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Optimization and Purification of Inulinase in Aspergillus Ficuum AF-98

Author: ZuoYaQin
Tutor: LuZhaoXin
School: Nanjing Agricultural College
Course: Fermentation Engineering
Keywords: Aspergillus ficuum inulinase optimization purification properties
CLC: TS201.25
Type: Master's thesis
Year: 2008
Downloads: 91
Quote: 1
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Abstract


Inulinases are 2,1-β-fructanohydrolases which convert inulin,a polymer of fructose inβ-2,1 linkage,to fructoses or fructooligosaccharides at proper temperature.Thus,the use of microbial inulinase has been proposed as the most promising approach to obtain fructoses and fructooligosaccharides.So the research on inulinase has been receiving more and more attention.A strain of Aspergillus ficuum AF-98 which produces inulinase was stored in our laboratory.In this paper,we studied the optimization of fermentation parameters,the purification and properties of inulinase from Aspergillus ficuum AF-98.The main research findings are as follows:1.Based on the results of single factor experiments,response surface methodology and orthogonal experiments have been used to optimize the cultivation medium and the fermentation parameters,respectively.The optimal levels oft he main factors are as follows: inulin 20.25g/L、protose-peptone 21.20g/L、（NH4）2SO4 5.3g/L,NaCl 5 g/L、MgSO4·7H2O 0.5 g/L,ZnSO4·7H2O 0.1 g/L、initial pH 6.5、inoculum amount 6%、volume of medium 50mL/250mL Erlenmeyer flask、cultivation temperature 30℃with a fermentation time of 48h.Under this condition,the enzyme activity value was158.44 U/mL.2.Inulinase was purified from the culture broth by ammonium sulphate precipitation, followed by successive chromatographies on DEAE-Sephacel and Sephadex G-100 columns. The enzyme was purified 7.06 fold with 4.9%activity yield from the starting culture broth and the specific activity reached 376.78U/mg.The molecular weight of the purified en-yme was estimated to be 48977KDa by SDS-PAGE.3.The optimal reaction temperature and pH were 60℃and 4.0 respectively.The enzyme were stable under 60℃within pH3.0～7.0.The enzyme activity was enhanced with 5mM Mn2+,whereas the addition of Co2+,Cu2+ and Mg2+ almost had no effect on inulin hydrolytic activity;on the contratry the inulinase activity was significantly inhibited in the presence of Ag+,Zn2+,Ca2+,Ba2+,Na+ and metal chelating agent EDTA.The Michaelis constant（Km） and maximum reaction velocity(Vmax) were found to be 35.72mg/mLand 16.34μmol·min-1mL-1,respectively.

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