This article provides an updated review of tyrosinase inhibitors, focusing on both natural and synthetic sources. Tyrosinase is a multifunctional, glycosylated, copper-containing oxidase that catalyzes the first two steps in mammalian melanogenesis and is responsible for enzymatic browning reactions in damaged fruits. The undesirable effects of hyperpigmentation in human skin and enzymatic browning in fruits have driven researchers to seek new potent tyrosinase inhibitors for use in foods and cosmetics. The article compares the inhibitory strength of newly discovered inhibitors with that of the standard inhibitor, kojic acid, and discusses their inhibitory mechanisms. The biochemical characteristics and reaction mechanisms of tyrosinase are briefly discussed, highlighting its role in melanin formation and the conservation of the central copper-binding domain across different sources. The article classifies tyrosinase inhibitors into six types: reducing agents, o-dopaquinone scavengers, alternative enzyme substrates, nonspecific enzyme inactivators, specific tyrosinase inactivators, and specific tyrosinase inhibitors. Only the last two types are considered "true inhibitors" that bind to the enzyme and reduce its catalytic capacity. The review then delves into the classification of polyphenols, benzaldehyde and benzoate derivatives, long-chain lipids and steroids, other natural or synthetic inhibitors, and irreversible inactivators based on chemical structures or inhibitory mechanisms. Polyphenols, including flavonoids, isoflavonoids, chalcones, stilbenes, and coumarins, are discussed in detail, with a focus on their structural requirements for potent inhibitory activity. The article also examines benzaldehyde and benzoate derivatives, highlighting their mechanisms of action and inhibitory strengths. Overall, the article provides a comprehensive overview of the current state of tyrosinase inhibitors, emphasizing the importance of specific structural features in achieving potent inhibitory activity.This article provides an updated review of tyrosinase inhibitors, focusing on both natural and synthetic sources. Tyrosinase is a multifunctional, glycosylated, copper-containing oxidase that catalyzes the first two steps in mammalian melanogenesis and is responsible for enzymatic browning reactions in damaged fruits. The undesirable effects of hyperpigmentation in human skin and enzymatic browning in fruits have driven researchers to seek new potent tyrosinase inhibitors for use in foods and cosmetics. The article compares the inhibitory strength of newly discovered inhibitors with that of the standard inhibitor, kojic acid, and discusses their inhibitory mechanisms. The biochemical characteristics and reaction mechanisms of tyrosinase are briefly discussed, highlighting its role in melanin formation and the conservation of the central copper-binding domain across different sources. The article classifies tyrosinase inhibitors into six types: reducing agents, o-dopaquinone scavengers, alternative enzyme substrates, nonspecific enzyme inactivators, specific tyrosinase inactivators, and specific tyrosinase inhibitors. Only the last two types are considered "true inhibitors" that bind to the enzyme and reduce its catalytic capacity. The review then delves into the classification of polyphenols, benzaldehyde and benzoate derivatives, long-chain lipids and steroids, other natural or synthetic inhibitors, and irreversible inactivators based on chemical structures or inhibitory mechanisms. Polyphenols, including flavonoids, isoflavonoids, chalcones, stilbenes, and coumarins, are discussed in detail, with a focus on their structural requirements for potent inhibitory activity. The article also examines benzaldehyde and benzoate derivatives, highlighting their mechanisms of action and inhibitory strengths. Overall, the article provides a comprehensive overview of the current state of tyrosinase inhibitors, emphasizing the importance of specific structural features in achieving potent inhibitory activity.