Optimization of chemical and enzymatic hydrolysis for production of chicken blood protein hydrolysate rich in angiotensin-I converting enzyme inhibitory and antioxidant activity.
IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore
View Archive Info| Field | Value | |
| Relation |
http://ir.cftri.res.in/14870/
https://doi.org/10.1016/j.psj.2021.101047 |
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| Title |
Optimization of chemical and enzymatic hydrolysis for production
of chicken blood protein hydrolysate rich in angiotensin-I
converting enzyme inhibitory and antioxidant activity.
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| Creator |
Nikhita, R.
Sachindra, N. M. |
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| Subject |
28 Meat, Fish & Poultry
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| Description |
Response surface methodology was
adopted to optimize hydrolysis conditions for the
production of antioxidant and angiotensin-I converting
enzyme (ACE) inhibitory peptides from chicken
red blood cells by both enzymatic and acid hydrolysis.
During acid hydrolysis, temperature (P , 0.001) and
acid concentration (P , 0.001) influenced the degree
of hydrolysis (DH%) and 1,1-diphenyl-2-
picrylhydrazyl (DPPH) radical scavenging activity of
the hydrolysate while ACE inhibitory activity of the
hydrolysate was strongly influenced by acid concentration
(P , 0.001). Temperature and time of hydrolysis
had no effect (P . 0.05) on the ACE inhibitory
activity of the hydrolysate. Acid hydrolysis conditions
of 50�C, 32 h, and 0.03 N hydrochloric acid resulted in
optimum DH% (33.1%), optimum DPPH scavenging
activity (46%), and optimum ACE inhibitory activity
(43.7%) of the hydrolysate. During enzymatic hydrolysis
of chicken red blood cells, DH% was influenced by
the temperature of hydrolysis (P , 0.001) and enzyme
concentration (P , 0.001). DPPH scavenging of the
hydrolysate was marginally (P , 0.05) influenced by
the temperature of hydrolysis and ACE inhibitory
activity of the hydrolysate was highly influenced by
temperature (P , 0.001) and enzyme concentration
(P , 0.001). Enzyme hydrolysis conditions of 60�C,
150 min, and 2.5% alcalase resulted in maximum DH%
of 63.9%, while the highest DPPH scavenging activity
(75%) of hydrolysate was observed under the hydrolysis
conditions of 60�C, 30 min, and 2.5% of the
enzyme. Optimum ACE inhibitory activity (45%) of
the hydrolysate was achieved at hydrolysis conditions
of 2.5% alcalase, 120 min of hydrolysis at 60�C. ACE
inhibitory activity of the enzymatically hydrolyzed
product was directly proportional to DH%, while
DPPH activity was inversely proportional to DH%.
DPPH scavenging activity of the acid hydrolysate was
recorded at a lower range (34.8–56.9%) compared to
the enzyme hydrolysate (40.4–77.4%), while ACE
inhibitory activity of both the hydrolysates was
observed in the same range (18.7–49.4 and 14.2–47.7%
for acid and enzyme hydrolysate, respectively). This
study indicated that chicken red blood cells could be
successfully hydrolyzed by both chemical and enzymatic
methods to obtain hydrolysates having antioxidant
and ACE inhibitory activity.
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| Date |
2021
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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.res.in/14870/1/2021%20Poultry%20Science%20100101047.pdf
Nikhita, R. and Sachindra, N. M. (2021) Optimization of chemical and enzymatic hydrolysis for production of chicken blood protein hydrolysate rich in angiotensin-I converting enzyme inhibitory and antioxidant activity. Poultry Science, 100. p. 101047. |
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