Journal
FOOD CHEMISTRY
Volume 182, Issue -, Pages 136-142Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2015.02.004
Keywords
Purification; Angiotensin converting enzyme inhibitory peptides; Magnetic affinity
Funding
- National Natural Science Foundation of China [51372043]
- Key Project of Guangxi Natural Science Foundation [2012GXNSFDA53004]
- Key Project of Guangxi Experiment Centre of Science and Technology [LGZX201208]
- State Key Laboratory of Chemical Resource Engineering [CRE-2012-C-202]
- Guangxi Cultivation Project of Excellent Doctoral Dissertation [YCBZ2012010]
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In this study, angiotensin converting enzyme (ACE) inhibitory peptides from lizard fish protein hydrolysate with neutral protease were purified through magnetic affinity separation. Magnetic agarose microsphere was prepared by reverse-phase microemulsion method, and its surface was modified with epoxy groups to immobilize ACE as a magnetic affinity medium (MAM-ACE) and then mixed with lizard fish ultrafiltration hydrolysate (<5 kDa). The MAM-ACE was recovered by a magnet. The bound peptides were released by 1 M NaCl and further purified by reverse-phase high-performance liquid chromatography. The amino acid sequence of the peptide with the highest ACE inhibitory activity was identified as Gly-Met-Lys-Cys-Ala-Phe, and its IC50 was 45.7 +/- 1.1 mu M. The result indicates that MAM-ACE is a faster and more efficient method for purifying micro-bioactive peptides from food protein complex mixtures compared with ion exchange and gel chromatography. (C) 2015 Elsevier Ltd. All rights reserved.
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