Co-immobilization mechanism of cellulase and xylanase on a reversibly soluble polymer.
Cellulase and xylanase from Trichoderma reesei were immobilized simultaneously on Eudragit L-100, a reversibly soluble polymer. The effects of polymer concentration and polymer precipitation pH on enzyme activity recovery were investigated at an enzyme complex concentration of 1%. The immobilization mechanism of cellulase and xylanase on the polymer was discussed. An activity recovery of 75% and 59% was obtained for the cellulase and the xylanase, respectively, under the condition of a polymer concentration at 2% and a polymer precipitation pH at 4.0. Most zymoproteins might be connected to the polymer by electrostatic attraction in a medium of pH 4.8. In addition, the covalent coupling between the zymoproteins and the polymer was demonstrated by the infrared spectrograms. It was suggested that dehydration-condensation reaction occurred between the zymoproteins and the polymer during the immobilization.
Xu
Zidong
Z
State Key Laboratory of Materials-Oriented Chemical Engineering, College of Food Science and Light Industrial Technology, Nanjing University of Technology, Jiangsu, Nanjing, China.
Miao
Yelian
Y
Chen
Jie Yu
JY
Jiang
Xuejian
X
Lin
Lijun
L
Ouyang
Pingkai
P
D002480:Cellulase / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry; D005656:Fungal Proteins / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D011108:Polymers / Q000737:chemistry*; D014242:Trichoderma / Q000737:chemistry / Q000201:enzymology*; D043325:Xylan Endo-1,3-beta-Xylosidase / Q000737:chemistry*
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D011108:Polymers; D043325:Xylan Endo-1,3-beta-Xylosidase; D002480:Cellulase