Immobilization of bacterial feruloyl esterase on mesoporous silica particles and enhancement of synthetic activity by hydrophobic-modified surface
Journal article, 2019

Here, we demonstrated the immobilization of bacterial feruloyl esterase (FAE) from Butyrivibrio sp. XPD2006, Lactobacillus crispatus, Butyrivibrio sp. AE2015, Ruminococcus albus, Cellulosilyticum ruminicola and Clostridium cellulovorans on SBA-15 and their ability to synthesize butyl ferulate (BFA). The BFae2 from Butyrivibrio sp. XPD2006 showed the best catalytic efficiency. High BFA yield was produced when the immobilization of BFae2 took place with a high protein loading and narrow pore sized SBA-15, suggesting alteration of enzyme behavior due to the crowding environment in SBA-15. Grafting of SBA-15 with octyl moieties led to shrinking pore size and resulted in 2.5-fold increment of BFA activity compared to the free enzyme and 70%mol BFA was achieved. The BFae2 encapsulated in hydrophobic-modified SBA-15 endured up to seven reaction cycles while the BFA activity remained above 60%. This is the first report showing the superior performance of hydrophobic-modified surface to entrap FAE to produce fatty phenolic esters.

SBA-15

Protein loading

Butyl ferulate

Pore size

Transesterification

Author

Sun-Li Chong

Chalmers, Biology and Biological Engineering, Industrial Biotechnology

Zhejiang Agriculture and Forestry University

Vânia Cardoso

University of Lisbon

Nzytech Lda

Joana L.A. Brás

Nzytech Lda

Milene Zezzi Do Valle Gomes

Chalmers, Chemistry and Chemical Engineering, Applied Chemistry, Applied Surface Chemistry

Carlos M.G.A. Fontes

Nzytech Lda

University of Lisbon

Lisbeth Olsson

Chalmers, Biology and Biological Engineering, Industrial Biotechnology

Bioresource Technology

0960-8524 (ISSN)

Vol. 293 122009

Subject Categories

Biochemistry and Molecular Biology

Biocatalysis and Enzyme Technology

Organic Chemistry

DOI

10.1016/j.biortech.2019.122009

PubMed

31493730

More information

Latest update

11/13/2019