dc.creator | Quintero Quiroz, Julián | |
dc.creator | Rojas Camargo, John Jairo | |
dc.date | 2020-10-26T16:35:23Z | |
dc.date | 2020-10-26T16:35:23Z | |
dc.date | 2018 | |
dc.date.accessioned | 2023-08-28T20:14:23Z | |
dc.date.available | 2023-08-28T20:14:23Z | |
dc.identifier | 0121-4004 | |
dc.identifier | http://hdl.handle.net/10495/17076 | |
dc.identifier | 10.17533/udea.vitae.v25n1a01 | |
dc.identifier | 2145-2660 | |
dc.identifier.uri | https://repositorioslatinoamericanos.uchile.cl/handle/2250/8475985 | |
dc.description | ABSTRACT: Proteins are macromolecules exhibiting amphiphilic properties, good biocompatibility, biodegradability, high nutritional value, and show strong interactions with several types of active compounds via hydrogen
bonding and electrostatic interactions (1). These plant or animal-derived macromolecules differ in their
molecular size depending on the number of amino acids present in their structure, which in turn, are linked
by peptide bonds between the carbonyl (-CO-) and amino groups (-NH) (2). This amino acid sequence
has its particular three-dimensional or folded organization, which provides each protein with (i) technofunctional characteristics (i.e., gelling, emulsifying, coagulating and encapsulating capabilities, softener,
adsorbents, etc); (ii) biological (i.e., nutritional value, transport, and other enzymatic functions); and (iii)
bioactive (i.e., antioxidant, antimicrobial, anticoagulant or anti-inflammatory activities) characteristics,
which are essential in the pharmaceutical and food fields (3). Another factor that affects the functional
characteristics of proteins is their source. Thus, proteins derived from vegetable sources are larger, less
flexible, and less soluble in extreme pH ranges. Further, they have a globular conformation with more
hydrophobic groups hidden within the molecular structure as compared to the animal counterparts
(4). However, animal-derived proteins are the most widely used due to their easy processing and water
solubility. In order to match those characteristics vegetable proteins can be functionalized, making them
more biodegradable and biocompatible. Moreover, they are renewable, highly available, their productions
implies less natural resources, and are considered as “environmentally economical” | |
dc.format | 2 | |
dc.format | application/pdf | |
dc.format | application/pdf | |
dc.language | spa | |
dc.publisher | Universidad de Antioquia, Facultad de Ciencias Farmacéuticas y Alimentarias | |
dc.publisher | Medellín, Colombia | |
dc.relation | Vitae | |
dc.rights | Atribución-NoComercial-CompartirIgual 2.5 Colombia (CC BY-NC-SA 2.5 CO) | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/co/ | |
dc.rights | http://purl.org/coar/access_right/c_abf2 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/4.0/ | |
dc.subject | Proteínas vegetales | |
dc.subject | Plant proteins | |
dc.subject | Editorial | |
dc.subject | Macromoleculas | |
dc.subject | Macromolecules | |
dc.title | Proteins Functionalization : a Strategy that Boost the Performance of these Macromolecules for Innovative Pharmaceutical and Food Developments | |
dc.type | info:eu-repo/semantics/contributionToPeriodical | |
dc.type | info:eu-repo/semantics/publishedVersion | |
dc.type | http://purl.org/coar/resource_type/c_b239 | |
dc.type | https://purl.org/redcol/resource_type/ARTEDIT | |
dc.type | Editorial | |