Belitz H D, Kaiser K P
Deutsche Forschungsanstalt für Lebensmittelchemie, Stiftung des öffentlichen Rechts, München, Germany.
Z Lebensm Unters Forsch. 1993 Aug;197(2):118-22. doi: 10.1007/BF01260305.
Two Cheddar cheeses from two different production plants were ripened over 24 weeks at 10 degrees C and then analysed for peptides soluble in citrate buffer at pH 4.6 by reversed-phase (RP)-HPLC. Thirteen peptides with a chain length of between 35 and 65 amino acid residues and molecular masses between 3800 and 7400 were isolated and assigned to the corresponding amino acid sequences of the casein fractions via Edman degradation and amino acid composition. All peptides were fragments of the region K29-S96 of beta-casein A1 and A2, and eleven of them had M93 as the C-terminal. The amounts and proportions of these peptides varied differently during ripening of the two cheeses, so they may be suitable markers for characterizing the stage of ripening.
来自两个不同生产厂的两种切达干酪在10摄氏度下熟化24周，然后通过反相（RP）-HPLC分析在pH 4.6的柠檬酸盐缓冲液中可溶的肽。分离出13条链长在35至65个氨基酸残基之间、分子量在3800至7400之间的肽，并通过埃德曼降解和氨基酸组成将其对应于酪蛋白组分的相应氨基酸序列。所有肽均为β-酪蛋白A1和A2的K29-S96区域的片段，其中11条以M93作为C末端。在两种干酪的熟化过程中，这些肽的量和比例变化不同，因此它们可能是表征熟化阶段的合适标志物。
