Abstract
Objective
To investigate the biocatalytic potential of Colletotrichum acutatum and Colletotrichum nymphaeae for monoterpene biotransformation.
Results
C. acutatum and C. nymphaeae used limonene, α-pinene, β-pinene, farnesene, citronellol, linalool, geraniol, perillyl alcohol, and carveol as sole carbon and energy sources. Both species biotransformed limonene and linalool, accumulating limonene-1,2-diol and linalool oxides, respectively. α-Pinene was only biotransformed by C. nymphaeae producing campholenic aldehyde, pinanone and verbenone. The biotransformation of limonene by C. nymphaeae yielded 3.34–4.01 g limonene-1,2-diol l−1, depending on the substrate (R-(+)-limonene, S-(−)-limonene or citrus terpene (an agro-industrial by-product). This is among the highest concentrations already reported for this product.
Conclusions
This is the first report on the biotransformation of these terpenes by Colletotrichum spp. and the biotransformation of limonene to limonene-1,2-diol possibly involves enzymes similar to those found in Grosmannia clavigera.
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Acknowledgements
The authors acknowledge the Citriculture Defense Fund and Brazilian Collection of Environmental and Industrial Microorganisms for the stains and Espaço da Escrita – Coordenadoria Geral da Universidade (UNICAMP) for the language services provided.
Supporting information
Supplementary information—Additional methods. Biomass growth and extraction, identification, and quantification of biotransformation products.
Supplementary Table 1—BLASTp output of reference enzymes from Grosmannia clavigera against Colletotrichum acutatum and Colletotrichum nymphaeae protein sets.
Supplementary Table 2—Colletotrichum nymphaeae enzymes - KAAS annotation.
Supplementary Table 3—Colletotrichum acutatum enzymes - KAAS annotation.
Supplementary Fig. 1—Sequence alignment of the epoxyde hydrolase candidate proteins from C. acutatum and C. nymphaeae (KXH64709.1) along with the previously described epoxide hydrolase from G. clavigera (F0X7A7).
Supplementary Fig. 2—Sequence alignment of the FAD-binding monooxygenase candidate proteins from C. acutatum and C. nymphaeae (KXH59233.1) along with the previously described FAD-binding monooxygenase from G. clavigera (F0X7A8).
Funding
This study was funded by the National Counsel of Technological and Scientific Development (CNPq) (Grant Numbers 473981/2012-2 and 400411/2016-4); São Paulo Research Foundation (FAPESP) (Grant Number 2016/21619-7) and Coordination for the Improvement of Higher Education Personnel (CAPES) (scholarship, A. Sales).
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Sales, A., Afonso, L.F., Americo, J.A. et al. Monoterpene biotransformation by Colletotrichum species. Biotechnol Lett 40, 561–567 (2018). https://doi.org/10.1007/s10529-017-2503-2
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DOI: https://doi.org/10.1007/s10529-017-2503-2