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  • Activity enhancement and stabilization of lipase from Pseudomonas cepacia in polyallylamine-mediated biomimetic silica.

Activity enhancement and stabilization of lipase from Pseudomonas cepacia in polyallylamine-mediated biomimetic silica.

Biotechnology letters (2010-11-04)
Guan-Chun Chen, I-Ching Kuan, Jian-Ren Hong, Bing-Hong Tsai, Shiow-Ling Lee, Chi-Yang Yu
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Lipase from Aspergillus oryzae, lyophilized, powder, white, ~50 U/mg
Sigma-Aldrich
Lipase from Candida rugosa, lyophilized, powder (fine), 15-25 U/mg
Sigma-Aldrich
Lipase from Aspergillus niger, powder (fine), ~200 U/g
Sigma-Aldrich
Lipase, immobilized on Immobead 150 from Pseudomonas cepacia, ≥900 U/g