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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

Hydrogen peroxide 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 hydrogen peroxide scavenging effects. Each value is expressed as mean ± S.D. (n = 3).
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f3-md-06-00607: Hydrogen peroxide 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 hydrogen peroxide scavenging effects. Each value is expressed as mean ± S.D. (n = 3).

Mentions: The dose-dependent antioxidant effect (P < 0.05) was observed from hydrogen peroxide scavenging activity of both supernatant and hydrolysates of A. subcrenata (Figure 3). The EC50 value of AH was 19.09 mg/ml, which displayed the highest scavenging effect on hydrogen peroxide among all three hydrolysates (P < 0.05), while that of PH was 23.52 mg/ml. Notably, NH at the final concentration of 24 mg/ml exhibited 26.11% scavenging effect on hydrogen peroxide, which was lower than the supernatant of A. subcrenata. It may be deduced that neutrase could destroy or decompose the supernatant function of scavenging hydrogen peroxide.


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)

Hydrogen peroxide 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 hydrogen peroxide 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

f3-md-06-00607: Hydrogen peroxide 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 hydrogen peroxide scavenging effects. Each value is expressed as mean ± S.D. (n = 3).
Mentions: The dose-dependent antioxidant effect (P < 0.05) was observed from hydrogen peroxide scavenging activity of both supernatant and hydrolysates of A. subcrenata (Figure 3). The EC50 value of AH was 19.09 mg/ml, which displayed the highest scavenging effect on hydrogen peroxide among all three hydrolysates (P < 0.05), while that of PH was 23.52 mg/ml. Notably, NH at the final concentration of 24 mg/ml exhibited 26.11% scavenging effect on hydrogen peroxide, which was lower than the supernatant of A. subcrenata. It may be deduced that neutrase could destroy or decompose the supernatant function of scavenging hydrogen peroxide.

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