Characteristics of NtCCD1-3 from tobacco, and protein engineering of the CCD1 to enhance ß -ionone production in yeast.
Front Microbiol
; 13: 1011297, 2022.
Article
en En
| MEDLINE
| ID: mdl-36212872
Biosynthesis of ß-ionone by microbial cell factories has become a promising way to obtain natural ß-ionone. The catalytic activity of carotenoid cleavage dioxygenase 1 (CCD1) in cleavage of ß-carotene to ß-ionone severely limits its biosynthesis. In this study, NtCCD1-3 from Nicotiana tabacum with high ability to cleave ß-carotene was screened. Multiple strategies for improving the ß-ionone yield in Saccharomyces cerevisiae were performed. The results showed that NtCCD1-3 could cleave a variety of caroteniods at the 9,10 (9',10') double bonds and lycopene at the 5,6 (5',6') positions. The insertion site delta for NtCCD1-3 gene was more suitable for enhancing the yield of ß-ionone, showing 19.1-fold increase compared with the rox1 site. More importantly, mutant K38A of NtCCD1-3 in membrane-bonding domains could greatly promote ß-ionone production by more than 3-fold. We also found that overexpression of the NADH kinase Pos5 could improve ß-ionone yield up to 1.5 times. These results may provide valuable references for biosynthesis of ß-ionone.
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1
Colección:
01-internacional
Base de datos:
MEDLINE
Idioma:
En
Revista:
Front Microbiol
Año:
2022
Tipo del documento:
Article
País de afiliación:
China
Pais de publicación:
Suiza