Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads

CAVELLO, IVANA; CONTRERAS ESQUIVEL, JUAN CARLOS; CAVALITTO, SEBASTIÁN FERNANDO

PROCESS BIOCHEMISTRY

ELSEVIER

Lugar: Amsterdam; Año: 2014 vol. 49 p. 1332 - 1336

0032-9592

Keratinase from Purpureocillium lilacinum LPSC # 876 was immobilized on chitosan beads using two different cross-linking agents: glutaraldehyde and genipin. For its immobilization certain parameters were investigated such as cross-linker concentration, activation time and activation temperature. Under optimum conditions, immobilization yield resulted to be 96 and 92.8 % for glutaraldehyde and genipin, respectively, although activity recovery was better when genipin was use, reaching up to 81 %. The immobilized keratinase showed better thermal and pH stabilities compared to the soluble form. The residual activity of immobilized keratinase remained more than 60 % of its initial activity after five hydrolytic cycles. The results in this study supported that glutaraldehyde could be replaced by genipin as an alternative cross-linking eco-friendly agent for enzyme immobilization