{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,26]],"date-time":"2026-08-26T19:11:07Z","timestamp":1787771467196,"version":"build-2784847793"},"reference-count":56,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2023,1,27]],"date-time":"2023-01-27T00:00:00Z","timestamp":1674777600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["scijournals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["J Sci Food Agric"],"published-print":{"date-parts":[[2023,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>BACKGROUND<\/jats:title><jats:p>Tyrosinase is the key enzyme involved in enzymatic browning of plant\u2010derived foods. Inhibition of tyrosinase activity contributes to the control of food browning. Due to safety regulations or other issues, most identified tyrosinase inhibitors are not suitable for practical use. Therefore, it is necessary to search for novel tyrosinase inhibitors. In this study, the anti\u2010tyrosinase activity and mechanism of albendazole and 2\u2010(2\u2010aminophenyl)\u20101<jats:italic>H<\/jats:italic>\u2010benzimidazole (2\u20102\u2010A\u20101HB) were investigated through ultraviolet\u2013visible absorption spectroscopy, fluorescence spectra, molecular docking, and molecular dynamic (MD) simulation. The anti\u2010browning effect of albendazole on fresh\u2010cut apples was then elucidated.<\/jats:p><\/jats:sec><jats:sec><jats:title>RESULTS<\/jats:title><jats:p>Albendazole and 2\u20102\u2010A\u20101HB were both efficient tyrosinase inhibitors with IC<jats:sub>50<\/jats:sub> of 51\u2009\u00b1\u20091.5 and 128\u2009\u00b1\u20091.3\u2009\u03bcmol\u2009L<jats:sup>\u22121<\/jats:sup>, respectively. Albendazole suppressed tyrosinase non\u2010competitively and formed tyrosinase\u2013albendazole complex statically. Hydrogen bond and hydrophobic interaction were major driving forces in stabilizing the tyrosinase\u2013albendazole complex. While 2\u20102\u2010A\u20101HB inhibited the enzyme competitively and quenched its intrinsic fluorescence through a static mechanism, it generated strong binding affinity with tyrosinase through hydrophobic interaction. MD simulations further validated that albendazole\/2\u20102\u2010A\u20101HB could form stable complexes with tyrosinase and loosened its basic framework structure, leading to a change in secondary structure and conformation. In addition, albendazole could delay the browning of fresh\u2010cut apples by inhibiting the activity of polyphenol oxidase, peroxidase and phenylalanine ammonia\u2010lyase, and reducing the oxidation of phenolic compounds.<\/jats:p><\/jats:sec><jats:sec><jats:title>CONCLUSION<\/jats:title><jats:p>This research might provide a deep view of tyrosinase inhibition by benzimidazole derivatives and a theoretical basis for developing albendazole as a potential fresh\u2010keeping agent. \u00a9 2023 Society of Chemical Industry.<\/jats:p><\/jats:sec>","DOI":"10.1002\/jsfa.12450","type":"journal-article","created":{"date-parts":[[2023,1,15]],"date-time":"2023-01-15T00:40:24Z","timestamp":1673743224000},"page":"2824-2837","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Inhibition of albendazole and 2\u2010(2\u2010aminophenyl)\u2010<scp>1<i>H<\/i><\/scp>\u2010benzimidazole against tyrosinase: mechanism, 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