Citation:
WANG Feng, LIANG Li-Man, GU Zheng-Biao, CUI Zheng-Gang. Immobilization of Amylase on PS-TEPA and PS-g-PEG Resins[J]. Chinese Journal of Applied Chemistry,
;2008, 25(11): 1259-1265.
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Chloroacetylated polystyrene resin was grafted with tetraethylenepentamine or polyethylene glycol which was used to immobilize α-amylase.The immobilization process and the influence of immobilization on the catalytic characteristics of the α-amylase was investigated.It was found that the adsorption of α-amylase by PS-TEPA reached 83%(enzyme activity) and 72%(protein),and the adsorption by PS-g-PEG was 60%(enzyme activity) and 56%(protein).The use of glutaraldehyde had no positive effect on the immobilization of α-amylase.Compared to the free enzyme,the immobilized enzyme exhibited a higher affinity for the substrates,the value of vmax/Km increased from 0.024(free enzyme) to 0.035(PS-TEPA) and 0.038(PS-g-PEG),the optimum temperature was raised from 40℃(free enzyme) to 50℃(PS-TEPA) and 60℃(PS-g-PEG).The optimum pH range was also widened,from pH 7~8(free enzyme) to pH 7~10(PS-TEPA) and pH 5~8(PS-g-PEG) respectively.After washing with deionized water for 43 h,the residual adsorption of the enzyme on PS-TEPA was 1.28 times higher than that on 717 type resin,1.69 times higher than that on PS.The half life of α-amylase,t1/2,was prolonged after the immobilization,from 1 h(free enzyme) to 4.5 h(PS-TEPA) and 7.5 h(PS-g-PEG) at 70℃.
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Keywords:
- PS-TEPA,
- PS-g-PEG,
- α-amylase,
- immobilization,
- function
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