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      Elucidation of secondary alcohol metabolism in Starmerella bombicola and contribution of primary alcohol oxidase FAO1

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          ABSTRACT

          The yeast Starmerella bombicola NBRC10243 is an excellent producer of sophorolipids, which are among the most useful biosurfactants. The primary alcoholic metabolic pathway of S. bombicola has been elucidated using alcohol oxidase FAO1, but the secondary alcohol metabolic pathway remains unknown. Although the FAO1 mutant was unable to grow with secondary alcohols and seemed to be involved in the secondary alcohol metabolism pathway of S. bombicola, it had very low activity toward secondary alcohols. By analyzing the products of secondary alcohol metabolism, alkyl polyglucosides hydroxylated at the ω position in the alkyl chain of the secondary alcohol were observed in the FAO1 mutant, but not in the wild-type yeast. In the double mutant of FAO1 and UGTA1, accumulation of 1,13-tetradecandiol and 2,13-tetradecandiol was observed. The above results indicated that hydroxylation occurred first at the ω and ω–1 positions in the secondary alcohol metabolism of S. bombicola, followed by primary alcohol oxidation.

          Abstract

          We clarified the long-chain secondary alcohol utilization pathway in glycolipid producing yeast Starmerella bombicola and clarified the contribution of FAO1, which is a primary alcohol oxidase.

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          Diversity of Alkane Hydroxylase Systems in the Environment

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            Regioselective ω-hydroxylation of medium-chain n-alkanes and primary alcohols by CYP153 enzymes from Mycobacterium marinum and Polaromonas sp. strain JS666.

            The oxofunctionalization of saturated hydrocarbons is an important goal in basic and applied chemistry. Biocatalysts like cytochrome P450 enzymes can introduce oxygen into a wide variety of molecules in a very selective manner, which can be used for the synthesis of fine and bulk chemicals. Cytochrome P450 enzymes from the CYP153A subfamily have been described as alkane hydroxylases with high terminal regioselectivity. Here we report the product yields resulting from C(5)-C(12) alkane and alcohol oxidation catalyzed by CYP153A enzymes from Mycobacterium marinum (CYP153A16) and Polaromonas sp. (CYP153A P. sp.). For all reactions, byproduct formation is described in detail. Following cloning and expression in Escherichia coli, the activity of the purified monooxygenases was reconstituted with putidaredoxin (CamA) and putidaredoxin reductase (CamB). Although both enzyme systems yielded primary alcohols and α,ω-alkanediols, each one displayed a different oxidation pattern towards alkanes. For CYP153A P. sp. a predominant ω-hydroxylation activity was observed, while CYP153A16 possessed the ability to catalyze both ω-hydroxylation and α,ω-dihydroxylation reactions.
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              From lab to market: An integrated bioprocess design approach for new-to-nature biosurfactants produced by Starmerella bombicola

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                Author and article information

                Journal
                FEMS Yeast Res
                FEMS Yeast Res
                femsyr
                FEMS Yeast Research
                Oxford University Press
                1567-1356
                1567-1364
                11 February 2019
                March 2019
                11 February 2019
                : 19
                : 2
                : foz012
                Affiliations
                [1 ]Biological Science Laboratories, KAO Corp., 1334 Minato, Wakayama-shi, Wakayama, 640–8580, Japan
                [2 ]Department of Mathematical and Life Sciences, Graduate School of Science, Hiroshima University, 1-3-1 Kagamiyama, Higashi Hiroshima-shi, Hiroshima, Japan
                Author notes
                Corresponding author: Fumikazu Takahashi. Biological Science Laboratories, KAO Corp., 1334 Minato, Wakayama-shi, Wakayama, 640–8580, Japan. Tel: +81 73 426 5022; Fax: +81 73 426 5027; E-mail: takahashi.fumikazu@ 123456kao.co.jp
                Article
                foz012
                10.1093/femsyr/foz012
                6392925
                30753455
                91d358b4-38b1-4828-98f3-f7e9ae788e7b
                © FEMS 2019.

                This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@ 123456oup.com

                History
                : 08 August 2018
                : 08 February 2019
                Page count
                Pages: 8
                Categories
                Research Article

                Molecular biology
                fatty alcohol oxidase,fao1,secondary alcohol metabolism,sophorolipids, starmerella bombicola,diols production

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