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Updated: Feb 15, 2026

Detection of Protease Activity by Fluorescent Peptide Zymography
Published on: January 20, 2019
Antioxidant and anti-freezing peptides from salmon collagen hydrolysate prepared by bacterial extracellular protease
RiBang Wu1, CuiLing Wu1, Dan Liu1
1School of Life Science, State Key Laboratory of Medical Genetics, Central South University, Changsha 410013, China.
Abstract:
Extracted salmon skin collagen was hydrolysed with the free or immobilized extracellular protease of Vibrio sp. SQS2-3. The hydrolysate exhibited anti-freezing activity (>3 kDa) and antioxidant activity (<3000 Da) after ultrafiltration. The antioxidant peptide was further purified by size-exclusion chromatography and found to scavenge DPPH (73.29 ± 1.03%), OH (72.73 ± 3.34%,), and intracellular ROS in HUVECs; protect DNA against oxidation-induced damage; and have an ORAC of 2.78 ± 0.28 mmol TE/g. The antioxidant peptide fraction was identified using mass spectrometry, and nineteen salmon collagen-sourced peptides were obtained. Of these, the peptide Pro-Met-Arg-Gly-Gly-Gly-Gly-Tyr-His-Tyr is a novel sequence and was the major component; this peptide was shown to have antioxidant activity via the ORAC assay (2.51 ± 0.14 mmol TE/g). These results suggested that the protease from Vibrio sp. SQS2-3 is suitable for preparation of anti-freezing peptides and antioxidant peptides in a single step and represents a comprehensive use of fish skin collagen.
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