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Isolation, identification, and inhibitory enzyme activity of phenolic substances present in Spirulina
Jian Li1, Guoxiang Chi1, Li Wang1
1College of Food and Biological Engineering, Jimei University, Xiamen, P.R. China.
Abstract:
Spirulina species are edible with high nutritional as well as potential therapeutic values. In this work, we show that phenolic extracts from Spirulina (p-Coumaric acid) possessed inhibitory potential on α-glucosidase (IC50 = 1.67 ± 0.02 mM) and tyrosinase (IC50 = 52.71 ± 3.01 mM). Moreover, p-Coumaric acid inhibited α-glucosidase and tyrosinase in a reversible mixed-type manner. Interestingly, molecular docking demonstrated that p-Coumaric acid penetrated in depth of the active-site of tyrosinase and α-glucosidase by the noncovalent force or interaction. Among them, making polar interactions with Cu2+ ions and the amino acid residue capable of forming cation-π significantly contribute to the strong binding of p-Coumaric acid on tyrosinase. p-Coumaric acid was isolated and identified from Spirulina for the first time, which can be used as a lead compound for the design of functional food additives and skin-lightening active ingredient in cosmetics, and pharmaceuticals against type 2 diabetes. PRACTICAL APPLICATIONS: A natural, food-derived compound possessing the potential for the development of an anti-hyperglycaemic and skin-lightening supplement is very promising in cosmetics, functional food, and pharmaceuticals against type 2 diabetes. Herein, the present study is the first to present high levels of p-Coumaric acid from Spirulina, which simultaneously possessed inhibition potential on α-glucosidase and tyrosinase. Importantly, we gained initial information about the polypeptide-inhibitor interactions and underlying mechanisms for Spirulina's therapeutic effects, which will provide the bases for developing new drugs for preventing or treating type 2 diabetes and enzyme inhibitors. Moreover, this work also demonstrates the potential of the extraction of high-value chemicals from Spirulina waste.
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