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α‐Amylase immobilization on functionalized nano CaCO 3 by covalent attachment
Author(s) -
Demir Serap,
Gök Sevda Burcu,
Kahraman Memet Vezir
Publication year - 2012
Publication title -
starch ‐ stärke
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.62
H-Index - 82
eISSN - 1521-379X
pISSN - 0038-9056
DOI - 10.1002/star.201100058
Subject(s) - glutaraldehyde , immobilized enzyme , chemistry , covalent bond , calcium carbonate , nuclear chemistry , nanoparticle , calcium alginate , amylase , yield (engineering) , enzyme , enzyme assay , calcium , chromatography , organic chemistry , nanotechnology , materials science , metallurgy
In this study, α‐amylase was immobilized on glutaraldehyde activated silanized calcium carbonate nanoparticles by a using covalent binding method. The surface modified nano calcium carbonate (CaCO 3 ) were characterized using FTIR and SEM. Immobilization yield was found as 199.43 mg/g of calcium carbonate nanoparticles. The maximum activity was observed at pH 6.5. The immobilized enzyme had a higher activity at elevated temperature (50–90°C) than the free one. Reuse studies demonstrated that the immobilized enzyme could reuse 25 times while retaining 18.2% of its activity. Free enzyme lost its activity completely within 15 days. V max values for the free and immobilized enzymes were calculated as 10 and 0.35 mg/mL/min, respectively.