Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 421510
Title Laccase-catalyzed modification of PES membranes with 4-hydroxybenzoic acid and gallic acid
Author(s) Nady, N.; Schroën, C.G.P.H.; Franssen, M.C.R.; Mohy Eldin, M.S.; Zuilhof, H.; Boom, R.M.
Source Journal of Membrane Science 394-395 (2012)March. - ISSN 0376-7388 - p. 69 - 79.
Department(s) Food Process Engineering
Laboratory for Organic Chemistry
Publication type Refereed Article in a scientific journal
Publication year 2012
Keyword(s) ultrafiltration membranes - surface modification - fungal laccases - green chemistry - water - ph - purification - adsorption - copolymers - conversion
Abstract We here report on the performance of poly(ethersulfone) membranes modified with 4-hydroxybenzoic acid and gallic acid as substrates, and using laccase as biocatalyst under several modification conditions. The average flux of the base membrane was never reduced more than 20% (mostly below 10% reduction) by modification with 4-hydroxybenzoic acid, and not more than 9% for gallic acid. The mechanical and thermal properties of the membrane were not adversely affected by the modification method. For 4-hydroxybenzoic acid, longer modification times (i.e., hours) and higher substrate concentrations lead to modified membranes with a better protein repellence. The reaction with gallic acid is faster, but less effective in terms of the resulting protein repellence. In conclusion, the laccase-catalyzed modification of poly(ethersulfone) membranes is a mild method with low environmental impact that leads to effective protein repellence while keeping the bulk properties of the base membrane intact. This makes laccase-catalyzed modification an interesting alternative for currently used membrane modification methods.
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