Open AccessTat-Dependent Heterologous Secretion of Recombinant Tyrosinase by Pseudomonas fluorescens Is Aided by a Translationally Fused Caddie Protein
Author(s) -
Jae-Wook Ryu,
Hyunjong Byun,
Joseph P. Park,
Jiyeon Park,
Kyung Ha Noh,
Joo Hee Chung,
Haeshin Lee,
Jung Hoon Ahn
Publication year - 2019
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01350-19
Subject(s) - tyrosinase , pseudomonas fluorescens , biochemistry , streptomyces , secretion , biology , hydroxylation , recombinant dna , enzyme , chemistry , gene , bacteria , genetics
We observed that theS. antibioticus extracellular tyrosinase secretion level was even higher in its nonnatural translationally conjugated fusion protein form than in the natural complex of two separated polypeptides. The results of this study demonstrate that tyrosinase-expressingP. fluorescens can be a stable source of bacterial tyrosinase through exploiting the secretory machinery ofP. fluorescens .
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