FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (9): 135-139.doi: 10.7506/spkx1002-6630-201309028

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Preparation and isolation of food-based gelatin peptide and the ice crystal inhibition

WANG Shao-yun,ZHAO Li-na,ZHOU Yan-fu,RAO Ping-fan   

  1. College of Biological Science and Technology, Fuzhou University, Fuzhou 350002, China
  • Received:2013-03-11 Revised:2013-04-15 Online:2013-05-15 Published:2013-05-07
  • Contact: WANG Shao-yun E-mail:shaoyunwang@gmail.cn

Abstract:

Food-based gelatin peptides with antifreeze activity were obtained under controlled hydrolysis conditions by Alcalase. The specific antifreeze peptide was isolated by chromatography and identified by mass-spectrum, the full amino acid sequences were determined. The result showed that with E/S of 1:15, hydrolyzing time of 30min, hydrolyzing temperature of 45℃, gelatin peptides demonstrated the best antifreeze activity. The antifreeze peptide on ice crystal inhibition shows specific rules during cold-heat-stage cycles, the key approach is how to control hydrolysis conditions. The specific antifreeze peptide was fractionated by size exclusion (Sephadex G-50), ion exchange (sulfopropyl-Sephadex C-25) columns and C18-HPLC, respectively. The molecular mass of the specific antifreeze peptide was determined to be 2107 Da by matrix assisted laser desorption ionization-time-of-flight (MALDI-TOF) mass spectrometry. The purified gelatin peptide with the molecular mass of 2107 Da strongly inhibited ice crystal growth in ice cream mix. The full amino acid sequences were determined to be GERGFPGERGSPGAQGLQGPR by Edman degradation.

Key words: hydrolysis, gelatin, antifreeze peptide, isolation

CLC Number: