Sepharoylaminocaproyl-3-chloroanilide (Sepharose-CH-3-Cl-anilide) was found to be an effective affinity adsorbent for a swep hydrolyzing enzyme from Paecilomyces varioti. It was adsorbed on this affinity column at pH 8.0, and eluted with 0.25 M NaCl in the starting buffer. From the active fractions, two enzymes were separated by the Sephadex G-200 column. One was termed swep hydrolase, hydrolyzing both swep and propanil. The other one was named propanil hydrolase, hydrolyzing only propanil.
The purified swep hydrolase appeared homogeneous on SDS disc electrophoresis, and the molecular weights of the enzyme and the subunit were 280, 000 and 70, 000, respectively. The isoelectric point of this enzyme was pH 4.8.

This article cannot obtain the latest cited-by information.