高等学校化学学报 ›› 1997, Vol. 18 ›› Issue (8): 1388.

• 论文 • 上一篇    下一篇

α-胰凝乳蛋白酶的固定化及其对DL-苯丙氨酸的光学拆分

刘立建, 杨平, 卓仁禧   

  1. 武汉大学化学系, 武汉 430072
  • 收稿日期:1996-06-14 出版日期:1997-08-24 发布日期:1997-08-24
  • 通讯作者: 卓仁禧
  • 作者简介:刘立建, 男, 42岁, 博士, 副教授.
  • 基金资助:

    国家自然科学基金

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

LIU Li-Jian, YANG Ping, ZHUO Ren-Xi   

  1. Department of Chemistry, Wuhan University, Wuhan 430072
  • Received:1996-06-14 Online:1997-08-24 Published:1997-08-24

摘要: 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.

关键词: &alpha, -胰凝乳蛋白酶, 固定化, L-苯丙氨酸, 光学拆分

Abstract: α-Chymotrypsin has been immobolized on porous silica beads. The activity,opti-mum temperature and pHof 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%.

Key words: α-Chymotrypsin, Immobolization, L-Phenylalanine, Optical resolution

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