Nutritional composition, ACE-inhibitory, and metal chelating properties of rohu (Labeo rohita) egg protein hydrolysate produced by Alcalase.
IR@CSIR-CFTRI
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Relation |
http://ir.cftri.com/13264/
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Title |
Nutritional composition, ACE-inhibitory, and metal chelating properties of rohu (Labeo rohita) egg protein hydrolysate produced by Alcalase. |
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Creator |
Chalamaiah, M.
Jyothirmayi, T. Diwan, P. V. Venu Babu, V. |
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Subject |
03 Proteins
Fish |
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Description |
Protein hydrolysate prepared from Rohu (Labeo rohita) egg by enzymatic hydrolysis using Alcalase was evaluated for nutritional composition, angiotensin-converting enzyme (ACE) inhibitory and metal chelating properties. The hydrolysis reaction was performed for 180 min at 55±1 °C after addition of Alcalase at a level of 2% (v/w). Nutritional composition of the hydrolysate revealed the presence of high protein content (71.6%) with all essential amino acids (PDCAAS 100) and substantial amounts of n-3 fatty acids, especially docosahexaenoic acid (DHA). Molecular mass analysis confirmed the presence of small molecular mass peptides below 10 kDa. The highest angiotensin-converting enzyme (ACE) inhibitory activity of rohu egg peptides was found to be 45.6%. Rohu egg protein hydrolysate had good metal chelating activity in a dose dependent manner. In addition, the hydrolysate showed excellent protein solubility to above 80% over a wide pH range of 2-12. The hydrolysate exhibited good foaming and emulsification at various pH values (2-10). These results suggest that the rohu egg protein hydrolysate could be useful in health food/nutraceutical/pharmaceutical industry for several applications. |
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Date |
2016
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Type |
Article
PeerReviewed |
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Format |
pdf
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Language |
en
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Identifier |
http://ir.cftri.com/13264/1/International%20Food%20Research%20Journal%2023%283%29%201017-1026%20%282016.pdf
Chalamaiah, M. and Jyothirmayi, T. and Diwan, P. V. and Venu Babu, V. (2016) Nutritional composition, ACE-inhibitory, and metal chelating properties of rohu (Labeo rohita) egg protein hydrolysate produced by Alcalase. International Food Research Journal, 23 (3). pp. 1017-1026. |
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