Optimization of antioxidant hydrolysate production from flying squid muscle protein using response surface methodology
► Hydrolysates from flying squid muscle protein exhibit antioxidative potentials. ► We optimize the hydrolysis condition of the protein. ► Reusing flying squid by-products can enhance economical effectiveness. The squid muscle protein, extracted from by-products of flying squid (Ommastrephes bartram...
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| Published in | Food and bioproducts processing Vol. 90; no. 4; pp. 676 - 682 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
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Rugby
Elsevier B.V
01.10.2012
Institution of Chemical Engineers |
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| Abstract | ► Hydrolysates from flying squid muscle protein exhibit antioxidative potentials. ► We optimize the hydrolysis condition of the protein. ► Reusing flying squid by-products can enhance economical effectiveness.
The squid muscle protein, extracted from by-products of flying squid (Ommastrephes bartrami) was hydrolyzed by five proteases (pepsin, trypsin, papain, alcalase and flavourzyme). DPPH radical scavenging power was used to evaluate antioxidative activity of hydrolysates. The hydrolysate obtained by papain exhibited the most excellent potential of antioxidative activity. Furthermore, response surface methodology (RSM) was employed to optimize hydrolysis conditions, including enzyme to substrate (E/S) ratio, reaction temperature, and hydrolysis time. The optimum conditions obtained were as follows: E/S ratio of 1.74%, temperature of 51°C and time of 46min, under which, DPPH radical scavenging activity of 74.25% was obtained. Moreover, it was found that the optimum hydrolysate of 8mg/mL displayed relatively stronger inhibitory effect on lipid peroxidation compared with α-Tocopherol of 0.1mg/mL. |
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| AbstractList | The squid muscle protein, extracted from by-products of flying squid (Ommastrephes bartrami) was hydrolyzed by five proteases (pepsin, trypsin, papain, alcalase and flavourzyme). DPPH radical scavenging power was used to evaluate antioxidative activity of hydrolysates. The hydrolysate obtained by papain exhibited the most excellent potential of antioxidative activity. Furthermore, response surface methodology (RSM) was employed to optimize hydrolysis conditions, including enzyme to substrate (E/S) ratio, reaction temperature, and hydrolysis time. The optimum conditions obtained were as follows: E/S ratio of 1.74%, temperature of 51°C and time of 46min, under which, DPPH radical scavenging activity of 74.25% was obtained. Moreover, it was found that the optimum hydrolysate of 8mg/mL displayed relatively stronger inhibitory effect on lipid peroxidation compared with α-Tocopherol of 0.1mg/mL. ► Hydrolysates from flying squid muscle protein exhibit antioxidative potentials. ► We optimize the hydrolysis condition of the protein. ► Reusing flying squid by-products can enhance economical effectiveness. The squid muscle protein, extracted from by-products of flying squid (Ommastrephes bartrami) was hydrolyzed by five proteases (pepsin, trypsin, papain, alcalase and flavourzyme). DPPH radical scavenging power was used to evaluate antioxidative activity of hydrolysates. The hydrolysate obtained by papain exhibited the most excellent potential of antioxidative activity. Furthermore, response surface methodology (RSM) was employed to optimize hydrolysis conditions, including enzyme to substrate (E/S) ratio, reaction temperature, and hydrolysis time. The optimum conditions obtained were as follows: E/S ratio of 1.74%, temperature of 51°C and time of 46min, under which, DPPH radical scavenging activity of 74.25% was obtained. Moreover, it was found that the optimum hydrolysate of 8mg/mL displayed relatively stronger inhibitory effect on lipid peroxidation compared with α-Tocopherol of 0.1mg/mL. The squid muscle protein, extracted from by-products of flying squid (Ommastrephes bartrami) was hydrolyzed by five proteases (pepsin, trypsin, papain, alcalase and flavourzyme). DPPH radical scavenging power was used to evaluate antioxidative activity of hydrolysates. The hydrolysate obtained by papain exhibited the most excellent potential of antioxidative activity. Furthermore, response surface methodology (RSM) was employed to optimize hydrolysis conditions, including enzyme to substrate (E/S) ratio, reaction temperature, and hydrolysis time. The optimum conditions obtained were as follows: E/S ratio of 1.74%, temperature of 51 degree C and time of 46 min, under which, DPPH radical scavenging activity of 74.25% was obtained. Moreover, it was found that the optimum hydrolysate of 8 mg/mL displayed relatively stronger inhibitory effect on lipid peroxidation compared with alpha -Tocopherol of 0.1 mg/mL. |
| Author | Yu, Hui Fang, Xubo Chen, Xiaoe Xie, Ningning Chen, Jing |
| Author_xml | – sequence: 1 givenname: Xubo surname: Fang fullname: Fang, Xubo – sequence: 2 givenname: Ningning surname: Xie fullname: Xie, Ningning – sequence: 3 givenname: Xiaoe surname: Chen fullname: Chen, Xiaoe email: xiaoechen@163.com – sequence: 4 givenname: Hui surname: Yu fullname: Yu, Hui – sequence: 5 givenname: Jing surname: Chen fullname: Chen, Jing |
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| Keywords | DPPH radical Lipid peroxidation Amino acid composition Papain Response surface methodology Flying squid Edible mollusc Shellfish Methodology Antioxidant Optimization Protein Cephalopoda Squid Hydrolysate Production Response surface Muscle Invertebrata Mollusca |
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| Snippet | ► Hydrolysates from flying squid muscle protein exhibit antioxidative potentials. ► We optimize the hydrolysis condition of the protein. ► Reusing flying squid... The squid muscle protein, extracted from by-products of flying squid (Ommastrephes bartrami) was hydrolyzed by five proteases (pepsin, trypsin, papain,... |
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| SubjectTerms | alpha-tocopherol Amino acid composition antioxidant activity Biological and medical sciences Byproducts DPPH radical enzyme substrates Fish and seafood industries Flight Flying squid Food industries free radical scavengers Fundamental and applied biological sciences. Psychology Hydrolysates hydrolysis Lipid peroxidation muscle protein Ommastrephes Optimization Papain pepsin Response surface methodology Scavenging Squid subtilisin temperature trypsin |
| Title | Optimization of antioxidant hydrolysate production from flying squid muscle protein using response surface methodology |
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