Format

Send to

Choose Destination
J Colloid Interface Sci. 2019 Jun 21;554:296-304. doi: 10.1016/j.jcis.2019.06.071. [Epub ahead of print]

Towards a molecular understanding of the water purification properties of Moringa seed proteins.

Author information

1
Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France; Faculty of Natural Sciences, Keele University, Staffordshire ST5 5BG, UK.
2
Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.
3
Univ. Grenoble Alpes, CEA, Inserm, BGE U1038, F-38000 Grenoble, France.
4
Faculty of Health and Applied Sciences, Namibia University of Science and Technology, Private Bag 13388, 13 Jackson Kaujeua Street, Windhoek, Namibia.
5
Department of Chemistry, University of Botswana, Private Bag UB00704, Gaborone, Botswana.
6
Institut Laue-Langevin, 71 Avenue des Martyrs, 38042 Grenoble Cedex 9, France.
7
Faculty of Natural Sciences, Keele University, Staffordshire ST5 5BG, UK; European Synchrotron Radiation Facility, 71 Avenue des Martyrs, 38043 Grenoble Cedex 9, France.
8
Centre for Neutron Scattering, Uppsala University, Box 516, 75120 Uppsala, Sweden.

Abstract

Seed extracts from Moringa oleifera are of wide interest for use in water purification where they can play an important role in flocculation; they also have potential as anti-microbial agents. Previous work has focused on the crude protein extract. Here we describe the detailed biophysical characterization of individual proteins from these seeds. The results provide new insights relating to the active compounds involved. One fraction, designated Mo-CBP3, has been characterized at a molecular level using a range of biochemical and biophysical techniques including liquid chromatography, X-ray diffraction, mass spectrometry, and neutron reflection. The interfacial behavior is of particular interest in considering water purification applications and interactions with both charged (e.g. silica) and uncharged (alumina) surfaces were studied. The reflection studies show that, in marked contrast to the crude extract, only a single layer of the purified Mo-CBP3 binds to a silica interface and that there is no binding to an alumina interface. These observations are consistent with the crystallographic structure of Mo-CBP3-4, which is one of the main isoforms of the Mo-CBP3 fraction. The results are put in context of previous studies of the properties of the crude extract. This work shows possible routes to development of separation processes that would be based on the specific properties of individual proteins.

KEYWORDS:

Mass spectrometry; Moringa oleifera seeds; Neutron reflectometry; Water treatment; X-ray diffraction

PMID:
31302367
DOI:
10.1016/j.jcis.2019.06.071
Free full text

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center