PURIFICATION OF HALOLIPASE FROM HALOFERAX LARSENII (KP636736): AN ARCHAEON ISOLATED FROM GUJARAT, INDIA

Abstract

Extremely halophilic microbes which inhabit the hypersaline environments such as marine salterns, salted food products, soda lakes, etc. are diverse in morphology, physiology and biotechnological applications. Gujarat has a very long coastline (approximately 1600 km) and there are several locations where the sea water is used for manufacturing marine chemicals. We report here the production and purification of an extracellular lipase from the archaeon Haloferax laresnii strain BVM005 (Gen Bank accession no. KP636736) that was isolated from the solar salt works at Okhamadhi, near Dwarka. This isolate had a remarkable characteristic of producing multiple extracellular hydrolyases namely, amylase, caseinase, gelatinase, lipases (hydrolyzed Tween 20, 40, 60 and 80), etc. The Haloferax larsenii lipase (HLL) produced in broth culture was precipitated by using isopropyl alcohol and further purified by reverse-phase chromatography (RPHPLC). Ultra-performance liquid chromatography (UPLC) analysis was used to determine the amino acid profiles. SDSPAGE and Matrix assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) analyses revealed that HLL was a monomer, with a molecular mass of 31kDa. Compared to Lipolase (Novozymes), HLL displayed an elevated and considerable compatibility with various commercialized laundry detergents, and wash performance analysis revealed that it could remove oil-stains effectively. HLL has a number of attractive properties that make it a potential candidate for the synthesis of non-aqueous peptides and application in detergent industry.