title: Purification and characterization of hepatic lipase from Todarodes pacificus.
abstract: Lipase was purified from squid (Todarodes pacificus) liver in an attempt to investigate the possibility of applying the enzyme for biotechnological applications. Crude extract of squid liver was initially fractionated by the batch type ion exchange chromatography. The fraction containing lipase activity was further purified with an octyl-Sepharose column. Finally, lipase was purified by eluting active protein from a non-dissociating polyacrylamide gel after zymographic analysis. Molecular weight of the purified enzyme was determined to be 27 kDa by SDS-polyacrylamide gel electrophoresis. The enzyme showed the highest activity at a temperature range of 35-40 degrees C and at pH 8.0. The activity was almost completely inhibited at 1 mM concentration of Hg(2+) or Cu(2+) ion. Partial amino acid sequence of the enzyme was also determined.
authors: Department of Chemistry, Kangnung National University, Gangneung, Korea.
authors: Jongwon
authors: J
authors: Park
authors: Soon-Yeong
authors: SY
authors: Cho
authors: Suk-Jung
authors: SJ
authors: Choi
mesh_terms: D000818:Animals; D001681:Biological Assay; D049832:Decapodiformes / Q000201:enzymology*; D004586:Electrophoresis; D006868:Hydrolysis; D008049:Lipase / Q000302:isolation & purification* / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D012015:Reference Standards; D013379:Substrate Specificity
chemical_list: D008049:Lipase