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Effect of immobilization on ficin specificity

學生姓名: 陳義洋
指導教授: 方翠筠
學  期: 113上
摘  要: The development of strategies that can permit to adjust the size specificity of immobilized proteases by the generation of steric hindrances may enlarge its applicability. Using as a model ficin immobilized on glyoxyl agarose, two strategies were assayed to generate tailor made steric hindrances. The combination of both strategies and the use of 37ºC during the proteolysis enabled to almost fully nullify the hydrolytic activity versus hemoglobin while preserving a high percentage of the activity versus casein. Using the Asp/HA supports (with different amount of HA) differences in the effect on enzyme activity versus the different substrates are much more significant, while with some substrates the immobilization produced a decrease in enzyme activity, with in other cases the activity increased. These different effects are even increased after glutaraldehyde treatment. That way, the conformational changes induced by the biocatalyst immobilization or the chemical modification fully altered the enzyme protein specificity
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