{"refrec":{"BRefID":113522,"RR":"<b>Dobretsov, S.; Xiong, H.; Xu, Y.; Levin, L.A.; Qian, P.-Y.</b> (2007). Novel antifoulants: inhibition of larval attachment by proteases. <i>Mar. Biotechnol. 9(3)</i>: 388-397. <a href=\"https://dx.doi.org/10.1007/s10126-007-7091-z\" target=\"_blank\">https://dx.doi.org/10.1007/s10126-007-7091-z</a>","BEntID":107978,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Mar. Biotechnol. 9(3)</i>: 388-397. <a href=\"https://dx.doi.org/10.1007/s10126-007-7091-z\" target=\"_blank\">https://dx.doi.org/10.1007/s10126-007-7091-z</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Dobretsov, S.; Xiong, H.; Xu, Y.; Levin, L.A.; Qian, P.-Y.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Dobretsov, S. <i>et al.</i>","Englishabstract":"We investigated the effect of commercially available enzymes (α-amylase, α-galactosidase, papain, trypsin, and lipase) as well as proteases from deep-sea bacteria on the larval attachment of the bryozoan <i>Bugula neritina</i> L. The 50% effective concentrations (EC<sub>50</sub>) of the commercial proteases were 10 times lower than those of other enzymes. Crude proteases from six deep-sea <i>Pseudoalteromonas</i> species significantly decreased larval attachment at concentrations of 0.03 to 1 mIU ml<sup>−1</sup>. The EC<sub>50</sub> of the pure protease from the bacterium <i>Pseudoalteromonas issachenkonii</i> UST041101-043 was close to 1 ng ml<sup>−1</sup> (0.1 mIU ml<sup>−1</sup>). The protease and trypsin individually incorporated in a water-soluble paint matrix inhibited biofouling in a field experiment. There are certain correlations between production of proteases by bacterial films and inhibition of larval attachment. None of the bacteria with biofilms that induced attachment of <i>B. neritina</i> produced proteolytic enzymes, whereas most of the bacteria that formed inhibitive biofilms produced proteases. 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