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

• Published in: Process biochemistry (1991) Vol. 49; no. 8; pp. 1332 - 1336
• Main Authors: Cavello, Ivana Alejandra, Contreras-Esquivel, Juan Carlos, Cavalitto, Sebastián Fernando
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.08.2014
• Subjects: Chitosan beads; Genipin; Hair waste; Immobilization; Keratinase; Keratinase; Immobilization; Hair waste; Chitosan beads; Genipin
• ISSN: 1359-5113; 1873-3298
• DOI: 10.1016/j.procbio.2014.04.016

•A novel keratinase was immobilized on chitosan beads using genipin as crosslinker.•Immobilized enzyme retained more than 85% of its activity at pH 11 after 1h.•After 1h at 50°C, the immobilized enzyme retained 74% of residual activity.•The immobilized keratinase exhibited high reusability for azocasein hydrolysis. 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 optimized such as cross-linker concentration, activation time and activation temperature. Under optimum conditions, enzyme immobilization resulted to be 96 and 92.8% for glutaraldehyde and genipin, respectively, with an activity recovery reaching up to 81% when genipin was used. The immobilized keratinase showed better thermal and pH stabilities compared to the soluble form, retaining more than 85% of its activity at pH 11 and 74% at 50°C after 1h of incubation. The residual activity of immobilized keratinase remained more than 60% of its initial value after five hydrolytic cycles. The results in this study support that glutaraldehyde could be replaced by genipin as an alternative cross-linking eco-friendly agent for enzyme immobilization.