Folia Biologica (Krakow) 2008-01-01

Partial characterization of a lipase from gypsy moth (lymantria dispar L.) larval midgut.

Marija Mrdaković, Jelica Lazarević, Vesna Perić-Mataruga, Larisa Ilijin, Milena Vlahović

Index: Folia Biol. (Krakow.) 56(1-2) , 103-10, (2008)

Full Text: HTML

Abstract

Lipase activity of the gypsy moth (Lymantria dispar L.) was studied by the spectrophotometric method using crude homogenate of fifth-instar larval midgut tissues as the enzyme source and p-nitrophenyl caprylate (pNPC) as substrate. A Km value of 0.310 mM and a Vmax value of 1.479 U/mg prot. were obtained for this substrate. Among various p-nitrophenyl esters tested, maximum activity was obtained for p-nitrophenyl caprylate and p-nitrophenyl caprate. The enzyme was most active at alkaline pH, with maximum at pH 8.2. Decreased activity was detected after preincubation in buffers of pH below 7.0 and above 8.2. The enzyme was unstable at room temperature. The enzyme was Ca2+ independent. Its activity was inhibited by PMSF, Fe2+, Ag+ and Pb2+, while Fe3+ inhibited enzyme activity by about 40%.

Related Compounds

  • 4-NITROPHENYL...

Related Articles:

Medium-based optimization of an organic solvent-tolerant extracellular lipase from the isolated halophilic Alkalibacillus salilacus.

2015-09-01

[Extremophiles 19 , 933-47, (2015)]

Inhibition of Cancer Cell Proliferation and Antiradical Effects of Decoction, Hydroalcoholic Extract, and Principal Constituents of Hemidesmus indicus R. Br.

2015-06-01

[Phytother Res. 29 , 857-63, (2015)]

Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase.

2009-12-08

[Biochemistry 48(48) , 11496-504, (2009)]

Interfacial reaction dynamics and acyl-enzyme mechanism for lipoprotein lipase-catalyzed hydrolysis of lipid p-nitrophenyl esters.

1986-09-15

[J. Biol. Chem. 261(26) , 12016-21, (1986)]

Switch of substrate specificity of hyperthermophilic acylaminoacyl peptidase by combination of protein and solvent engineering.

2011-06-01

[Protein Cell. 2(6) , 497-506, (2011)]

More Articles...