Hyaluronidase(HAase)is widespread throughout the natural world,ranging from complex higher animals to simpler bacterial species.It catalyzes the degradation of hyaluronic acid,resulting in the loss of moisturizing components.The research into the inhibitory mechanism of rhamnan sulfate(RS),extracted from naturally grown Monostroma nitidum,on HAase activity is beneficial for the future development and utilization of algal polysaccharides in moisturizing skincare and health products.The IR analysis of RS,HAase and their mixture revealed the presence of sulfate groups identical to those in RS within the formed complexes;the formation of precipitation in the RS-HAase complex was found to be associated with sulfate groups and pH values;the biuret protein assay indicated that sulfate groups were involved in the formation of HAase and RS complexes,and the degree of inhibition of HAase activity by RS was dependent on the sulfate group content of RS;The analysis of enzyme inhibition kinetics demonstrated that the inhibition of HAase by the RS was of a com-petitive inhibition nature.
rhamnan sulfatehyaluronidasesulfate group contentinhibitionMonostroma nitidum
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