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Physicochemical and catalytic properties of acylase I from aspergillus melleus immobilized on amino‐ and carbonyl‐grafted stöber silica
Author(s) -
KołodziejczakRadzimska Agnieszka,
Zdarta Jakub,
Jesionowski Teofil
Publication year - 2018
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.2610
Subject(s) - glutaraldehyde , chemistry , catalysis , nuclear chemistry , chemical modification , fourier transform infrared spectroscopy , chromatography , organic chemistry , polymer chemistry , chemical engineering , engineering
Acylase I from Aspergillus melleus was immobilized on supports consisting of unmodified and modified silica. Modification was performed using 3‐aminopropyltriethoxysilane (APTES) and glutaraldehyde (GA). The effectiveness of immobilization was investigated using the standard Bradford method in addition to a number of physicochemical techniques, including spectroscopic methods (FTIR, 29 Si and 13 C CP MAS NMR), porous structure and elemental analysis, and zeta potential measurement. A determination of catalytic activity was made based on the deacetylation reaction of N‐acetyl‐ l ‐methionine. Furthermore, the effect of pH and temperature on the catalytic activity of the free and immobilized enzyme, as well as the reusability of the silica‐bound aminoacylase, were determined. The immobilized systems demonstrated a high degree of catalytic activity. The best catalytic parameters were those of aminoacylase immobilized on silica modified with APTES (apparent activity 3937 U/g, relative activity 61.6%). © 2018 American Institute of Chemical Engineers Biotechnol. Prog. , 34:767–777, 2018