A highly stable biocatalyst obtained from covalent immobilization of a non-commercial cysteine phytoprotease

OBREGÓN, WALTER D.; CISNEROS J.S.; CECCACCI FLORENCIA; QUIROGA, EVELINA

Journal of Bioprocessing & Biotechniques

OMICS Group International

Año: 2015

In this work, araujiain (enzymatic preparation obtained from the latex of Araujia hortorum fruits) was successfully immobilized onglyoxyl-agarose via multipoint covalent attachment. Thus, good efficiency of immobilization and high operational stability of immobilizedenzyme were obtained. The activity of araujiain at alkaline pH was significantly improved after immobilization. In addition, immobilizedaraujiain also showed high activity and good stability, without significant loss in its activity, at temperatures between 37 and 60°C andin the presence of immiscible organic solvents. Immobilized araujiain also showed good performance in a mixture of 50% ethyl acetatein buffer, used for peptide synthesis, with better results than when the free enzyme was used as catalyst. These results indicate thatimmobilized araujiain via multipoint covalent attachment can be highly stabilized and this method might be used for practical applicationsof araujiain in hydrolytic and synthetic processes.