h. The complex DOWEX (R)-1X4-200/invertase (D1X4-2001) (V-max = 0.0450 U mL(-1) and K = 18.3 mM) had an optimal activity at 45 degrees C and pH 4.5. The catalytic performance of D1X4-2001 was evaluated through the sucrose hydrolysis in a continuous membrane reactor coupled with a UF-membrane (cut off 100 kDa) or a MF-membrane (a pore diameter of 5 mu m). The assays were carried out for at least 30 h under an agitation of 100 rpm, a dilution rate of 1.6 h(-1), a substrate concentration of 2.5 mM, pH 5.5 and 30 degrees C. No enzyme leakage from the support was detected and hydrolysis yield of both 84 and 95% were attained with UF- and MF-membranes, respectively. (c) 2006 Elsevier Ltd. All rights reserved.