Enzymatic Hydrolysis of Organic Phosphates Adsorbed on Mineral Surfaces
(2012) In Environmental Science & Technology 46. p.285-291- Abstract
- Esters of phosphoric acid constitute a sizable fraction of the total phosphorus supply in the environment and thus play an important role in the global phosphorus cycle. Enzymatic hydrolysis of these esters to produce orthophosphate is often a required reaction preceding phosphorus uptake by plants and microorganisms. Generally, adsorption to environmental particles is assumed to limit this process. Here we show, however, that the rate of enzymatic hydrolysis of glucose-1-phosphate (G1P) adsorbed on goethite by acid phosphatase (AcPase) can be of the same order of magnitude as in aqueous solution. The surface process releases carbon to the solution whereas orthophosphate remains adsorbed on goethite. This hydrolysis reaction is strictly an... (More)
- Esters of phosphoric acid constitute a sizable fraction of the total phosphorus supply in the environment and thus play an important role in the global phosphorus cycle. Enzymatic hydrolysis of these esters to produce orthophosphate is often a required reaction preceding phosphorus uptake by plants and microorganisms. Generally, adsorption to environmental particles is assumed to limit this process. Here we show, however, that the rate of enzymatic hydrolysis of glucose-1-phosphate (G1P) adsorbed on goethite by acid phosphatase (AcPase) can be of the same order of magnitude as in aqueous solution. The surface process releases carbon to the solution whereas orthophosphate remains adsorbed on goethite. This hydrolysis reaction is strictly an interfacial process governed by the properties of the interface. A high surface concentration of substrate mediates the formation of a catalytically active layer of AcPase, and although adsorption likely reduces the catalytic efficiency of the enzyme, this reduction is almost balanced by the fact that enzyme and substrate are concentrated at the mineral surfaces. Our results suggest that mineral surfaces with appropriate surface properties can be very effective in concentrating substrates and enzymes thereby creating microchemical environments of high enzymatic activity. Hence, also strongly adsorbed molecules in soils and aquatic environments may be subjected to biodegradation by extracellular enzymes. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4332272
- author
- Olsson, Rickard ; Giesler, Reiner ; Loring, John S. and Persson, Per LU
- publishing date
- 2012
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Environmental Science & Technology
- volume
- 46
- pages
- 285 - 291
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:84855331270
- pmid:22103404
- ISSN
- 1520-5851
- DOI
- 10.1021/es2028422
- language
- English
- LU publication?
- no
- additional info
- 1
- id
- 38748fed-a181-406e-ae53-a7bc9b3d6aab (old id 4332272)
- date added to LUP
- 2016-04-01 13:05:59
- date last changed
- 2022-04-21 19:45:33
@article{38748fed-a181-406e-ae53-a7bc9b3d6aab,
abstract = {{Esters of phosphoric acid constitute a sizable fraction of the total phosphorus supply in the environment and thus play an important role in the global phosphorus cycle. Enzymatic hydrolysis of these esters to produce orthophosphate is often a required reaction preceding phosphorus uptake by plants and microorganisms. Generally, adsorption to environmental particles is assumed to limit this process. Here we show, however, that the rate of enzymatic hydrolysis of glucose-1-phosphate (G1P) adsorbed on goethite by acid phosphatase (AcPase) can be of the same order of magnitude as in aqueous solution. The surface process releases carbon to the solution whereas orthophosphate remains adsorbed on goethite. This hydrolysis reaction is strictly an interfacial process governed by the properties of the interface. A high surface concentration of substrate mediates the formation of a catalytically active layer of AcPase, and although adsorption likely reduces the catalytic efficiency of the enzyme, this reduction is almost balanced by the fact that enzyme and substrate are concentrated at the mineral surfaces. Our results suggest that mineral surfaces with appropriate surface properties can be very effective in concentrating substrates and enzymes thereby creating microchemical environments of high enzymatic activity. Hence, also strongly adsorbed molecules in soils and aquatic environments may be subjected to biodegradation by extracellular enzymes.}},
author = {{Olsson, Rickard and Giesler, Reiner and Loring, John S. and Persson, Per}},
issn = {{1520-5851}},
language = {{eng}},
pages = {{285--291}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Environmental Science & Technology}},
title = {{Enzymatic Hydrolysis of Organic Phosphates Adsorbed on Mineral Surfaces}},
url = {{http://dx.doi.org/10.1021/es2028422}},
doi = {{10.1021/es2028422}},
volume = {{46}},
year = {{2012}},
}