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Pineapple stem bromelain immobilized on different supports: Catalytic properties in model wine
Author(s) -
Ilaria Benucci,
Marco Esti,
Katia Liburdi,
Maria Vittoria Garzillo Anna
Publication year - 2012
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.1639
Subject(s) - bromelain , glutaraldehyde , wine , chemistry , covalent bond , immobilized enzyme , substrate (aquarium) , biocatalysis , catalysis , chitosan , chromatography , protease , combinatorial chemistry , enzyme , organic chemistry , food science , biology , reaction mechanism , ecology
Bromelain from pineapple stem has been covalently immobilized on different supports to select the more efficient biocatalyst that should be applied toward unstable proteins in real white wine. In this preliminary study, catalytic properties of different immobilized bromelain forms were compared under wine‐like conditions, against a synthetic substrate (Bz‐Phe‐Val‐Arg‐pNA).Covalent immobilization affected protease kinetic properties, even if all immobilized forms presented both a better substrate affinity and higher half‐life (with the exception of a few procedures) with respect to the free enzyme. Stem bromelain was successfully immobilized on chitosan beads without glutaraldehyde thus yielding a food‐safe and promising biocatalyst for unstable real wine future application. © 2012 American Institute of Chemical Engineers Biotechnol. Prog., 2012