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Biological evaluation of two Keggin‐type polyoxometalates containing glycine as mushroom tyrosinase inhibitors
Author(s) -
Xing Rui,
Wang Fang,
Zheng Aping,
Wang Li,
Fei Dan,
Yu Yaping
Publication year - 2015
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1424
Subject(s) - tyrosinase , glycine , chemistry , non competitive inhibition , uncompetitive inhibitor , mushroom , nuclear chemistry , kinetics , stereochemistry , enzyme , biochemistry , food science , amino acid , physics , quantum mechanics
Two Keggin‐type polyoxometalates (POMs) containing glycine, (HGly) 3 PW 12 O 40 and (HGly) 4 SiW 12 O 40 , were synthesized and evaluated as mushroom tyrosinase inhibitors. The spectrophotometric method results showed that both (HGly) 3 PW 12 O 40 and (HGly) 4 SiW 12 O 40 could strongly inhibit the diphenolase activity of the tyrosinase and that their inhibition mechanisms were reversible. Their half‐inhibition concentration values were estimated to be 1.55 and 1.39 mmol/L, respectively. The inhibition kinetics analysis by Lineweaver–Burk plots indicated that (HGly) 3 PW 12 O 40 was an uncompetitive inhibitor with K IS = 0.046 mmol/L, whereas (HGly) 4 SiW 12 O 40 was a noncompetitive inhibitor with K I = K IS = 2.17 mmol/L. This study may help to extend the application of POMs in the fields of medicine and food preservation.