Engineering polyelectrolyte multilayer coatings as a strategy to optimize enzyme immobilization on a membrane support

Andrei Popkov; Ziran Su; Sigyn Björk Sigurdardóttir; Jianquan Luo; Magdalena Malankowska; Manuel Pinelo

doi:10.1016/j.bej.2023.108838

Engineering polyelectrolyte multilayer coatings as a strategy to optimize enzyme immobilization on a membrane support

Andrei Popkov, Ziran Su, Sigyn Björk Sigurdardóttir, Jianquan Luo, Magdalena Malankowska, Manuel Pinelo^*

^*Corresponding author for this work

Chinese Academy of Sciences

Research output: Contribution to journal › Journal article › Research › peer-review

53 Downloads (Pure)

Abstract

This study presents a systematic design of a biocatalytic membrane reactor, where we combined physical adsorption and chemical conjugation of Alcohol Dehydrogenase (ADH) in a novel type of polyelectrolyte (PE) layer-by-layer (LbL) assembly system. The hybrid LbL structure is proposed as a strategy to simultaneously advance activity and operational stability of enzymes immobilized on a membrane surface. Using poly(allylamine hydrochloride) (PAH) and poly(methacrylic acid) sodium salt (PMAA) allowed functionalization of polysulfone (Psf) membrane for subsequent ADH immobilization with no resistance to substrate mass transfer and no decrease in water permeability (WP) (56.5±8.8 Lm⁻²h ⁻¹bar⁻¹) compared to the pristine membrane (50.8±1.7 Lm⁻²h⁻¹bar⁻¹). Tailoring membrane surface chemistry, enzyme concentration, time, and pH during the adsorption step allowed to increase specific activity of the biocatalytic membrane from 1.13±0.18 mU/cm² for immobilization on the pristine membrane to 4.09±0.53 mU/cm² for immobilization on a PAH-modified coating. Conjugation of adsorbed ADH with PMAA layer improved reusability compared to the non-conjugated membrane (by retaining 73.4±3.2% of the starting activity on the third conversion run against 58.7±2.4%) and shifted pH optimum by 1 unit compared to the free ADH. The presented approach of LbL assembly synthesis provides a potential foundation for engineering of biocatalytic nanoscale reactors.

Original language	English
Article number	108838
Journal	Biochemical Engineering Journal
Volume	193
Number of pages	10
ISSN	1369-703X
DOIs	https://doi.org/10.1016/j.bej.2023.108838
Publication status	Published - 2023

Keywords

LbL assembly
Enzyme immobilization
Membrane modification
Polyelectrolytes

Access to Document

10.1016/j.bej.2023.108838Licence: CC BY

FulltextFinal published version, 6.09 MBLicence: CC BY

OpenUrl availability

Full text

Cite this

@article{4485bd3eb3fd43ef8c0c80660320338e,

title = "Engineering polyelectrolyte multilayer coatings as a strategy to optimize enzyme immobilization on a membrane support",

abstract = "This study presents a systematic design of a biocatalytic membrane reactor, where we combined physical adsorption and chemical conjugation of Alcohol Dehydrogenase (ADH) in a novel type of polyelectrolyte (PE) layer-by-layer (LbL) assembly system. The hybrid LbL structure is proposed as a strategy to simultaneously advance activity and operational stability of enzymes immobilized on a membrane surface. Using poly(allylamine hydrochloride) (PAH) and poly(methacrylic acid) sodium salt (PMAA) allowed functionalization of polysulfone (Psf) membrane for subsequent ADH immobilization with no resistance to substrate mass transfer and no decrease in water permeability (WP) (56.5±8.8 Lm−2h −1bar−1) compared to the pristine membrane (50.8±1.7 Lm−2h−1bar−1). Tailoring membrane surface chemistry, enzyme concentration, time, and pH during the adsorption step allowed to increase specific activity of the biocatalytic membrane from 1.13±0.18 mU/cm2 for immobilization on the pristine membrane to 4.09±0.53 mU/cm2 for immobilization on a PAH-modified coating. Conjugation of adsorbed ADH with PMAA layer improved reusability compared to the non-conjugated membrane (by retaining 73.4±3.2% of the starting activity on the third conversion run against 58.7±2.4%) and shifted pH optimum by 1 unit compared to the free ADH. The presented approach of LbL assembly synthesis provides a potential foundation for engineering of biocatalytic nanoscale reactors.",

keywords = "LbL assembly, Enzyme immobilization, Membrane modification, Polyelectrolytes",

author = "Andrei Popkov and Ziran Su and Sigurdard{\'o}ttir, {Sigyn Bj{\"o}rk} and Jianquan Luo and Magdalena Malankowska and Manuel Pinelo",

year = "2023",

doi = "10.1016/j.bej.2023.108838",

language = "English",

volume = "193",

journal = "Biochemical Engineering Journal",

issn = "1369-703X",

publisher = "Elsevier",

}

TY - JOUR

T1 - Engineering polyelectrolyte multilayer coatings as a strategy to optimize enzyme immobilization on a membrane support

AU - Popkov, Andrei

AU - Su, Ziran

AU - Sigurdardóttir, Sigyn Björk

AU - Luo, Jianquan

AU - Malankowska, Magdalena

AU - Pinelo, Manuel

PY - 2023

Y1 - 2023

N2 - This study presents a systematic design of a biocatalytic membrane reactor, where we combined physical adsorption and chemical conjugation of Alcohol Dehydrogenase (ADH) in a novel type of polyelectrolyte (PE) layer-by-layer (LbL) assembly system. The hybrid LbL structure is proposed as a strategy to simultaneously advance activity and operational stability of enzymes immobilized on a membrane surface. Using poly(allylamine hydrochloride) (PAH) and poly(methacrylic acid) sodium salt (PMAA) allowed functionalization of polysulfone (Psf) membrane for subsequent ADH immobilization with no resistance to substrate mass transfer and no decrease in water permeability (WP) (56.5±8.8 Lm−2h −1bar−1) compared to the pristine membrane (50.8±1.7 Lm−2h−1bar−1). Tailoring membrane surface chemistry, enzyme concentration, time, and pH during the adsorption step allowed to increase specific activity of the biocatalytic membrane from 1.13±0.18 mU/cm2 for immobilization on the pristine membrane to 4.09±0.53 mU/cm2 for immobilization on a PAH-modified coating. Conjugation of adsorbed ADH with PMAA layer improved reusability compared to the non-conjugated membrane (by retaining 73.4±3.2% of the starting activity on the third conversion run against 58.7±2.4%) and shifted pH optimum by 1 unit compared to the free ADH. The presented approach of LbL assembly synthesis provides a potential foundation for engineering of biocatalytic nanoscale reactors.

AB - This study presents a systematic design of a biocatalytic membrane reactor, where we combined physical adsorption and chemical conjugation of Alcohol Dehydrogenase (ADH) in a novel type of polyelectrolyte (PE) layer-by-layer (LbL) assembly system. The hybrid LbL structure is proposed as a strategy to simultaneously advance activity and operational stability of enzymes immobilized on a membrane surface. Using poly(allylamine hydrochloride) (PAH) and poly(methacrylic acid) sodium salt (PMAA) allowed functionalization of polysulfone (Psf) membrane for subsequent ADH immobilization with no resistance to substrate mass transfer and no decrease in water permeability (WP) (56.5±8.8 Lm−2h −1bar−1) compared to the pristine membrane (50.8±1.7 Lm−2h−1bar−1). Tailoring membrane surface chemistry, enzyme concentration, time, and pH during the adsorption step allowed to increase specific activity of the biocatalytic membrane from 1.13±0.18 mU/cm2 for immobilization on the pristine membrane to 4.09±0.53 mU/cm2 for immobilization on a PAH-modified coating. Conjugation of adsorbed ADH with PMAA layer improved reusability compared to the non-conjugated membrane (by retaining 73.4±3.2% of the starting activity on the third conversion run against 58.7±2.4%) and shifted pH optimum by 1 unit compared to the free ADH. The presented approach of LbL assembly synthesis provides a potential foundation for engineering of biocatalytic nanoscale reactors.

KW - LbL assembly

KW - Enzyme immobilization

KW - Membrane modification

KW - Polyelectrolytes

U2 - 10.1016/j.bej.2023.108838

DO - 10.1016/j.bej.2023.108838

M3 - Journal article

SN - 1369-703X

VL - 193

JO - Biochemical Engineering Journal

JF - Biochemical Engineering Journal

M1 - 108838

ER -

Engineering polyelectrolyte multilayer coatings as a strategy to optimize enzyme immobilization on a membrane support

Abstract

Keywords

Access to Document

OpenUrl availability

Fingerprint

Cite this