A chromogenic oxidative coupling reaction of laccase: applications for laccase and angiotensin I converting enzyme assay.

T Shin, S Murao, E Matsumura
Author Information
  1. T Shin: Department of Applied Microbial Technology, Kumamoto Institute of Technology, Japan.

Abstract

A sensitive chromogenic assay for p-hydroxybenzoic acid, laccase activity, and angiotensin I converting enzyme activity is described. The method relies on the oxidative coupling of 2,2'-azino-di(3-ethylbenzothiazoline-6-sulfonic acid) and p-hydroxybenzoic acid. Lacase catalyzes the formation of a deep-purple compound, which shows a broad absorption between 530 and 630 nm with a maximum at 593 nm (the molar absorption coefficient was calculated to be 26,900). By means of this chromogenic coupling reaction, a spectrophotometric method for the assay of laccase activity and estimation of the amount of p-hydroxybenzoic acid was developed; laccase activity in the range 1-10 pmol protein could be estimated with a 10-min incubation time. Angiotensin I converting enzyme was also assayed by the laccase-catalyzed indicator reaction, using p-hydroxybenzoyl-glycyl-histidyl-leucine as the substrate, and N alpha-carbobenzoxy amino acid urethane hydrolase as the coupling enzyme.

MeSH Term

Chemical Phenomena
Chemistry
Kinetics
Laccase
Oxidation-Reduction
Oxidoreductases
Peptidyl-Dipeptidase A

Chemicals

Oxidoreductases
Laccase
Peptidyl-Dipeptidase A

Word Cloud

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