» Articles » PMID: 35740077

Molecular Properties of β-Carotene Oxygenases and Their Potential in Industrial Production of Vitamin A and Its Derivatives

Overview
Date 2022 Jun 24
PMID 35740077
Authors
Affiliations
Soon will be listed here.
Abstract

β-Carotene 15,15'-oxygenase (BCO1) and β-carotene 9',10'-oxygenase (BCO2) are potential producers of vitamin A derivatives, since they can catalyze the oxidative cleavage of dietary provitamin A carotenoids to retinoids and derivative such as apocarotenal. Retinoids are a class of chemical compounds that are vitamers of vitamin A or are chemically related to it, and are essential nutrients for humans and highly valuable in the food and cosmetics industries. β-carotene oxygenases (BCOs) from various organisms have been overexpressed in heterogeneous bacteria, such as , and their biochemical properties have been studied. For the industrial production of retinal, there is a need for increased production of a retinal producer and biosynthesis of retinal using biocatalyst systems improved by enzyme engineering. The current review aims to discuss BCOs from animal, plants, and bacteria, and to elaborate on the recent progress in our understanding of their functions, biochemical properties, substrate specificity, and enzyme activities with respect to the production of retinoids in whole-cell conditions. Moreover, we specifically propose ways to integrate BCOs into retinal biosynthetic bacterial systems to improve the performance of retinal production.

Citing Articles

Concurrent Production of α- and β-Carotenes with Different Stoichiometries Displaying Diverse Antioxidative Activities via Lycopene Cyclases-Based Rational System.

Luo H, He W, Dai Z, Zhang Z, Bao Y, Li D Antioxidants (Basel). 2022; 11(11).

PMID: 36421453 PMC: 9686992. DOI: 10.3390/antiox11112267.

References
1.
Keeble A, Howarth M . Power to the protein: enhancing and combining activities using the Spy toolbox. Chem Sci. 2021; 11(28):7281-7291. PMC: 7844731. DOI: 10.1039/d0sc01878c. View

2.
Sui X, Kiser P, von Lintig J, Palczewski K . Structural basis of carotenoid cleavage: from bacteria to mammals. Arch Biochem Biophys. 2013; 539(2):203-13. PMC: 3818509. DOI: 10.1016/j.abb.2013.06.012. View

3.
Xu X, Tian L, Tang S, Xie C, Xu J, Jiang L . Design and tailoring of an artificial DNA scaffolding system for efficient lycopene synthesis using zinc-finger-guided assembly. J Ind Microbiol Biotechnol. 2019; 47(2):209-222. DOI: 10.1007/s10295-019-02255-6. View

4.
Daruwalla A, Zhang J, Lee H, Khadka N, Farquhar E, Shi W . Structural basis for carotenoid cleavage by an archaeal carotenoid dioxygenase. Proc Natl Acad Sci U S A. 2020; 117(33):19914-19925. PMC: 7443882. DOI: 10.1073/pnas.2004116117. View

5.
Kiefer C, Hessel S, Lampert J, Vogt K, Lederer M, Breithaupt D . Identification and characterization of a mammalian enzyme catalyzing the asymmetric oxidative cleavage of provitamin A. J Biol Chem. 2001; 276(17):14110-6. DOI: 10.1074/jbc.M011510200. View