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Main Author:	Bessy Cutiño-Avila
Format:	Artículo científico
Language:	en
Published:	Universidad Nacional de Colombia 2014
Subjects:	Biología papain Bromelain rational design covalent immobilization immobilized derivatives
Online Access:	https://www.redalyc.org/articulo.oa?id=77631180002
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Computer-aided design of bromelain and papain covalent immobilization Bessy Cutiño-Avila Dayrom Gil Pradas Carlos Aragón Abreu Yuniel Fernández Marrero Martha Hernández de la Torre Emir Salas Sarduy María de los Ángeles Chávez Planes José Manuel Guisán Seijas Joaquín Díaz Brito Alberto del Monte-Martínez Biología papain Bromelain rational design covalent immobilization immobilized derivatives Enzymes as immobilized derivatives have been widely used in Food, Agrochemical, Pharmaceutical and Biotechnological industries. Protein immobilization is probably the most used technology to improve the operational stability of these mo - lecules. Bromelain ( Ananas comosus ) and papain ( Carica papaya ) are cystein proteases extensively used as immobilized biocatalyst with several applications in therapeutics, racemic mixtures resolution, affinity chromatography and others in - dustrial scenarios. The aim of this work was to optimize the covalent immobilization of bromelain and papain via rational design of immobilized derivatives strategy (RDID) and RDID 1.0 program. Were determined the maximum protein quantity to immobilize, the optimum immobilization pH (in terms of functional activity retention), was predicted the most probable configuration of the immobilized derivative and the probabilities of multipoint covalent attachment. As support material was used Glyoxyl-Sepharose CL 4B. The accuracy of RDID 1.0 program ́s prediction was demonstrated comparing with ex - perimental results. Bromelain and papain immobilized derivatives showed desired characteristics for industrial biocatalysis, such as: elevate pH stability retaining 95% and 100% residual activity at pH 7.0 and 8.0, for bromelain and papain, respec - tively; high thermal stability at 30 °C retaining 90% residual activity for both immobilized enzymes; a catalytic configuration bonded by immobilization at optimal pH; and the ligand load achieve ensure the minimization of diffusional restrictions. 2014 artículo científico 0123-3475 https://www.redalyc.org/articulo.oa?id=77631180002 en http://www.redalyc.org/revista.oa?id=776 Revista Colombiana de Biotecnología application/pdf Universidad Nacional de Colombia Revista Colombiana de Biotecnología (Colombia) Num.1 Vol.XVI

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