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用不同的氨基保护的消旋氨基酸或酯作为羧基组分，在α－胰凝乳蛋白酶或木瓜蛋白酶的催化下与另一氨基酸的酰胺或酯缩合形成预期的光活性肽产物．以Ｌ－构型底物计算肽的产率为５５％～８３％，化合物的物理学常数与用相应的Ｎ－保护－Ｌ－氨基酸或酯为羧基组分，分别用化学法或酶促法测定所得结果一致．研究结果表明：利用酶的立体专一性，在形成肽键的过程中进行立体选择可得到光学活性的产物而不需预先拆分；只要溶剂体系中含有酶所需要的微量必需水，酶促反应在有机溶剂中可以顺利地进行．
Racemic amino acids or esters protected with different amino groups as the carboxyl component are condensed with the amide or ester of another amino acid under the catalysis of alpha-chymotrypsin or papain to form the expected photoactive peptide product. The yield of the peptide was calculated from the L-configuration substrate at 55% to 83%. The physical constants of the compounds were determined with the corresponding N-protected-L-amino acids or esters as the carboxyl component by chemical or enzymatic methods Determination of the results obtained. The results show that: the use of three-dimensional enzyme specificity in the formation of peptide bonds in the process of stereoselective optically active products can be obtained without prior resolution; as long as the solvent system contains trace amounts of water necessary for the enzyme, enzyme The reaction can be carried out smoothly in an organic solvent.