Cloning and expression of pectinase gene from two forest soil bacteria, Streptomyces sp.

Abstract

Pectinase is a prominent industrial enzyme with a high market demand and huge applications in diverse avenues. There are different sources for pectinase production; however, a highly stable microbial pectinase that can withstand different physiochemical conditions is needed. Therefore, this study explored the thermostability of the pectinase protein cloned and expressed in Escherichia coli BL21(DE3) from two forest soil bacteria (S-5 and S-14) identified as Streptomyces sp. The pectinase gene illustrated about 750 bp on the gel after electrophoresis and encoded a product of approximately 25 kDa molecular weight. Both expressed pectinase proteins showed optimal activity at 2 different pHs (pH 5 and 9) and 50 ℃. When both recombinant pectinases were exposed to different temperatures, they were able to retain their activity for 120 min indicating both have important thermostable properties. These enzymes could have great potential in industrial biotechnological processes due to their stability over broad pH and high temperatures.