Activity enhancement and stabilization of lipase from Pseudomonas cepacia in polyallylamine-mediated biomimetic silica.
Triacylglycerol lipase from Pseudomonas cepacia and Fe(3)O(4) magnetic nanoparticles were encapsulated simultaneously within biomimetic silica through the catalysis of polyallylamine. The encapsulation efficiency reached 96% with an activity recovery of 51%. After 5 h at 37°C, the activities of the free and encapsulated lipases decreased by 77 and 16%, respectively. Addition of 10 and 15 mol% trimethylmethoxysilane to tetramethoxysilane during encapsulation doubled the lipase activity while inclusion of 50 and 60 mol% γ-(methacryloxypropyl)-trimethoxysilane tripled the activity. Thus, such encapsulation not only stabilized P. cepacia lipase but also could enhance the activity by varying silane additives.
Department of Bioengineering, Tatung University, 40 Chungshan N. Rd. Sec. 3, Taipei, 10452, Taiwan.
Guan-Chun
GC
Chen
I-Ching
IC
Kuan
Jian-Ren
JR
Hong
Bing-Hong
BH
Tsai
Shiow-Ling
SL
Lee
Chi-Yang
CY
Yu
D032701:Biomimetics; D016956:Burkholderia cepacia / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D011073:Polyamines / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*; D013696:Temperature
D011073:Polyamines; C063994:polyallylamine; D012822:Silicon Dioxide; D008049:Lipase