Influence of molecular weight on intracellular antioxidant activity of invasive silver carp ( Hypophthalmichthys molitrix ) protein hydrolysates

The objective of this research was to make a protein hydrolysates from catfish (Pangasius pangasius) enzymatically using papain enzyme and analyzed the antioxidant activity of protein hydrolysates produced. The research used the method completely randomized design with two replications the treatment were the difference concentration of the papain enzyme (0%, 1%, 2%, 3%, 4%, 5%, and 6%). The parameters of research were antioxidative activity using DPPH (2,2-difenil-1–pikrilhidrazil), protein content, and molecular weight using SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis). The results showed that catfish protein hydrolysates prepared by papain enzyme has antioxidative activity. The highest degree of hydrolysis was 71.98% at enzyme concentration of 6%. Based on the DPPH scavenging method catfish protein hydrolysates has the antioxidative activity with the value 37.85-67.62%. The protein content of catfish protein hydrolysates were 20.86-54.47 mg/ml. The molecular weight of catfish protein hydrolyzates were 11.90-65.20 kDa. Keywords: Antioxidant, catfish, papain enzyme, protein hydrolyzate

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Cryoprotective Effects of Protein Hydrolysates Prepared from By-Products of Silver Carp (Hypophthalmichthys Molitrix) on Freeze-Thawed Surimi

Applied Sciences ◽

10.3390/app9030563 ◽

2019 ◽

Vol 9 (3) ◽

pp. 563

Author(s):

Wen-Juan Zhou ◽

Fa-Xiang Wang ◽

Jian Yu ◽

Xiang-Hong Li ◽

Yong-Le Liu

Keyword(s):

Atpase Activity ◽

Silver Carp ◽

Textural Properties ◽

Surface Hydrophobicity ◽

Protein Hydrolysates ◽

Control Group ◽

Hypophthalmichthys Molitrix ◽

Freeze Thaw ◽

And Control ◽

By Products

The cryoprotective effects of different amounts of protein hydrolysates prepared from by-products of silver carp using Protamex and Alcalase on surimi that were subjected to six freeze-thaw cycles were investigated. Commercial cryoprotectant (8% w/w 1:1 sucrose-sorbitol blend, SuSo) and control (without cryoprotectant) groups were used for comparison. After six freeze-thaw cycles, the lowest actomyosin extractability, Ca2+-ATPase activity and total sulfhydryl content, along with the highest surface hydrophobicity of actomyosin, were observed in the control group (P < 0.05). On the contrary, the group with addition of 2 g of hydrolysate prepared by Protamex hydrolysis (PH-2) displayed the highest actomyosin extractability, Ca2+-ATPase activity and correspondingly, lowest surface hydrophobicity of actomyosin (P < 0.05). Total sulfhydryl content of actomyosin and textural properties of heat-set surimi gels were similar between samples with PH-2 and those with SuSo (P > 0.05). Differences in molecular weight distribution, total and free amino acid compositions between the hydrolysates prepared by Protamex and Alcalase hydrolysis were possible reasons attributing to their variable cryoprotective effects on freeze-thawed surimi. Results from this study clearly support that hydrolysate prepared by Protamex hydrolysis at an appropriate amount could serve as an effective cryoprotectant without increasing the sweetness of surimi products. Furthermore, our findings suggest that the hydrolysates follow a different cryoprotection mechanism compared to SuSo (sucrose-sorbitol blend).

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