Actinidin: A Review from Molecular Mechanisms to Biotechnological Applications
6 affiliations
- 1Facultad de Ciencias de la Nutrición y Alimentos, Universidad de Ciencias y Artes de Chiapas, Tuxtla Gutiérrez 29050, Chiapas, Mexico
- 2Facultad de Nutrición, Universidad Pablo Guardado Chávez, Libramiento Nte. Ote. 3450, Amp las Palmas, Tuxtla Gutiérrez 29040, Chiapas, Mexico
- 3Faculty of Nutrition, Alfenas Federal University, 700 Gabriel Monteiro da Silva St., Alfenas 37130-000, MG, Brazil
- 4Departamento de Química Inorgánica, Instituto Universitario de Materiales, Universidad de Alicante, 03690 Alicante, Spain
- 5Departamento de Biocatálisis, ICP-CSIC, Campus UAM-CSIC, 28049 Madrid, Spain
- 6Transformation and Food Product Elaboration Laboratory, Nutrition and Food Technology Institute (INATAA), University of Brothers Mentouri Constantine 1, Constantine 25017, Algeria
Abstract
Actinidin is a cysteine protease recognized as the predominant protease in kiwifruit. It possesses distinctive catalytic and structural properties that determine its specificity and behavior with different substrates. This, along with its plant origin, has made it one of the most prominent plant-derived proteases. This review offers a comprehensive overview of the available knowledge on this enzyme, addressing its molecular and biochemical characteristics, its production, extraction, purification, and technological optimization. The main biotechnological applications of actinidin are also presented and discussed, with particular emphasis on its use in the processing of food proteins in diverse matrices such as meat, milk, and gluten proteins, its role in digestion, and its antigenic relevance. The available information suggests that actinidin is effective in the hydrolysis of multiple proteins, but its activity clearly depends on the substrate and reaction conditions, which explains its advantages and limitations compared to other enzymes. The diverse range of studies conducted on actinidin reflects the versatility of this enzyme. However, compared with other proteases, relatively few studies have investigated its immobilization or its application in the production of bioactive peptides. Thus, there are significant technological and academic gaps and a need for further studies on actinidin so that its catalytic properties may be fully understood and exploited, on par with other proteases such as papain and bromelain.
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BibTeX
@article{castanedavalbuena2026actinidin,
title = {{Actinidin: A Review from Molecular Mechanisms to Biotechnological Applications}},
author = {Daniel Castañeda-Valbuena and Olga Tavano and Ángel Berenguer-Murcia and Pedro Abellanas-Perez and El Hocine Siar and Roberto Fernandez-Lafuente and Veymar G. Tacias-Pascacio},
journal = {Catalysts},
year = {2026},
month = oct,
doi = {10.3390/catal16110936},
url = {https://www.mdpi.com/2073-4344/16/11/936},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - Actinidin: A Review from Molecular Mechanisms to Biotechnological Applications
AU - Daniel Castañeda-Valbuena
AU - Olga Tavano
AU - Ángel Berenguer-Murcia
AU - Pedro Abellanas-Perez
AU - El Hocine Siar
AU - Roberto Fernandez-Lafuente
AU - Veymar G. Tacias-Pascacio
PY - 2026
DA - 2026/10/22
JO - Catalysts
DO - 10.3390/catal16110936
UR - https://www.mdpi.com/2073-4344/16/11/936
AB - Actinidin is a cysteine protease recognized as the predominant protease in kiwifruit. It possesses distinctive catalytic and structural properties that determine its specificity and behavior with different substrates. This, along with its plant origin, has made it one of the most prominent plant-derived proteases. This review offers a comprehensive overview of the available knowledge on this enzyme, addressing its molecular and biochemical characteristics, its production, extraction, purification, and technological optimization. The main biotechnological applications of actinidin are also presented and discussed, with particular emphasis on its use in the processing of food proteins in diverse matrices such as meat, milk, and gluten proteins, its role in digestion, and its antigenic relevance. The available information suggests that actinidin is effective in the hydrolysis of multiple proteins, but its activity clearly depends on the substrate and reaction conditions, which explains its advantages and limitations compared to other enzymes. The diverse range of studies conducted on actinidin reflects the versatility of this enzyme. However, compared with other proteases, relatively few studies have investigated its immobilization or its application in the production of bioactive peptides. Thus, there are significant technological and academic gaps and a need for further studies on actinidin so that its catalytic properties may be fully understood and exploited, on par with other proteases such as papain and bromelain.
SN - 2073-4344
ER -