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    Abstract
2012 (Vol. 4, Issue: 4)
Article Information:

Purification of a Hepta-peptide with Iron Binding Activity from Shrimp Processing By-products Hydrolysates

Guang-rong Huang, Zhang-yan Ren, Jia-xin Jiang and Wen-wei Chen
Corresponding Author:  Huang Guangrong 

Key words:  Amino acid sequence , enzymatic hydrolysis, flavourzyme, iron binding peptide, isolation, ,
Vol. 4 , (4): 207-212
Submitted Accepted Published
June 08, 2012 July 09, 2012 August 20, 2012
Abstract:

The aim of this study was focused on isolation and purification of an iron binding peptide derived from shrimp processing by-products. The shrimp processing by-products was hydrolyzed by Flavourzyme to produce iron binding peptides hydrolysate. Then the hydrolysate with iron binding ability was isolated and purified by SPSepharose Fast Flow cation exchanger, Sephadex G-25 gel filtration and reversed phase high-performance liquid chromatography (RP-HPLC), respectively. A peptide of molecular mass 699 Da with strong iron binding ability was obtained and identified by mass spectrometry (MALDI-TOF-TOF) to be LPTGPKS after analysis and alignment in database. Results indicated that the production of iron-binding peptides from shrimp processing by-products supported further applications for high-value bioproducts in health care product.
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  Cite this Reference:
Guang-rong Huang, Zhang-yan Ren, Jia-xin Jiang and Wen-wei Chen, 2012. Purification of a Hepta-peptide with Iron Binding Activity from Shrimp Processing By-products Hydrolysates.  Advance Journal of Food Science and Technology, 4(4): 207-212.
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