4.7 Article

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

期刊

JOURNAL OF COLLOID AND INTERFACE SCIENCE
卷 554, 期 -, 页码 296-304

出版社

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jcis.2019.06.071

关键词

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

资金

  1. FRISBI within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-INBS-05-02]
  2. GRAL within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-LABX-49-01]
  3. 'Investissement d'Avenir Infrastructures Nationales en Biologie et Sante' programme (ProFI project)
  4. Swedish Research Council [348-2011-7241]
  5. EPSRC [GR/R99393/01, EP/C015452/1]
  6. EPSRC [EP/C015452/1] Funding Source: UKRI

向作者/读者索取更多资源

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. (C) 2019 The Authors. Published by Elsevier Inc.

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