植物乳杆菌产乳酸脱氢酶的发酵条件优化及酶的纯化

Fermentation Optimization and Purification of Lactate Dehydrogenase from Lactobacillus Plantarum

对植物乳杆菌突变株RS2-2的发酵条件做了优化,在25 L发酵罐上进行放大实验,使菌株RS2-2的乳酸脱氢酶(Lactate Dehydrogenase)产酶水平有了较大提高,细胞抽提液比酶活达到24.6 U/mg.利用DEAE离子交换、疏水层析对酶的纯化进行了研究,最终酶的纯化倍数为49.1,比活力达1 208.6 U/mg,初步确定了LDH的纯化路线.

High output of the lactate dehydrogenase （LDH） from lactobacillus plantarum RS2-2 was achieved after optimization of the fermentation conditions and magnified experiment was carried out on 25 L fermentor. The LDH activity of cell extraction reached to 24.6 U/mg. Purification of the LDH was also studied by means of DEAE ion-exchange and hydrophobic chromatography, which resulted in 49.1-fold purification and 1 208.6 U/mg specific activity. The routine of LDH separation was primarily determined.