当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Lipase immobilization on synthesized hyaluronic acid-coated magnetic nanoparticle-functionalized graphene oxide composites as new biocatalysts: Improved reusability, stability, and activity.

Lipase immobilization on synthesized hyaluronic acid-coated magnetic nanoparticle-functionalized graphene oxide composites as new biocatalysts: Improved reusability, stability, and activity.

Abstract：

BACKGROUND:Lipase is an enzyme that catalyzes the hydrolysis of lipids in watery and organic interactions they can catalyze synthetic reactions, involving inter esterification among triglycerides and alcohols to produce glycerin and fatty acids. The recovery of soluble lipase is not possible which makes this assay method expensive. METHODS:The current study efforts on the development of the stability of a lipase B Candida antarctica as Cross-Linked Enzyme Aggregates (CLEAs). Then the graphene oxide nanoparticles (GO-MNPs) were prepared, different conditions such as temperature, pH, storage stability, reusability, and organic solvents were used to compare the free lipase and lipase-GO-MNPs-CLEAs activities. Different techniques were used to analyze the preparation compounds. RESULTS:The saturated ammonium sulfate (55%) and cross-linked with 125 mM glutaraldehyde for 10 h at 4 °C were found to optimization the synthesis of lipase-GO-MNPs-CLEAs with the maximum activity recovery of 96.5%. Storage stability significantly developed for the lipase-GO-MNPs-CLEAs comparing to the free lipase. CONCLUSIONS:The current study for the first time modified the MNPs by using hyaluronic acid (HA) which improved the stability and nano-biocatalytic performance in conditions into the solvent and temperature which will have a significant influence on the improvement of bio catalytic systems in the industrial applications.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Atiroğlu V

doi

10.1016/j.ijbiomac.2019.12.233

subject

Has Abstract

pub_date

2020-02-15 00:00:00

pages

456-465

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(19)39397-3

journal_volume

145

pub_type

杂志文章

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