Ali_2022_Antonie.Van.Leeuwenhoek__

Lipase being a hydrolysable enzyme plays a major role in serving various purposes of the industries. Thus, it is very important to have a sustainable and efficient source of this enzyme. In this present study, several microorganisms were isolated from medicinal effluent of a pharmaceutical industry that could produce efficient lipase activity. Among these isolates, a designated strain scl1 was isolated and based on the molecular and biochemical characterisation was tentatively assigned to the genus Serratia. Preliminary studies confirmed the strain scl1 was found to exhibit the highest production of lipase at a temperature and pH of 35 degreesC and 7, respectively under the incubation for 48 h. Further, the lipase activity was measured by following spectrophotometric method using pNPP as the substrate in which the Km and Vmax of the crude enzyme was found to be 3.349 x 10(-3) M and 5.68 x 10(-1) unit/mL, respectively. The extracellular crude lipase was found to show a temperature and pH optima of 75 degreesC and 8, respectively which gave a strong indication that the enzyme appeared to be highly thermostable. This study revealed the strain scl1 is able to produce a thermostable lipase which can meet the needs of the modern-day industrialization techniques. However, more work is required to purify the enzyme and get it ready for commercial applications.