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Abstract
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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
Submitted: June 08, 2012
Accepted: July 09, 2012
Published: August 20, 2012 |
Abstract:
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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.
Key words: Amino acid sequence , enzymatic hydrolysis, flavourzyme, iron binding peptide, isolation, ,
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Abstract
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Cite this Reference:
Guang-rong Huang, Zhang-yan Ren, Jia-xin Jiang and Wen-wei Chen, . Purification of a Hepta-peptide with Iron Binding Activity from Shrimp Processing By-products Hydrolysates. Advance Journal of Food Science and Technology, (4): 207-212.
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ISSN (Online): 2042-4876
ISSN (Print): 2042-4868 |
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