TY - JOUR
T1 - Screening and characterization of a novel reversible 4-hydroxyisophthalic acid decarboxylase from Cystobasidium slooffiae HTK3
AU - Aono, Riku
AU - Yoshihara, Tomoya
AU - Nishida, Hotaka
AU - Kino, Kuniki
N1 - Publisher Copyright:
© 2021 The Author(s) 2021. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.
PY - 2021/7/1
Y1 - 2021/7/1
N2 - Owing to carboxylation activity, reversible decarboxylases can use CO2 as a C1-building block to produce useful carboxylic acids. Although many reversible decarboxylases can synthesize aromatic monocarboxylic acids, only a few reversible decarboxylases have been reported to date that catalyze the synthesis of aromatic dicarboxylic acids. In the present study, a reversible 4-hydroxyisophthalic acid decarboxylase was identified in Cystobasidium slooffiae HTK3. Furthermore, recombinant 4-hydroxyisophthalic acid decarboxylase was prepared, characterized, and used for 4-hydroxyisophthalic acid production from 4-hydroxybenzoic acid.
AB - Owing to carboxylation activity, reversible decarboxylases can use CO2 as a C1-building block to produce useful carboxylic acids. Although many reversible decarboxylases can synthesize aromatic monocarboxylic acids, only a few reversible decarboxylases have been reported to date that catalyze the synthesis of aromatic dicarboxylic acids. In the present study, a reversible 4-hydroxyisophthalic acid decarboxylase was identified in Cystobasidium slooffiae HTK3. Furthermore, recombinant 4-hydroxyisophthalic acid decarboxylase was prepared, characterized, and used for 4-hydroxyisophthalic acid production from 4-hydroxybenzoic acid.
KW - aromatic dicarboxylic acid
KW - microbial screening
KW - reversible decarboxylase
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U2 - 10.1093/bbb/zbab082
DO - 10.1093/bbb/zbab082
M3 - Article
C2 - 33942852
AN - SCOPUS:85110251632
SN - 0916-8451
VL - 85
SP - 1658
EP - 1664
JO - Bioscience, Biotechnology and Biochemistry
JF - Bioscience, Biotechnology and Biochemistry
IS - 7
ER -