Heterologous expression, refolding, and characterization of a calcium-independent phospholipase A1 from Streptomyces albidoflavus

Phospholipase A1 (PLA1) is a member of the hydrolase family with applications in various fields, especially food industry. A calcium-independent PLA1 from Streptomyces albidoflavus was expressed E. coli BL21 (DE3) this study. The results indicated that soluble expression at low level, which possibly due to toxicity host. In contrast, enzyme as inclusion bodies exhibited high-level and 0.3 mg protein could be derived 1 mL culture medium. Furthermore, renaturation achieved through direct dilution method, yielding 29.6 U/mL activity after 16 h 4 °C. For improving efficiency refolding process, continuous strategy established, 155 process. With soybean lecithin substrate, specific purified renatured 1380 U/mg optimal temperature pH found 60 °C 6.5. addition, observed better towards phosphatidyl inositol, whilst lipase detected when catalyzing below 55 Overall, study provides possible solution obtain high yield by heterologous hence promote its further application field