由L-精氨酸化学酶法制备D-鸟氨酸盐酸盐

CHEMO-ENZYMATIC PREPARATION OF D-ORNITHINE HYDROCHLORIDE FROM L-ARGININE

实验在碱性溶液中,L-精氨酸经一锅煮水解-消旋反应可获得DL-鸟氨酸,再直接用蜂房哈夫尼菌(Hafnia alvei AS1.1009)中的赖氨酸脱羧酶对其进行生物转化,可制备D-鸟氨酸盐酸盐,收率为45.3%;同时获得腐胺,收率为41.5%。确定了在回流条件下,以1.0 mol/L氢氧化钠水溶液,用0.10摩尔比的水杨醛催化L-精氨酸在3 h内反应为DL-鸟氨酸;对生物转化中赖氨酸脱羧酶性质研究结果表明:添加1 mmol/L的Fe^(2+)可将比酶活性提高为6 119 U。在此优化条件下转化时间为16 h,为制备D-鸟氨酸盐酸盐和腐胺提供了一种新的方法。

The DL-ornithine crystals from the one pot reaction of hydrolysis-racemization of L-arginine was treated as substrate with Hafnia alvei AS1. 1009 intact cells as biocatalysts to produce crystalline D-ornithine hydrochloride with a yield of 45.3% and putrescine with a yield of 41.5% from the reaction mixture after simple purification. In a medium of 1. 0 mol/L NaOH under 100℃ the whole process of racemizing L-arginine can be completed within circa 3 h, using 0. 10 molar equivalent of Salicylaldehyde. D-ornithine and putrescine were produced by means of biotransformation of DL-ornithine in the presence of Hafnia alvei AS1. 1009 decarboxylase. Under the optimization conditions of 1 mmol/L Fe^2＋ ion concentration, the specific activity was up to 6 119 U. L-ornithine can be completely degraded by the decarboxylase for 16 h under the optimization conditions. It provides a new method to prepare D-ornithine and putrescine.