Development of an effective method for purifying trypsin using a recombinant inhibitor.

A trypsin affinity material was prepared by covalently immobilizing buckwheat trypsin inhibitor (BTI) on epichlorohydrin-activated cross-linked agarose gel (Selfinose CL 6B). The optimal conditions for activating Selfinose CL 6B were 15% epichlorohydrin and 0.8 M NaOH at 40°C for 2 h. The optimal pH for immobilizing BTI was 9.5. BTI-Sefinose CL 6B showed a maximum adsorption capacity of 2.25 mg trypsin/ (g support). The material also displayed good reusability, retaining over 90% of its initial adsorption capacity after 30 cycles. High-purity trypsin was obtained from locust homogenate using BTI-Selfinose CL 6B through one-step affinity chromatography. The molecular mass and K

Informations de copyright

Copyright © 2024. Published by Elsevier Inc.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare no conflict of interest.