Immobilization of a keratinolytic protease from Purpureocillium lilacinum on genipin activated-chitosan beads |
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| Affiliation: | 1. Research and Development Center for Industrial Fermentations, CINDEFI (CONICET-La Plata, UNLP), Calle 47 y 115, B1900ASH La Plata, Argentina;2. Laboratory of Applied Glycobiotechnology, Food Research Department, School of Chemistry, Universidad Autónoma de Coahuila, Saltillo 252800, Coahuila, Mexico;1. Department of Genetics, School of Biological Sciences, Madurai Kamaraj University, Madurai, India;2. Department of Biotechnology, Indian Institute of Technology Madras, Chennai, India;3. VIT Bhopal University, Bhopal, India;1. Sustainable Biotechnology Laboratory (LIBioS), National University of Quilmes, Roque Sáenz Peña 352, Bernal B1876BXD, Argentina;2. Heterogeneous Biocatalysis Group, CIC Biomagune, Edificio Empresarial “C”, Paseo Miramón 182, Donostia-San Sebastián 20009, Spain;3. Ikerbasque, Basque Foundation for Science, Alda. Urquijo, Urkixo Zumarkalea 36, Bilbao 48011, Spain;4. Institute of Catalysis and Petrochemistry (ICP-CSIC), Campus UAM-Cantoblanco, Madrid 28049, Spain;1. Institute of Theoretical Chemistry, School of Chemistry and Chemical Engineering, Shandong University, Jinan, PR China;2. Department of Chemical and Environmental Engineering, Anyang Institute of Technology, Anyang 455000, China |
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| Abstract: | 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 1 h 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. |
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| Keywords: | Keratinase Immobilization Genipin Chitosan beads Hair waste |
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