从环境土壤中筛选到一株酶活较高、高温耐碱性的果胶酶菌株AP-1并对其产酶性质和分离纯化做了初步研究。酶活性质研究结果表明:该酶最适温度为70℃,最适p H 7.5。稳定性实验表明:该酶具有较好的耐碱性,同等条件下Mg(2+)对该酶具有显著的激活作用。分离纯化实验表明:硫酸铵盐析法中80%饱和度的硫酸铵溶液的纯化倍数最高达到了2.20倍;有机溶剂沉淀法中乙醇(2∶1)的纯化效果最好达到了5.20倍。
A bacterial strain producing high-activity and high-temperature alkaline pectinase was obtained from the soil and was named as AP-1. The characteristics and the separation and purification of the pectinase produced by AP-1 were preliminarily studied. The result of the study on pectinase activity showed that the optimal temperature and p H of the pectinase were 70℃ and 7. 5,respectively. The experiment of stability showed that the enzyme had good resistance to alkali and was activated remarkably by Mg~(2 +)under the same conditions.The separation and purification showed that the purification effect was better when the enzyme was treated by 80% saturation of ammonium sulfate solution than other,but the purification effect was the best when the enzyme was treated by ethanol.