TY - JOUR
T1 - Enzymatic oxidation of oleuropein and 3-hydroxytyrosol by laccase, peroxidase and tyrosinase
AU - Manzano-Nicolas, Jesus
AU - Taboada-Rodriguez, Amaury
AU - Teruel-Puche, Jose Antonio
AU - Marin-Iniesta, Fulgencio
AU - García-Molina, Francisco
AU - García‐Cánovas, Francisco
AU - Tudela‐Serrano, Jose
AU - Munoz-Munoz, Jose
N1 - Funding information: This work was partially supported by several grants, FEDER RTC-2017-5964-2 InsectFlour project “Aprovechamiento de subproductos industriales agrícolas para la producción de harinas de insectos para consumo humano y animal”/“Exploitation of industrial agronomic by-products to the production of insect flours for human and animal consumption” from Ministerio de Ciencia, Innovacion y Universidades (Madrid, Spain), 20961/PI/18 project from Fundacion Seneca (CARM, Murcia, Spain), and AEIP-15452 project from Murcia University (Murcia, Spain). J. M.-M. has funding from internal grants in Northumbria University.
PY - 2021/8/1
Y1 - 2021/8/1
N2 - The oxidation of oleuropein and 3‐hydroxytyrosol by oxidases laccase, tyrosinase, and peroxidase has been studied. The use of a spectrophotometric method and another spectrophotometric chronometric method has made it possible to determine the kinetic parameters Vmax and KM for each enzyme. The highest binding affinity was shown by laccase. The antioxidant capacities of these two molecules have been characterized, finding a very similar primary antioxidant capacity between them. Docking studies revealed the optimal binding position, which was the same for the two molecules and was a catalytically active position. Practical applications: One of the biggest environmental problems in the food industry comes from olive oil mill wastewater with a quantity of approximately 30 million tons per year worldwide. In addition, olive pomace, the solid residue obtained from the olive oil production, is rich in hydroxytyrosol and oleuropein and the action of enzymatic oxidases can give rise to products in their reactions that can lead to polymerization. This polymerization can have beneficial effects because it can increase the antioxidant capacity with potential application on new functional foods or as feed ingredients. Tyrosinase, peroxidase, and laccase are the enzymes degrading these important polyphenols. The application of a spectrophotometric method for laccase and a chronometric method, for tyrosinase and peroxidase, allowed us to obtain the kinetic information of their reactions on hydroxytyrosol and oleuropein. The kinetic information obtained could advance in the understanding of the mechanism of these important industrial enzymes.
AB - The oxidation of oleuropein and 3‐hydroxytyrosol by oxidases laccase, tyrosinase, and peroxidase has been studied. The use of a spectrophotometric method and another spectrophotometric chronometric method has made it possible to determine the kinetic parameters Vmax and KM for each enzyme. The highest binding affinity was shown by laccase. The antioxidant capacities of these two molecules have been characterized, finding a very similar primary antioxidant capacity between them. Docking studies revealed the optimal binding position, which was the same for the two molecules and was a catalytically active position. Practical applications: One of the biggest environmental problems in the food industry comes from olive oil mill wastewater with a quantity of approximately 30 million tons per year worldwide. In addition, olive pomace, the solid residue obtained from the olive oil production, is rich in hydroxytyrosol and oleuropein and the action of enzymatic oxidases can give rise to products in their reactions that can lead to polymerization. This polymerization can have beneficial effects because it can increase the antioxidant capacity with potential application on new functional foods or as feed ingredients. Tyrosinase, peroxidase, and laccase are the enzymes degrading these important polyphenols. The application of a spectrophotometric method for laccase and a chronometric method, for tyrosinase and peroxidase, allowed us to obtain the kinetic information of their reactions on hydroxytyrosol and oleuropein. The kinetic information obtained could advance in the understanding of the mechanism of these important industrial enzymes.
KW - 3-hydroxytyrosol
KW - laccase
KW - oleuropein
KW - peroxidase
KW - tyrosinase
UR - http://www.scopus.com/inward/record.url?scp=85109080174&partnerID=8YFLogxK
U2 - 10.1111/jfbc.13803
DO - 10.1111/jfbc.13803
M3 - Article
SN - 0145-8884
VL - 45
SP - 1
EP - 14
JO - Journal of Food Biochemistry
JF - Journal of Food Biochemistry
IS - 8
M1 - e13803
ER -