Screening of Alcohol Dehydrogenase-Activating Peptides from Sturgeon Skin Enzymatic Hydrolysate

This study used sturgeon skin to prepare and screen alcohol dehydrogenase (ADH)-activating peptides. Optimal hydrolysis conditions were trypsin, 4.7 h, and 11.4 U/mg at 37°C and pH 7.5. Membrane separation showed that the 1–3 kDa fraction had the highest ADH activation activity, and LC-MS/MS identified 47 peptides within it. In silico prediction of peptide properties enabled screening of three potential ADH-activating peptides: FFSPKQPDLF, WIALPPLPSPR, and WLLPPSFL. Synthetic validation showed that WLLPPSFL had the weakest ADH activation, whereas FFSPKQPDLF and WIALPPLPSPR were significantly more active; WIALPPLPSPR is a more promising candidate due to its low predicted allergenicity.