Open AccessEvaluation of inorganic matrixes as supports for immobilization of microbial lipase
Author(s) -
Heizir F. de Castro,
M.L.C.P. Silva,
G.L.J.P Silva
Publication year - 2000
Publication title -
brazilian journal of chemical engineering/brazilian journal of chemical engineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.313
H-Index - 52
eISSN - 1678-4383
pISSN - 0104-6632
DOI - 10.1590/s0104-66322000000400048
Subject(s) - lipase , chemistry , candida rugosa , glutaraldehyde , hydrolysis , adsorption , thermal stability , chromatography , immobilized enzyme , tributyrin , nuclear chemistry , organic chemistry , enzyme
Candida rugosa was immobilized by physical adsorption on several inorganic supports using hexane as coupling medium. The enzymatic activities of the different derivatives were determined by both hydrolysis of olive oil and esterification of n-butanol with butyric acid. The results were compared to previous data obtained by using a controlled porous silica matrix. The goal was to contribute in searching inexpensive supports for optimum lipase performance. All supports examined exhibited good properties for binding the enzyme lipase. Zirconium phosphate was the best support, giving the highest percentage of protein fixation (86%) and the highest retention of lipase activity after immobilization (34%). The operational stability performance for niobium oxide derivative was improved by previously activated the support with silane and glutaraldehyde. Thermal stabilities were also examined by thermal gravimetric analysis (TG)