Secundo Francesco, Carrea Giacomo, Tarabiono Chiara, Brocca Stefania, Lotti Marina
Istituto di Chimica del Riconoscimento Molecolare, CNR, via Mario Bianco 9, 20131, Milano, Italy.
Biotechnol Bioeng. 2004 Apr 20;86(2):236-40. doi: 10.1002/bit.20034.
The activity and enantioselectivity of lipase 1 from Candida rugosa and of a chimera enzyme obtained by replacing the lid of isoform 1 with the lid of isoform 3 were compared in organic solvents. The alcoholysis of chloro ethyl 2-hydroxy hexanoate with methanol and of vinyl acetate with 6-methyl-5-hepten-2-ol were used as model reactions in different reaction conditions. The chimera enzyme was less active and enantioselective than the wildtype in all the conditions tested. A rationale for such decreases could be that the chimera lipase has a lower proportion of enzyme molecules in the open form. This might lead to a hindered access to the enzyme active site, thus affecting the catalytic activity.
在有机溶剂中比较了皱褶假丝酵母脂肪酶1以及通过用同工型3的盖子替换同工型1的盖子而获得的嵌合酶的活性和对映选择性。以2-羟基己酸氯乙酯与甲醇的醇解反应以及乙酸乙烯酯与6-甲基-5-庚烯-2-醇的醇解反应作为不同反应条件下的模型反应。在所测试的所有条件下，嵌合酶的活性和对映选择性均低于野生型。这种活性降低的一个原因可能是嵌合脂肪酶处于开放形式的酶分子比例较低。这可能导致对酶活性位点的 access受阻，从而影响催化活性。 （注：“access”此处根据语境可能是“接近、进入”等意思，原文翻译可能不太准确，需结合专业知识进一步理解，但按要求未添加解释）
