α-胰凝乳蛋白酶的固定化及其对DL-苯丙氨酸的光学拆分

Immobilization of α-Chymotrypsin and its Application to Resolution of DL-Phenylalanine

以氨丙基多孔硅球为载体，戊二醛为交联剂制得固定化α-胰凝乳蛋白酶．其含酶量为3．6mg／g，米氏常数Km=1．2×10－3mol／L，最适宜温度为35℃，pH值为7．0，对热、酸碱、甲醇以及尿素的稳定性有较大提高，Ca2+激活效应明显．用该固定化酶连续拆分DL-苯丙氨酸制备L-苯丙氨酸时，拆分产率高于90％，产品纯度超过96％；连续使用2个月后仍能保持较高酶活力．

α-Chymotrypsin has been immobolized on porous silica beads. The activity,opti-mum temperature and pH of the immobilized chymotrypsin as well as its Micllaelis constant have also been determined. its stabilities to heat, acid, base, methanol and urea are in-creased remarkably. It has been applied to resolving DL-phenylalanine continuously more than two months with good performance. L-Phenylalanine is obtained in a yield of 90%, and its optical purity reaches as high as 96%.