Enzyme and Microbial Technology, volume 160, pages 110069
Production of 3,4-dihydroxy-L-phenylalanine using novel tyrosinases from Bacillus megaterium
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Namhae Garlic Research Institute, 2465-8 Namhaedaero, Namhae, Gyeongsangnam-do 52430, Republic of Korea
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Publication type: Journal Article
Publication date: 2022-10-01
Journal:
Enzyme and Microbial Technology
Quartile SCImago
Q2
Quartile WOS
Q2
Impact factor: 3.4
ISSN: 01410229, 18790909
Biochemistry
Applied Microbiology and Biotechnology
Biotechnology
Bioengineering
Abstract
Tyrosinases, type-3 copper proteins responsible for melanin formation in various organisms, have considerable potential to produce bioactive catechol derivatives such as 3,4-dihydroxy- L -phenylalanine ( L -DOPA). They catalyze the ortho-hydroxylation of L -tyrosine to L -DOPA via monophenolase activity and the subsequent oxidation of L -DOPA to dopaquinone through diphenolase activity, which then spontaneously converts to melanin. In this study, six novel Bacillus megaterium strains, GJ802, GJ803, DY801, DY802, DY804, and DY805, were isolated from rice straw in South Korea. The tyrosinases of the novel strains were cloned, purified, and characterized. They exhibited catalytic activity over a broad pH range and showed high thermal stability. In addition, a tyrosinase of the B. megaterium DY805 strain (DY805), having the highest monophenolase activity among the tyrosinases, was used to produce L -DOPA as a biocatalyst. DY805 produced 8.77 mg/L L -DOPA from 200 µM L -tyrosine (36.2 mg/L), with a yield of 23.3%. After the optimization of several parameters for L -DOPA production, DY805 could produce up to 264 mg/L L -DOPA (30-fold increase), with a yield of 97.2% from 1500 µM L -tyrosine (272 mg/L). Taken together, these novel tyrosinases could be considered useful biocatalysts in L -DOPA production and other biotechnology fields. • Six novel Bacillus megaterium strains were isolated from rice straw. • Tyrosinases of B. megaterium were cloned, expressed, and purified. • Tyrosinases were active in the pH range of 4–10 and had high thermal stability. • Tyrosinase from B. megaterium DY805 strain was used to produce L -DOPA.
Top-30
Citations by journals
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Current Opinion in Biotechnology
1 publication, 33.33%
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Chemical Engineering Journal
1 publication, 33.33%
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Process Biochemistry
1 publication, 33.33%
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Citations by publishers
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Elsevier
3 publications, 100%
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Cha G. S. et al. Production of 3,4-dihydroxy-L-phenylalanine using novel tyrosinases from Bacillus megaterium // Enzyme and Microbial Technology. 2022. Vol. 160. p. 110069.
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Cha G. S., Mok J., Yun C., Park C. M. Production of 3,4-dihydroxy-L-phenylalanine using novel tyrosinases from Bacillus megaterium // Enzyme and Microbial Technology. 2022. Vol. 160. p. 110069.
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TY - JOUR
DO - 10.1016/j.enzmictec.2022.110069
UR - https://doi.org/10.1016/j.enzmictec.2022.110069
TI - Production of 3,4-dihydroxy-L-phenylalanine using novel tyrosinases from Bacillus megaterium
T2 - Enzyme and Microbial Technology
AU - Cha, Gun Su
AU - Mok, Ji-Ae
AU - Yun, Chul-Ho
AU - Park, Chan Mi
PY - 2022
DA - 2022/10/01 00:00:00
PB - Elsevier
SP - 110069
VL - 160
SN - 0141-0229
SN - 1879-0909
ER -
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@article{2022_Cha,
author = {Gun Su Cha and Ji-Ae Mok and Chul-Ho Yun and Chan Mi Park},
title = {Production of 3,4-dihydroxy-L-phenylalanine using novel tyrosinases from Bacillus megaterium},
journal = {Enzyme and Microbial Technology},
year = {2022},
volume = {160},
publisher = {Elsevier},
month = {oct},
url = {https://doi.org/10.1016/j.enzmictec.2022.110069},
pages = {110069},
doi = {10.1016/j.enzmictec.2022.110069}
}