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標題: Adsorption/Intercalation of Chymotrypsin in Montmorillonite and its Effects on Enzymatic Activity
關鍵字: 蛋白質;protein;蒙脫土;活性;插層;吸附;酵素;chymotrypsin;adsorption;intercalation;activity;montmorillonite;enzyme
出版社: 化學工程學系
In this study, the protein, α-chymotrypsin, was successfully intercalated in the gallery of montmorillonite (MMT). The protein intercalation in MMT preintercalated with polypropylene oxide (D2000) was highly enhanced (4.4 mg/mg clay) as compared to that (1.7 mg/mg clay) adsorbed at the surface of native Na-montmorillonite (Na-MMT). The d-spacing of MMT after α-chymotrypsin intercalation increased from 5.8 to 7.0 nm by XRPD analysis. The result shows that strong interactions occur between α-chymotrypsin and MMT, leading to the pronounced stabilization effect on the enzyme in the gallery of clay. Except for pH 11, the interaction of the enzyme occurred in the whole range of pH used in this study, although the amount intercalation protein varied with pH. The highest extent of intercalation has been observered at pH 7. While α-chymotrypsin adsorbed at the surface of Na-MMT lost most of its enzymatic activity, the catalytic capability of α-chymotrypsin intercalated in MMT toward low molecular weight substrates remained to a significant extent.

於本研究中,成功插層蛋白質酵素(α-chymotrypsin)於蒙脫土層間中。高分子(D2000)插層之蒙脫土(MMT-D2000)對α-chymotrypsin具有極佳之吸附/插層能力,約為天然蒙脫土(Na-MMT)之2.5倍(MMT-D2000最大之吸附量為4.4 mg/mg clay,Na-MMT為1.7 mg/mg clay)。由X光粉末繞射儀中可得知,MMT-D2000之d-spacing由原本的5.8 nm提高至7.0 nm,亦即α-chymotrypsin與MMT-D2000中之D2000發生置換,而進入其層間。插層之α-chymotrypsin與蒙脫土間具有一定之作用力,不易發生脫落。改變吸附溶液之pH 值,α-chymotrypsin亦能插層進入MMT-D2000層間(除pH 11外),且吸附量隨pH值改變而有差異,於pH 7時最大。α-chymotrypsin吸附於Na-MMT後,其活性大幅下降,且失活速率相當快,酵素活性不因吸附量多寡而改變;插層於MMT-D2000後,其活性並無明顯改變,而與溶液中之α-chymotrypsin相近,酵素活性隨插層量比例增加而增加,且層間的α-chymotrypsin對基質具有一定之選擇性。
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