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

Sun Li Chong; Vânia Cardoso; Joana L A Brás; Milene Zezzi do Valle Gomes; Carlos M G A Fontes; Lisbeth Olsson

doi:10.1016/j.biortech.2019.122009

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

Bioresour Technol. 2019 Dec:293:122009. doi: 10.1016/j.biortech.2019.122009. Epub 2019 Aug 14.

Authors

Sun Li Chong¹, Vânia Cardoso², Joana L A Brás³, Milene Zezzi do Valle Gomes⁴, Carlos M G A Fontes², Lisbeth Olsson⁵

Affiliations

¹ State Key Laboratory of Subtropical Silviculture, Zhejiang A&F University, Lin'an, 311300 Hangzhou, China; Chalmers University of Technology, Department of Biology and Biological Engineering, Division of Industrial Biotechnology, Kemivägen 10, SE-412 96 Göteborg, Sweden.
² NZYTech Genes & Enzymes, Campus do Lumiar, 1649-038 Lisbon, Portugal; CIISA - Faculty of Veterinary Medicine, University of Lisbon, 1300-477 Lisboa, Portugal.
³ NZYTech Genes & Enzymes, Campus do Lumiar, 1649-038 Lisbon, Portugal.
⁴ Chalmers University of Technology, Department of Chemistry and Chemical Engineering, Applied Chemistry, SE 412 96 Gothenburg, Sweden.
⁵ Chalmers University of Technology, Department of Biology and Biological Engineering, Division of Industrial Biotechnology, Kemivägen 10, SE-412 96 Göteborg, Sweden. Electronic address: lisbeth.olsson@chalmers.se.

PMID: 31493730
DOI: 10.1016/j.biortech.2019.122009

Abstract

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.

Keywords: Butyl ferulate; Pore size; Protein loading; SBA-15; Transesterification.

MeSH terms

Carboxylic Ester Hydrolases*
Catalysis
Hydrophobic and Hydrophilic Interactions
Silicon Dioxide*

Substances

Silicon Dioxide
Carboxylic Ester Hydrolases
feruloyl esterase