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Using a Membrane Reactor for Sucrose Hydrolysis: The Effect of Reactor's Design on Invertase Stability

Using a Membrane Reactor for Sucrose Hydrolysis: The Effect of Reactor's Design on Invertase Stability

作     者:Francesco di Addezio Ester Junko Yoriyaz Laura Cantarella Maria Cantarella Michele Vitolo 

作者机构:Department of lndustrial and lnformation Engineering and Economics University of L 'Aquila L 'Aquila 67100 Italy Department of Biochemical and Pharmaceutical Technology University of Sao Paulo S6o Paulo 05508900 Brazil Department of Civil and Mechanical Engineering University of Cassino and of Lazio Meridionale Cassino 03043 Italy 

出 版 物:《Journal of Environmental Science and Engineering(A)》 (环境科学与工程(A))

年 卷 期:2013年第2卷第9期

页      面:582-592页

学科分类:081702[工学-化学工艺] 08[工学] 0817[工学-化学工程与技术] 0822[工学-轻工技术与工程] 082202[工学-制糖工程] 

主  题:Invertase sucrose membrane reactor. 

摘      要:Invertase hydrolyses sucrose, produces inverted sugar syrup, which is used, mainly, as a food composition in industries. To carry out the hydrolysis properly, the invertase should be stable in the soluble form through a considerable reaction period and recovered afterwards. The chosen reactor was a CSTR-type (continuous stirred tank reactor-type) coupled with an UFM (ultrafiltration-membrane), the so-called MR (membrane reactor). The varied parameters were: sucrose concentration (10-300 mM), temperature (5-65 ℃), reaction volume (14 mL and 65 mL), stirring (100-500 rpm), volumetric feeding rate (2.2-12 mL/h) and UFM MWCO (molecular weight cut off) (10, 20, 30, 50 and 100 kDa). The invertase kinetic constants (KM = 23.5 mM; Vmax = 2,758 μmolgluJmin-mgprot; Ea = 9.1 kcal/mol) and the temperature deactivation energy (Ead= 20 kcal/mol) were calculated. Moreover, the invertase was unstable as the MR capacity diminished and the agitation increased up to 500 rpm most likely due to the damaging effect of shearing forces (present inside the MR) on the invertase molecule. Finally, both the MWCO and the chemical nature of the UFM affected the invertase stability along the hydrolysis. The enzyme stability increased as the UFM cut-off decreased, the highest value being observed with the 10 kDa-UFM.

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