FOOD SCIENCE ›› 2017, Vol. 38 ›› Issue (11): 122-127.doi: 10.7506/spkx1002-6630-201711020

• Basic Research • Previous Articles     Next Articles

Purification and Identification of Antibacterial Peptides from Cottonseed Protein Isolate Hydrolysates

HAN Xiaoyan, BAO Yuming, XIN Fengjiao, HUANG Ying, Christophe BLECKER, DAI Xiaofeng   

  1. 1. Key Laboratory of Agro-Products Processing, Ministry of Agriculture, Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China; 2. Department of Food Science, University of Liège, Liège 999013, Belgium
  • Online:2017-06-15 Published:2017-06-19

Abstract: Cottonseed protein isolate (CPI) was digested in vitro to prepare hydrolysates with antibacterial activity. Ultrafiltration (UF), anion exchange chromatography (AEC), and semi preparative high performance liquid chromatography (semi-P-HPLC) were used to isolate and purify antibacterial peptides from CPI hydrolysates, and the purified peptides were sequenced by electrospray ionization-tandem mass spectrometry (ESI-MS/MS). During the purification process, CPI hydrolysates were separated into three fractions: U-Ⅰ, U-Ⅲ and U-III by UF and the obtained U-Ⅲ, with higher antibacterial ability, was further separated into QF-Ⅰ, QF-Ⅱ and QF-Ⅲ by AEC. After filtration, QF-Ⅱ, which showed higher antibacterial ability, was further fractionated using semi-P-HPLC into four subfractions: PF-Ⅰ, PF-Ⅱ, PF-Ⅲ and PF-Ⅳ, among which, PF-Ⅲ was determined to have the highest antibacterial activity. The purity of PF-Ⅲ showed a single peak in HPLC. Finally, by ESI-MS/MS, and the amino acid sequence of the peptide was identified as ISGLIYEETR (Ile-Ser-Gly-Leu-Ile-Tyr-Glu-Glu-Thr-Arg).

Key words: cottonseed protein isolate hydrolysates, peptide with antibacterial activity, isolation and purification, amino acid sequence

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