Journal of Polymers and the Environment

, Volume 21, Issue 2, pp 564–567

Preparation of Fish-scale Gelatins by Mild Hydrolysis and Their Characterization

Original Paper

DOI: 10.1007/s10924-012-0546-y

Cite this article as:
Jiang, L. J Polym Environ (2013) 21: 564. doi:10.1007/s10924-012-0546-y


This study characterized gelatins prepared by mild hydrolysis of freshwater fish-scale collagen. Among the selected types of protease (trypsin, neutral protease, papain, and alkaline protease), alkaline protease was proven to be the most effective enzyme for gelatin extraction by hydrolysis of fish-scale collagen. The optimum hydrolysis conditions were as follows: reaction time, 6 h; temperature, 50 °C; pH 9; and enzyme amount, 3 % (w/w). Under these optimum hydrolysis conditions, the gelatin yield reached 48.1 % (w/w). The gelatins prepared by alkaline protease hydrolysis show higher emulsion activity and lower emulsion stability indices than those prepared by water extraction.


Fish-scale gelatinEmulsion activity indexEmulsion stability indexAlkaline protease

Copyright information

© Springer Science+Business Media New York 2012

Authors and Affiliations

  1. 1.School of Marine Science and TechnologyHuaihai Institute of TechnologyXinpuChina