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American Journal of Food Technology
  Year: 2009 | Volume: 4 | Issue: 6 | Page No.: 226-240
DOI: 10.3923/ajft.2009.226.240
 
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Optimization of Enzymatic Hydrolysis of Defatted Sesame Flour by Different Proteases and their Effect on the Functional Properties of the Resulting Protein Hydrolysate

Philip John Kanu, Jestina Baby Kanu, Edward H. Sandy, Joseph B.A. Kandeh, Philip M.P. Mornya and Zhou Huiming

Abstract:
Sesame Protein Hydrolysate (SPH) was prepared from defatted sesame (Sesamum indicum L.) flour (DSF) after screening with different proteases. The proteases under different conditions showed varied effects on the protein recovery process. For example, Alcalase® 2.4 L produced the highest degree of protein recovery (96.68%) at 60°C and pH 8 followed by Flavourzyme (69.76%). However, at 50°C and pH 7, the highest protein recovery was noted for Flavourzyme (79.28%) followed by Alcalase 2.4 L (77.62%). The hydrolysis conditions (Temperature T, pH, Enzyme/Substrate E/S, time t) were engineered to optimize the degree of hydrolysis (DH) with the process studied using the Response Surface Methodology (RSM). The DH ranged from 1.19 to 18.8% while the solubility of the Defatted Sesame Protein Isolate (DSPI) increased with increase in pH. The SPH was observed to be a better emulsifier with significantly higher foaming properties, water and oil capacities compared to the untreated DSF. Nonetheless, the stability of the resulting foam diminished on standing over time. The Sesame protein hydrolysate obtained using Alcalase was noted to have better functional attributes compared to that obtained using Flavourzyme.
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How to cite this article:

Philip John Kanu, Jestina Baby Kanu, Edward H. Sandy, Joseph B.A. Kandeh, Philip M.P. Mornya and Zhou Huiming, 2009. Optimization of Enzymatic Hydrolysis of Defatted Sesame Flour by Different Proteases and their Effect on the Functional Properties of the Resulting Protein Hydrolysate. American Journal of Food Technology, 4: 226-240.

DOI: 10.3923/ajft.2009.226.240

URL: https://scialert.net/abstract/?doi=ajft.2009.226.240

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