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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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Hydrolytic curves of A. subcrenata by three commercial enzymes and the endogenous enzymes.
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f1-md-06-00607: Hydrolytic curves of A. subcrenata by three commercial enzymes and the endogenous enzymes.

Mentions: During the hydrolysis, the homogenate was rapidly converted from viscous mince into a free flowing liquid. Hydrolytic curves of A. subcrenata by the enzymes and endogenous enzymes alone were shown in Figure 1. All curves exhibited an initial fast reaction followed by a slowdown. The shape of these progress curves was similar to what has been reported for enzymatic hydrolysis of different protein substrates [22].


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)

Hydrolytic curves of A. subcrenata by three commercial enzymes and the endogenous enzymes.
© Copyright Policy
Related In: Results  -  Collection

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

f1-md-06-00607: Hydrolytic curves of A. subcrenata by three commercial enzymes and the endogenous enzymes.
Mentions: During the hydrolysis, the homogenate was rapidly converted from viscous mince into a free flowing liquid. Hydrolytic curves of A. subcrenata by the enzymes and endogenous enzymes alone were shown in Figure 1. All curves exhibited an initial fast reaction followed by a slowdown. The shape of these progress curves was similar to what has been reported for enzymatic hydrolysis of different protein substrates [22].

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