Collagen-rich meat processing by-products have potential utilization value. Extracellular protease Hap from meat-borne Aeromonas salmonicida has been identified as an ideal protease for hydrolyzing collagen. Here, to explore the possible application of Hap for giving chicken by-products a high added value, the hydrolysis ability and mechanism were investigated. With a V of 31.9 μg/mL/min and a K of 1.18 mg/mL, Hap demonstrated obvious substrate specificity to pepsin-solubilized collagen (PSC) derived from chicken by-products, and significantly affected the tertiary structure and microstructure of PSC. Hap was found to preferentially cleave the peptide bond between Gly-X by peptide release kinetics, attacking from two ends to the middle region for α1 chain. Sixteen peptides are anticipated to be non-toxic with twenty potential biological activities at the end of hydrolysis. These observations will enrich the collagen hydrolysis mechanism of protease secreted by meat-borne bacteria and provide new insights into the utilization of meat by-products.
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