Abstract
Oyster (Crassostrea talienwhanensis) protein was hydrolyzed by trypsin to produce peptides with different response values, and response surface methodology (RSM) was applied to optimize the hydrolysis conditions. The highest degree of hydrolysis (DH) of the oyster peptide (OP) was obtained at an enzyme concentration of 1593.2 U/g, a pH of 8.2, a hydrolysis temperature of 40.1 °C, a hydrolysis time of 6.0 h, and a water/material ratio of 8.2. The greatest hydroxyl-radical-scavenging activity of OP was obtained at an enzyme concentration of 1546.3 U/g, a pH of 9.0, a hydrolysis temperature of 50.2 °C, a hydrolysis time of 5.1 h, and a water/material ratio of 5.6. The largest branched-chain amino acid (BCAA) content of OP was obtained at an enzyme concentration of 1323.8 U/g, a pH of 8.3, a hydrolysis temperature of 41.7 °C, a hydrolysis time of 6.7 h, and a water/material ratio of 4.8. The three experimental values were significantly in agreement with the predicted values within the 95% confidence interval. Furthermore, ultrafiltration and chromatographic methods were used to purify the OP, and 13 peptides that were rich in Lys, Arg, His, and Thr were identified by LC-MS/MS. The results of this study offer different optimum hydrolysis conditions to produce target peptides from oyster protein by using RSM, and this study provide a theoretical basis for the high-value utilization of oyster protein.
Highlights
Oysters, as one of the most widely distributed marine biological resources worldwide, are rich in nutrients, including special amino acids, taurine, and trace elements
The results of this study offer different optimum hydrolysis conditions to produce target peptides from oyster protein by using response surface methodology (RSM), and this study provide a theoretical basis for the high-value utilization of oyster protein
Oysters have been shown to have many biological activities, e.g., Zha et al [2] reported that the Hong Kong oyster (Crassostrea hongkongensis) has high acetylcholinesterase (AChE) activity, Wang et al [3] confirmed that oyster (Crassostrea gigas) hydrolysates had anti-tumor activity and immunostimulatory effects in BALB/c mice, Lee et al [4] studied the anti-inflammatory effects of oyster shells, and Miao et al [5]
Summary
As one of the most widely distributed marine biological resources worldwide, are rich in nutrients, including special amino acids, taurine, and trace elements. Molecules 2020, 25, 2844 components, there has been no systematic evaluation of the extraction conditions for oyster protein hydrolysates according to different applications. Some studies have reported that the functional and bioactive properties of peptides are directly linked to their structural features, including molecular size, presence or absence of charges, amino acid sequence, hydrophobicity, and hydrophilicity [7]. The functional properties of protein hydrolysates depend on the degree of hydrolysis (DH), which affects the size and the amino-acid composition of the peptides [8]. While a high DH may not coincide with a high amount of hydrolysates, uncontrolled or prolonged hydrolysis of proteins may result in a low content of active peptides [9]. It is important to choose the appropriate conditions during hydrolysis
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