The　Escherichia　coli　aspartate　aminotransferase　gene　was　introduced　into　a　high　2-phenylethanol　(2-PEA)　producing　Saccharomyces　cerevisiae　YS58,　and　the　recombinant　strain　of　S. cerevisiae　was　utilized　for　the　co-production　of　2-PEA　and　L-homophenylalanine　(L-HPA)　via　a　fermentation　process.　The　L-HPA　productivity　of　the　recombinant　S. cerevisiae　improved　78.9%　in　comparison　to　the　wild-type　S. cerevisiae.　High　yields　of　43.7 mM　L-HPA　and　32.4 mM　2-PEA　were　achieved.　As　a　result,　the　coupling　of　the　biosynthesis　process　for　these　two　products　in　the　recombinant　strain　led　to　a　more　complete　and　efficient　utilization　of　the　substrate,　L-phenylalanine.　©　2016　The　Society　for　Biotechnology,　Japan