当前位置： SCI文献检索 > ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS期刊下所有文献 > Covalent immobilization of a halophilic, alkalithermostable lipase LipR2 on Florisil® nanoparticles for production of alkyl levulinates.

Covalent immobilization of a halophilic, alkalithermostable lipase LipR2 on Florisil® nanoparticles for production of alkyl levulinates.

Abstract：

:A novel halophilic, alkalithermostable lipase LipR2 from Alkalispirillum sp. NM-ROO2 was cloned and expressed. LipR2 was covalently immobilized on Florisil® functionalized with glutaraldehyde. Protein binding efficiency of functionalized Florisil® was 94.7%. Immobilized LipR2 retained 97.5% of specific activity of the free enzyme. Free LipR2 has maximal activity at 52 °C, pH 9.3 and 1.9 M NaCl and is resistant to surfactants and organic solvents. Immobilization enhanced LipR2's extreme characteristics, and increased thermostability of LipR2 with the half-life at 50 °C increasing three-fold. Immobilized LipR2 was used as a biocatalyst for esterification of levulinic acid with n-butanol. Under optimal conditions, a 45.9% ester yield was obtained after 12 h. Immobilized LipR2 catalyzed production of ethyl levulinate and 1-dodecyl levulinate with 48.8% and 26.2% ester yields, respectively. When used in repetitive batch esterification, LipR2 retained 69%, 57% and 18.5% of initial activity on esterification of levulinic acid with ethanol, n-butanol and 1-dodecanol, respectively.

journal_name

Arch Biochem Biophys

journal_title

Archives of biochemistry and biophysics

authors

Mesbah NM

doi

10.1016/j.abb.2019.04.004

subject

Has Abstract

pub_date

2019-05-30 00:00:00

pages

22-29

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(19)30142-0

journal_volume

667

pub_type

杂志文章

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