In modern society, there is increasing the interest in effect of health promotion due to increase in national income and westernization. The functional healthy foods were developed and acquired in marine-derived sources. The aim of this study was to investigate standard conditions for oyster hydroly...
In modern society, there is increasing the interest in effect of health promotion due to increase in national income and westernization. The functional healthy foods were developed and acquired in marine-derived sources. The aim of this study was to investigate standard conditions for oyster hydrolysate(Crassostrea gigas) processing and also to develop the functional food which have the effect of liver protection.
Chapter 1.
Transglutaminase(TGase), followed by Protamex and Neutrase were used for the standard conditions of oyster hydrolysate processing as enzymes. The oyster hydrolysate had protective action against ethanol-induced liver injury. For the characterization of the purified peptide, amino acid sequence was analyzed by LC/MS/MS. The molecular weights and amino acid sequences of peptides were identified as follows: G-S-S-G-M-K-I-I-F-R (1,094.5907 Da), K-S-G-A-T-A-K-V-K (888.5392 Da), Y-N-N-C-Q-K(868.3497 Da), M-Q-F-V-V-N-K-A-T-E (1208.5859 Da), R-C-A-V-K-L-L-G-G (972.5539 Da) and S-S-T-I-G-S-P-E (776.3552 Da).
Chapter 2.
The index peptide for quality control of oyster hydrolysate was validated according to specificity, linearity, accuracy, precision test, and recovery test. Specificity was confirmed with identical retention time, and calibration curves of MQF showed good linear regression (R2>0.9992). The LOD and LOQ were 267.8 μg/mL and 811.43 μg/mL, respectively. The amount of MQF in hydrolysate from oyster was about 377.6 μg /sample-g by the validated method. Also this study was designed to establish the shelf-life of the oyster hydrolysate using the quality changes, including moisture, E. coli, color, available methionine and cysteine. The decrease of available methionine was significantly correlated with storage time and temperature (p<0.05) and the shelf-life of oyster hydrolysate based on the available methionine was predicted as 54.8 months by Arrehnius equations.
Chapter 3.
The physicochemical properties of the oyster hydrolysate were investigated by amino acid composition, solubilities as pH and NaCl concentration, and partition coefficient of octanol/water. The major total amino acids of the oyster hydrolysate were Glu, Asp, Pro, Lys, Leu and Arg, whereas the major free amino acids were Tau, Pro, Glu, Ala, Pro and Arg. The maximum solubility against pH and NaCl of the oyster hydrolysate were observed at pH 4 and 0..2 M NaCl, respectively.
Chapter 4.
The maximum ester reaction between oyster hydrolysates and ethanol was occurred at 62℃. The synthesized peptides showed 117-125% recovery ability against alcohol damaged Chang cells in the concentration range of 1-200 μg/mL. The ligand KYW showed the highest binding affinity for the receptor PPAR-γ. The amino acid residues of PPAR-γ that interacted with all the ligands tested were Ile281, Cys285, Arg288, Ser289, Ile326, Leu333, Ile341. These results suggested that the oyster hydrolysate had the protective action against ethanol-impared liver.
The oyster hydrolysate has a potential application for the functional healthy foods or prodrug for liver protection. However more research is required about the mechanisms of liver protective activity and clinical studies.
In modern society, there is increasing the interest in effect of health promotion due to increase in national income and westernization. The functional healthy foods were developed and acquired in marine-derived sources. The aim of this study was to investigate standard conditions for oyster hydrolysate(Crassostrea gigas) processing and also to develop the functional food which have the effect of liver protection.
Chapter 1.
Transglutaminase(TGase), followed by Protamex and Neutrase were used for the standard conditions of oyster hydrolysate processing as enzymes. The oyster hydrolysate had protective action against ethanol-induced liver injury. For the characterization of the purified peptide, amino acid sequence was analyzed by LC/MS/MS. The molecular weights and amino acid sequences of peptides were identified as follows: G-S-S-G-M-K-I-I-F-R (1,094.5907 Da), K-S-G-A-T-A-K-V-K (888.5392 Da), Y-N-N-C-Q-K(868.3497 Da), M-Q-F-V-V-N-K-A-T-E (1208.5859 Da), R-C-A-V-K-L-L-G-G (972.5539 Da) and S-S-T-I-G-S-P-E (776.3552 Da).
Chapter 2.
The index peptide for quality control of oyster hydrolysate was validated according to specificity, linearity, accuracy, precision test, and recovery test. Specificity was confirmed with identical retention time, and calibration curves of MQF showed good linear regression (R2>0.9992). The LOD and LOQ were 267.8 μg/mL and 811.43 μg/mL, respectively. The amount of MQF in hydrolysate from oyster was about 377.6 μg /sample-g by the validated method. Also this study was designed to establish the shelf-life of the oyster hydrolysate using the quality changes, including moisture, E. coli, color, available methionine and cysteine. The decrease of available methionine was significantly correlated with storage time and temperature (p<0.05) and the shelf-life of oyster hydrolysate based on the available methionine was predicted as 54.8 months by Arrehnius equations.
Chapter 3.
The physicochemical properties of the oyster hydrolysate were investigated by amino acid composition, solubilities as pH and NaCl concentration, and partition coefficient of octanol/water. The major total amino acids of the oyster hydrolysate were Glu, Asp, Pro, Lys, Leu and Arg, whereas the major free amino acids were Tau, Pro, Glu, Ala, Pro and Arg. The maximum solubility against pH and NaCl of the oyster hydrolysate were observed at pH 4 and 0..2 M NaCl, respectively.
Chapter 4.
The maximum ester reaction between oyster hydrolysates and ethanol was occurred at 62℃. The synthesized peptides showed 117-125% recovery ability against alcohol damaged Chang cells in the concentration range of 1-200 μg/mL. The ligand KYW showed the highest binding affinity for the receptor PPAR-γ. The amino acid residues of PPAR-γ that interacted with all the ligands tested were Ile281, Cys285, Arg288, Ser289, Ile326, Leu333, Ile341. These results suggested that the oyster hydrolysate had the protective action against ethanol-impared liver.
The oyster hydrolysate has a potential application for the functional healthy foods or prodrug for liver protection. However more research is required about the mechanisms of liver protective activity and clinical studies.
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