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Antioxidant activities of hydrolysates of Arca subcrenata prepared with three proteases.

Song L, Li T, Yu R, Yan C, Ren S, Zhao Y - Mar Drugs (2008)

Bottom Line: Three proteases (neutrase, alcalase and papain) were applied to hydrolyze the homogenate of A. subcrenata.Viewed from the angle of reducing power, such as scavenging activities against alpha,alpha-diphenyl-beta-picrylhydrazyl (DPPH) radical and hydrogen peroxide, the antioxidant activities of the alcalase hydrolysate (AH) were superior to neutrase hydrolysate (NH) and papain hydrolysate (PH), and its EC(50) values in DPPH radical and hydrogen peroxide scavenging effect were 6.23 mg/ml and 19.09 mg/ml, respectively.Moreover, compared with products hydrolyzed by neutrase and papain, the molecular mass of AH was lower and its content of amino acid of peptides was higher.

View Article: PubMed Central - PubMed

Affiliation: College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.

ABSTRACT
In order to get products with antioxidant activity from Arca subcrenata Lischke, the optimal hydrolase and hydrolysis conditions were investigated in the paper. Three proteases (neutrase, alcalase and papain) were applied to hydrolyze the homogenate of A. subcrenata. An orthogonal design was used to optimize hydrolysis conditions, and the pH-stat methods was used to determine the degree of hydrolysis. Viewed from the angle of reducing power, such as scavenging activities against alpha,alpha-diphenyl-beta-picrylhydrazyl (DPPH) radical and hydrogen peroxide, the antioxidant activities of the alcalase hydrolysate (AH) were superior to neutrase hydrolysate (NH) and papain hydrolysate (PH), and its EC(50) values in DPPH radical and hydrogen peroxide scavenging effect were 6.23 mg/ml and 19.09 mg/ml, respectively. Moreover, compared with products hydrolyzed by neutrase and papain, the molecular mass of AH was lower and its content of amino acid of peptides was higher. Therefore, alcalase was selected as the optimal enzyme to produce active ingredients since its hydrolysate exhibited the best antioxidant activity among them and possessed large amount of potential active peptides.

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Related in: MedlinePlus

DPPH free radical scavenging activity of the extracts and hydrolysates of A. subcrenata. NH: the hydrolysate treated by neutrase; AH: the hydrolysate treated by alcalase; PH: the hydrolysate treated by papain; SH: the supernatant of unprocessed homogenate of A. subcrenata. Ascorbic acid (Vc) was used as positive control. Regression equations were obtained from linear regression of the concentrations of the extracts and hydrolysates of A. subcrenata and DPPH radical scavenging effects. Each value is expressed as mean ± S.D. (n = 3).
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f2-md-06-00607: DPPH free radical scavenging activity of the extracts and hydrolysates of A. subcrenata. NH: the hydrolysate treated by neutrase; AH: the hydrolysate treated by alcalase; PH: the hydrolysate treated by papain; SH: the supernatant of unprocessed homogenate of A. subcrenata. Ascorbic acid (Vc) was used as positive control. Regression equations were obtained from linear regression of the concentrations of the extracts and hydrolysates of A. subcrenata and DPPH radical scavenging effects. Each value is expressed as mean ± S.D. (n = 3).

Mentions: Seen from Figure 2, all three hydrolysates exhibited the ability to eliminate DPPH radicals. Furthermore, the DPPH radical scavenging activity could be enhanced with the increase of protein concentrations in the samples (P < 0.05). AH showed a better effect than the other two in the range from 2 to 12 mg/ml (P < 0.05). According to the regression equations, the EC50 values of the hydrolysates for scavenging activity against DPPH were 10.50 mg/ml (NH), 6.23 mg/ml (AH) in order.


Antioxidant activities of hydrolysates of Arca subcrenata prepared with three proteases.

Song L, Li T, Yu R, Yan C, Ren S, Zhao Y - Mar Drugs (2008)

DPPH free radical scavenging activity of the extracts and hydrolysates of A. subcrenata. NH: the hydrolysate treated by neutrase; AH: the hydrolysate treated by alcalase; PH: the hydrolysate treated by papain; SH: the supernatant of unprocessed homogenate of A. subcrenata. Ascorbic acid (Vc) was used as positive control. Regression equations were obtained from linear regression of the concentrations of the extracts and hydrolysates of A. subcrenata and DPPH radical scavenging effects. Each value is expressed as mean ± S.D. (n = 3).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2630850&req=5

f2-md-06-00607: DPPH free radical scavenging activity of the extracts and hydrolysates of A. subcrenata. NH: the hydrolysate treated by neutrase; AH: the hydrolysate treated by alcalase; PH: the hydrolysate treated by papain; SH: the supernatant of unprocessed homogenate of A. subcrenata. Ascorbic acid (Vc) was used as positive control. Regression equations were obtained from linear regression of the concentrations of the extracts and hydrolysates of A. subcrenata and DPPH radical scavenging effects. Each value is expressed as mean ± S.D. (n = 3).
Mentions: Seen from Figure 2, all three hydrolysates exhibited the ability to eliminate DPPH radicals. Furthermore, the DPPH radical scavenging activity could be enhanced with the increase of protein concentrations in the samples (P < 0.05). AH showed a better effect than the other two in the range from 2 to 12 mg/ml (P < 0.05). According to the regression equations, the EC50 values of the hydrolysates for scavenging activity against DPPH were 10.50 mg/ml (NH), 6.23 mg/ml (AH) in order.

Bottom Line: Three proteases (neutrase, alcalase and papain) were applied to hydrolyze the homogenate of A. subcrenata.Viewed from the angle of reducing power, such as scavenging activities against alpha,alpha-diphenyl-beta-picrylhydrazyl (DPPH) radical and hydrogen peroxide, the antioxidant activities of the alcalase hydrolysate (AH) were superior to neutrase hydrolysate (NH) and papain hydrolysate (PH), and its EC(50) values in DPPH radical and hydrogen peroxide scavenging effect were 6.23 mg/ml and 19.09 mg/ml, respectively.Moreover, compared with products hydrolyzed by neutrase and papain, the molecular mass of AH was lower and its content of amino acid of peptides was higher.

View Article: PubMed Central - PubMed

Affiliation: College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.

ABSTRACT
In order to get products with antioxidant activity from Arca subcrenata Lischke, the optimal hydrolase and hydrolysis conditions were investigated in the paper. Three proteases (neutrase, alcalase and papain) were applied to hydrolyze the homogenate of A. subcrenata. An orthogonal design was used to optimize hydrolysis conditions, and the pH-stat methods was used to determine the degree of hydrolysis. Viewed from the angle of reducing power, such as scavenging activities against alpha,alpha-diphenyl-beta-picrylhydrazyl (DPPH) radical and hydrogen peroxide, the antioxidant activities of the alcalase hydrolysate (AH) were superior to neutrase hydrolysate (NH) and papain hydrolysate (PH), and its EC(50) values in DPPH radical and hydrogen peroxide scavenging effect were 6.23 mg/ml and 19.09 mg/ml, respectively. Moreover, compared with products hydrolyzed by neutrase and papain, the molecular mass of AH was lower and its content of amino acid of peptides was higher. Therefore, alcalase was selected as the optimal enzyme to produce active ingredients since its hydrolysate exhibited the best antioxidant activity among them and possessed large amount of potential active peptides.

Show MeSH
Related in: MedlinePlus