Home
Resources
Publications
Plant Biochemistry of Xenobiotics. Purification and Properties of a Wheat Esterase Hydrolyzing the Plasticizer Chemical, bis(2-ethylhexyl)phthalate

Plant Biochemistry of Xenobiotics. Purification and Properties of a Wheat Esterase Hydrolyzing the Plasticizer Chemical, bis(2-ethylhexyl)phthalate

H W Krell, H Sandermann Jr

Eur J Biochem. 1984 Aug 15;143(1):57-62.

PMID: 6468391

Abstract:

A soluble wheat esterase, catalyzing a cleavage of the mass-produced plasticizer chemical, bis(2-ethylhexyl)phthalate (DEHP), has been discovered. Although wheat plants and seeds as well as cultured wheat cells contained more than 12 non-specific esterase activities, only a single protein with a marked preference for a substrate chain-length of 6-8 carbon atoms was active with DEHP. This enzyme is shown to differ from all previously characterized plant lipases and esterases. The enzyme was purified 10-fold from wheat plants and 280-fold, to electrophoretic homogeneity, from cultured wheat cells. An apparent functional molecular mass of 38 000 Da and an apparent subunit molecular mass of 22 000 Da were determined. Inhibitor experiments pointed to the catalytic involvement of a serine residue. Cleavage of DEHP by the purified enzyme was about 10(4) times slower than cleavage of 4-nitrophenyl octanoate. This was consistent with previous evidence for a rate-limiting role of the esterase reaction in DEHP metabolism by intact wheat cells.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1956101	4-Nitrophenyl octanoate		1956-10-1	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: