Abstract:In order to improve the quality of hairtail surimi products, the effects of soybean trypsin inhibitor (STI) on the proteolysis and gel properties of hairtail surimi were determined by the trichloroacetic acid-soluble (TCA-soluble) peptide content, protein components and gel strength. The results showed that: the autolysis of hairtail surimi was significantly associated with temperture. Myosin heavy chain (MHC) of hairtail surimi protein was gradually disappeared, as the temperature increased.. Meanwhile, TCA-soluble peptide increased to the maximum value of 1.3μmol tyrosine·g-1 at 70℃. Proteolysis in both kamaboko and modori gels were inhibited by STI. With the addition of 0.10‰ STI, they had the lowest TCA-soluble peptide of 0.13 and 0.30μmol tyrosine·g-1, the highest gel strength of 414.74 and 1 262.28 g·mm, and the expressible moisture content dropped to 5.44% and 3.76%, respectively. Compared with the control group, the gel structure of hairtail surimi, was more dense and uniform under the electron microscope, and the gel whiteness slightly decreased. It was concluded that STI could effectively improve the quality of hairtail surimi products, thus providing a basis for the production of high-quality hairtail surimi