Stability of Oxidases Immobilized in Silica Gels Export

@article{citeulike:5805973, abstract = {The gain or loss of stability of three flavoprotein oxidases, glucose oxidase, lactate oxidase, and glycolate oxidase, upon immobilization in a hydrated silica gel by a solgel process was quantified. Glucose oxidase (isoelectric point, IP, pH 3.8) retained most or all of its initial activity, while lactate oxidase and glycolate lost most of theirs. The half-life of glucose oxidase at 63 oC increased upon immobilization 200-fold; the half-lives of lactate oxidase and of glycolate oxidase were not extended beyond those of the water-dissolved enzymes. After lactate oxidase (IP pH 4.6) was electrostatically complexed with the weak base poly(N-vinylimidazole) prior to its immobilization, most of its activity was retained and its half-life at 63o C increased 150-fold. Lactate oxidase was also stabilized when electrostatically complexed with the stronger base poly(ethyleneimine) prior to immobilization. Glycolate oxidase (IP pH 9.6) was not stabilized by poly(N-vinylimidazole) but was stabilized by poly(ethyleneimine) complexing prior to immobilization. The complexed enzyme retained its initial activity upon immobilization, and its half-life at 60 oC also increased 100-fold. The results show that encaging an oxidase in a silica gel can lead either to gain in stability or to loss of activity and that electrostatic complexing is required for stabilization by encapsulation of some, but not all, flavoprotein oxidases.}, author = {Chen, Qiang and Kenausis, Gregory L. and Heller, Adam}, citeulike-article-id = {5805973}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/ja971750k}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/ja971750k}, day = {1}, doi = {10.1021/ja971750k}, journal = {Journal of the American Chemical Society}, keywords = {activity, deactivation, inactivation, pei}, month = {May}, number = {19}, pages = {4582--4585}, posted-at = {2009-09-19 22:50:28}, priority = {2}, title = {Stability of Oxidases Immobilized in Silica Gels}, url = {http://dx.doi.org/10.1021/ja971750k}, volume = {120}, year = {1998} }

TY - JOUR ID - citeulike:5805973 L3 - citeulike-article-id:5805973 N2 - The gain or loss of stability of three flavoprotein oxidases, glucose oxidase, lactate oxidase, and glycolate oxidase, upon immobilization in a hydrated silica gel by a solgel process was quantified. Glucose oxidase (isoelectric point, IP, pH 3.8) retained most or all of its initial activity, while lactate oxidase and glycolate lost most of theirs. The half-life of glucose oxidase at 63 oC increased upon immobilization 200-fold; the half-lives of lactate oxidase and of glycolate oxidase were not extended beyond those of the water-dissolved enzymes. After lactate oxidase (IP pH 4.6) was electrostatically complexed with the weak base poly(N-vinylimidazole) prior to its immobilization, most of its activity was retained and its half-life at 63o C increased 150-fold. Lactate oxidase was also stabilized when electrostatically complexed with the stronger base poly(ethyleneimine) prior to immobilization. Glycolate oxidase (IP pH 9.6) was not stabilized by poly(N-vinylimidazole) but was stabilized by poly(ethyleneimine) complexing prior to immobilization. The complexed enzyme retained its initial activity upon immobilization, and its half-life at 60 oC also increased 100-fold. The results show that encaging an oxidase in a silica gel can lead either to gain in stability or to loss of activity and that electrostatic complexing is required for stabilization by encapsulation of some, but not all, flavoprotein oxidases. IS - 19 JF - Journal of the American Chemical Society EP - 4585 TI - Stability of Oxidases Immobilized in Silica Gels VL - 120 SP - 4582 KW - activity KW - deactivation KW - inactivation KW - pei AU - Chen, Qiang AU - Kenausis, Gregory AU - Heller, Adam PY - 1998/05/01/ UR - http://dx.doi.org/10.1021/ja971750k ER -