Peptides with biological and technofunctional properties produced by bromelain hydrolysis of proteins from different sources: A review.


Journal

International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578

Informations de publication

Date de publication:
31 Dec 2023
Historique:
received: 31 08 2023
revised: 02 10 2023
accepted: 02 10 2023
medline: 24 11 2023
pubmed: 9 10 2023
entrez: 8 10 2023
Statut: ppublish

Résumé

Bromelains are cysteine peptidases with endopeptidase action (a subfamily of papains), obtained from different parts of vegetable belonging to the Bromeliaceae family. They have some intrinsic medical activity, but this review is focused on their application (individually or mixed with other proteases) to produce bioactive peptides. When compared to other proteases, perhaps due to the fact that they are commercialized as an extract containing several proteases, the hydrolysates produced by this enzyme tends to have higher bioactivities than other common proteases. The peptides and the intensity of their final properties depend on the substrate protein and reaction conditions, being the degree of hydrolysis a determining parameter (but not always positive or negative). The produced peptides may have diverse activities such as antioxidant, antitumoral, antihypertensive or antimicrobial ones, among others or they may be utilized to improve the organoleptic properties of foods and feeds. Evolution of the use of this enzyme in this application is proposed to be based on a more intense direct application of Bromeliaceae extract, without the cost associated to enzyme purification, and the use of immobilized biocatalysts of the enzyme by simplifying the enzyme recovery and reuse, and also making the sequential hydrolysis using diverse proteases possible.

Identifiants

pubmed: 37806416
pii: S0141-8130(23)04141-7
doi: 10.1016/j.ijbiomac.2023.127244
pii:
doi:

Substances chimiques

Bromelains 9001-00-7
Peptides 0
Peptide Hydrolases EC 3.4.-
Endopeptidases EC 3.4.-
Protein Hydrolysates 0

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

127244

Informations de copyright

Copyright © 2023 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Veymar G Tacias-Pascacio (VG)

Facultad de Ciencias de la Nutrición y Alimentos, Universidad de Ciencias y Artes de Chiapas, Lib. Norte Pte. 1150, 29039 Tuxtla Gutiérrez, Chiapas, Mexico.

Daniel Castañeda-Valbuena (D)

Facultad de Ciencias de la Nutrición y Alimentos, Universidad de Ciencias y Artes de Chiapas, Lib. Norte Pte. 1150, 29039 Tuxtla Gutiérrez, Chiapas, Mexico.

Olga Tavano (O)

Faculty of Nutrition, Alfenas Federal Univ., 700 Gabriel Monteiro da Silva St, Alfenas, MG 37130-000, Brazil.

Ángel Berenguer Murcia (ÁB)

Departamento de Química Inorgánica e Instituto Universitario de Materiales, Universidad de Alicante, Alicante, Spain.

Beatriz Torrestina-Sánchez (B)

Tecnológico Nacional De México/IT-Veracruz, Av. M. A. De Quevedo # 2779, Veracruz 91897, Mexico. Electronic address: beatriz.ts@veracruz.tecnm.mx.

Roberto Fernandez-Lafuente (R)

Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, Madrid, Spain. Electronic address: rfl@icp.csic.es.

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Classifications MeSH