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2011 (Vol. 3, Issue: 5)
Article Information:

Preparation and Characteristic of Iron-Binding Peptides from Shrimp Processing Discards Hydrolysates

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

Key words:  Amino acid composition, enzymatic hydrolysis, iron-binding activity, response surface methodology, shrimp processing discards, ,
Vol. 3 , (5): 348-354
Submitted Accepted Published
2011 June, 21 2011 August, 27 2011 October, 25

The aim of this study was focused on preparation of iron-binding peptides from Shrimp Processing Discards (SPD) hydrolysate using response surface methodology (RSM) and characteristic of the iron-peptides complex. Six kinds of protease (tyrpsin, pepsin, protmex, flavourzyme, neutrase and alcalase) were used to hydrolysis the SPD protein and the trypsin hydrolysate showed the highest iron-binding activity. The factorial design experiments showed that pH, trypsin concentration and hydrolysis time affected significantly the ironbinding activity of hydrolysate. Then the trypsin hydrolysis conditions (time, enzyme concentration, pH) were optimized by RSM using central composition design for produing highest iron-binding activity. The pH 8.18, enzyme concentration of 500 U/mL and a hydrolysis time of 120 min were found to be the optimum conditions to obtain a higher iron-binding activity of 6.75 μg-EDTA/mg-protein, which is very closed to the three verificated replicated experiments with 6.73 μg-EDTA/mg-protein. The amino acid composition of the ironpeptides complex was closed to FAO reference protein. The main compositions of the iron-peptides complex were iron of 11.1%, protein of 71.5% and ash of 19.3%. The peptides bound with iron were certified by infrared chromatgraphy.
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  Cite this Reference:
Zhang-yan Ren, Guang-rong Huang, Jia-xin Jiang and Wen-wei Chen, 2011. Preparation and Characteristic of Iron-Binding Peptides from Shrimp Processing Discards Hydrolysates.  Advance Journal of Food Science and Technology, 3(5): 348-354.
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ISSN (Online):  2042-4876
ISSN (Print):   2042-4868
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