Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase: structure-activity relationship

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Standard

Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase : structure-activity relationship. / Lu, Yao; Xu, Yi; Song, Meng-Ting; Qian, Ling-Ling; Liu, Xiao-Lin; Gao, Rong-Yao; Han, Rui-Min; Skibsted, Leif H.; Zhang, Jian-Ping.

In: RSC Advances, Vol. 11, No. 23, 2021, p. 13769-13779.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Lu, Y, Xu, Y, Song, M-T, Qian, L-L, Liu, X-L, Gao, R-Y, Han, R-M, Skibsted, LH & Zhang, J-P 2021, 'Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase: structure-activity relationship', RSC Advances, vol. 11, no. 23, pp. 13769-13779. https://doi.org/10.1039/d1ra01369f

APA

Lu, Y., Xu, Y., Song, M-T., Qian, L-L., Liu, X-L., Gao, R-Y., Han, R-M., Skibsted, L. H., & Zhang, J-P. (2021). Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase: structure-activity relationship. RSC Advances, 11(23), 13769-13779. https://doi.org/10.1039/d1ra01369f

Vancouver

Lu Y, Xu Y, Song M-T, Qian L-L, Liu X-L, Gao R-Y et al. Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase: structure-activity relationship. RSC Advances. 2021;11(23):13769-13779. https://doi.org/10.1039/d1ra01369f

Author

Lu, Yao ; Xu, Yi ; Song, Meng-Ting ; Qian, Ling-Ling ; Liu, Xiao-Lin ; Gao, Rong-Yao ; Han, Rui-Min ; Skibsted, Leif H. ; Zhang, Jian-Ping. / Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase : structure-activity relationship. In: RSC Advances. 2021 ; Vol. 11, No. 23. pp. 13769-13779.

Bibtex

@article{0edb111f5f134532a43d75ae2fb1553d,
title = "Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase: structure-activity relationship",
abstract = "Tyrosinase, widely distributed in nature, is a copper-containing polyphenol oxidase involved in the formation of melanin. Flavonoids are most often considered as tyrosinase inhibitors but have also been confirmed to be tyrosinase substrates. Four structure-related flavonoids including flavones (apigenin and luteolin) and flavonols (kaempferol and quercetin) are found to promote not inhibit browning induced by tyrosinase catalyzed oxidation both in model systems and in mushrooms under aerobic conditions. A comparison with enzymatic oxidation and autooxidation of flavonoids alone has helped to clarify why flavonoids function as a substrate rather than an inhibitor. Flavonoids almost do not affect the kinetics of melanin formation from enzymatic oxidation ofl-dopa in excess. In addition, a new brown complex formed during the reaction of flavonoid quinone and dopaquinone is suggested to enhance the browning effects by competing with isomerization and autooxidation. Structure-activity relationships of the four flavonoids in melanin formation leading to browning induced by autooxidation and enzymatic oxidation confirm the enzymatic nature of the browning.",
author = "Yao Lu and Yi Xu and Meng-Ting Song and Ling-Ling Qian and Xiao-Lin Liu and Rong-Yao Gao and Rui-Min Han and Skibsted, {Leif H.} and Jian-Ping Zhang",
year = "2021",
doi = "10.1039/d1ra01369f",
language = "English",
volume = "11",
pages = "13769--13779",
journal = "RSC Advances",
issn = "2046-2069",
publisher = "RSC Publishing",
number = "23",

}

RIS

TY - JOUR

T1 - Promotion effects of flavonoids on browning induced by enzymatic oxidation of tyrosinase

T2 - structure-activity relationship

AU - Lu, Yao

AU - Xu, Yi

AU - Song, Meng-Ting

AU - Qian, Ling-Ling

AU - Liu, Xiao-Lin

AU - Gao, Rong-Yao

AU - Han, Rui-Min

AU - Skibsted, Leif H.

AU - Zhang, Jian-Ping

PY - 2021

Y1 - 2021

N2 - Tyrosinase, widely distributed in nature, is a copper-containing polyphenol oxidase involved in the formation of melanin. Flavonoids are most often considered as tyrosinase inhibitors but have also been confirmed to be tyrosinase substrates. Four structure-related flavonoids including flavones (apigenin and luteolin) and flavonols (kaempferol and quercetin) are found to promote not inhibit browning induced by tyrosinase catalyzed oxidation both in model systems and in mushrooms under aerobic conditions. A comparison with enzymatic oxidation and autooxidation of flavonoids alone has helped to clarify why flavonoids function as a substrate rather than an inhibitor. Flavonoids almost do not affect the kinetics of melanin formation from enzymatic oxidation ofl-dopa in excess. In addition, a new brown complex formed during the reaction of flavonoid quinone and dopaquinone is suggested to enhance the browning effects by competing with isomerization and autooxidation. Structure-activity relationships of the four flavonoids in melanin formation leading to browning induced by autooxidation and enzymatic oxidation confirm the enzymatic nature of the browning.

AB - Tyrosinase, widely distributed in nature, is a copper-containing polyphenol oxidase involved in the formation of melanin. Flavonoids are most often considered as tyrosinase inhibitors but have also been confirmed to be tyrosinase substrates. Four structure-related flavonoids including flavones (apigenin and luteolin) and flavonols (kaempferol and quercetin) are found to promote not inhibit browning induced by tyrosinase catalyzed oxidation both in model systems and in mushrooms under aerobic conditions. A comparison with enzymatic oxidation and autooxidation of flavonoids alone has helped to clarify why flavonoids function as a substrate rather than an inhibitor. Flavonoids almost do not affect the kinetics of melanin formation from enzymatic oxidation ofl-dopa in excess. In addition, a new brown complex formed during the reaction of flavonoid quinone and dopaquinone is suggested to enhance the browning effects by competing with isomerization and autooxidation. Structure-activity relationships of the four flavonoids in melanin formation leading to browning induced by autooxidation and enzymatic oxidation confirm the enzymatic nature of the browning.

U2 - 10.1039/d1ra01369f

DO - 10.1039/d1ra01369f

M3 - Journal article

C2 - 35423946

AN - SCOPUS:85104303436

VL - 11

SP - 13769

EP - 13779

JO - RSC Advances

JF - RSC Advances

SN - 2046-2069

IS - 23

ER -

ID: 261163358