Optimization of an amino acid analysis method and determination of active peptides and free amino ac

来源 :2016年食品与健康国际研讨会 | 被引量 : 0次 | 上传用户:hzy11
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  To determinate conveniently active peptides (GSH,L-Camosine,Anserine) and free amino acids in shellfish muscle,an automatic amino acid method was established.The research optimizes the composition of buffer solution and elution process,and determinates the linear range,detection limit,precision and recovery rate of this new method with 0.02mol/L hydrochloric acid solution and 5% of the sulfosalicylic acid solution used as the extracting agent and the protein precipitation agent,respectively.Results indicated that active peptides and free amino acids in shellfish muscle were completely separated using this new method.The correlation coefficients of this method was above 0.999;the lowest detection limit was a range from 0.08 to 0.28μM;the mean recovery rate was a range from 83.6% to 103.6% and the concentration of RSD during the day and the night were respectively a range from 0.31%,1.23% to 0.71%,2.35%.Besides,the research found the main active peptides in shellfish muscle is GSH and the main free acid amino acid are Tau,Glu,Gly,Ala,Arg.The research suggest that the method is suitable for determination and analysis of a variety of active peptides and free amino acids in shellfish muscle.
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