Premium
New methods for binding enzyme molecules into a water‐insoluble matrix: Properties after insolubilization
Author(s) -
Broun G.,
Thomas D.,
Gellf G.,
Domurado D.,
Berjonneau A. M.,
Guillon C.
Publication year - 1973
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260150211
Subject(s) - enzyme , proteolysis , chemistry , cofactor , matrix (chemical analysis) , denaturation (fissile materials) , enzyme assay , molecule , biochemistry , biophysics , chromatography , organic chemistry , biology , nuclear chemistry
New methods of crosslinking enzyme molecules inside a matrix with or without an inactive protein are described. Enzyme activity yields range between 30 and 80% of the activity of the untreated preparations. Even fragile enzyme systems, for instance those using mobile cofactors, can be efficiently immobilized. Increased resistance towards heat denaturation and proteolysis results.