Premium
Self‐Assembly of Amyloid Fibrils That Display Active Enzymes
Author(s) -
Zhou XiaoMing,
Entwistle Aiman,
Zhang Hong,
Jackson Antony P.,
Mason Thomas O.,
Shimanovich Ulyana,
Knowles Tuomas P. J.,
Smith Andrew T.,
Sawyer Elizabeth B.,
Perrett Sarah
Publication year - 2014
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201402125
Subject(s) - enzyme , microreactor , fibril , chemistry , biophysics , amyloid fibril , yield (engineering) , biocatalysis , self assembly , enzyme catalysis , immobilized enzyme , combinatorial chemistry , materials science , biochemistry , catalysis , amyloid β , organic chemistry , reaction mechanism , biology , disease , medicine , pathology , metallurgy
Enzyme immobilization is an important strategy to enhance the stability and recoverability of enzymes and to facilitate the separation of enzymes from reaction products. However, enzyme purification followed by separate chemical steps to allow immobilization on a solid support reduces the efficiency and yield of the active enzyme. Here we describe polypeptide constructs that self‐assemble spontaneously into nanofibrils with fused active enzyme subunits displayed on the amyloid fibril surface. We measured the steady‐state kinetic parameters for the appended enzymes in situ within fibrils and compare these with the identical protein constructs in solution. Finally, we demonstrated that the fibrils can be recycled and reused in functional assays both in conventional batch processes and in a continuous‐flow microreactor.