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Protein characterisation of Brosimum gaudichaudii Trécul latex and study of nanostructured latex film formation
Author(s) -
Barbosa Eduardo F.,
MongeFuentes Victoria,
Oliveira Natiela B.,
Tavares Rebecca,
Xavier MaryAnn E.,
Bemquerer Marcelo Porto,
Silva Luciano P.
Publication year - 2014
Publication title -
iet nanobiotechnology
Language(s) - English
Resource type - Journals
ISSN - 1751-875X
DOI - 10.1049/iet-nbt.2013.0042
Subject(s) - trypsin inhibitor , chemistry , amino acid residue , trypsin , residue (chemistry) , biochemistry , enzyme , peptide sequence , gene
Brosimum gaudichaudii Tréc. (Moraceae) is a common Brazilian Cerrado plant known by its pharmaceutical industry relevance. The authors investigated the latex protein components and potential biotechnological applications. Some protein fragments had their sequences elucidated, presenting similarities to jacalin and Kunitz‐type trypsin inhibitors. Amino acid residue modifications were found, such as glutamine N ‐terminal residue cyclisation into pyroglutamic acid residue, and mass differences corresponding to hexoses and N ‐acetylhexosamine presence. The latex was used to produce a nanoscale structured film, which presented an increased attraction and reduced adhesion behaviours. The film presented high homogeneity, as observed by low nanoroughness values, probably because of its intrinsic components, such as the jacalin‐like protein that has known agglutination properties. The immobilised Kunitz‐type trypsin inhibitor presence in the latex film allow us to point out to applications related to this inhibition, as in active food packaging, since these peptidase inhibitors are able to inhibit pests and microorganism proliferation.

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