10334-06-2Relevant academic research and scientific papers
In vivo and in vitro hydroxylation of cineole and camphor by cytochromes P450CYP101A1, CYP101B1 and N242A CYP176A1
Stok, Jeanette E.,Hall, Emma A.,Stone, Isobella S.J.,Noble, Margaret C.,Wong, Siew Hoon,Bell, Stephen G.,De Voss, James J.
, p. 52 - 64 (2016)
Cytochromes P450 (P450s) are valuable enzymes that can generate a range of useful compounds via biocatalytic oxidations that complement traditional synthetic chemistry. In this study three bacterial P450s, P450cam (CYP101A1), CYP101B1 and the m
Multiple monohydroxylation products from rac-camphor by marine fungus Botryosphaeria sp. Isolated from marine alga Bostrychia radicans
De Jesus, Hugo C.R.,Jeller, Alex H.,Debonsi, Hosana M.,Alves, Péricles B.,Porto, André L.M.
, p. 498 - 504 (2017/01/24)
This manuscript describes the biooxidation of rac-camphor using whole cells of marine-derived fungus Botryosphaeria sp. CBMAI 1197. The main biotransformation products of this monoterpene were achieved via a hydroxylation reaction and occurred with 5 days of rac-camphor incubation. Products were identified by means of gas chromatography mass spectrometry (GC-MS) and nuclear magnetic resonance (NMR) data. The major hydroxylated products were 6-endo-hydroxycamphor, 6-exo-hydroxycamphor, 5-exo-hydroxycamphor, 5-endo-hydroxycamphor, 3-exo-hydroxycamphor and 8-hydroxycamphor. The 6-exo-hydroxycamphor was obtained through a retro-aldol reaction when 6-endo-hydroxycamphor was maintained in presence of CDCl3; this isomerization was confirmed by 1H NMR and GC-MS data.
