Michaelidou A, Alichanidis E, Urlaub H, Polychroniadou A, Zerfiridis G K
Laboratory of Dairy Technology, Berlin, Germany.
J Dairy Sci. 1998 Dec;81(12):3109-16. doi: 10.3168/jds.S0022-0302(98)75875-8.
Peptides were isolated from the water-soluble fraction of Feta cheese by reversed-phase HPLC in three successive steps. Peptide sequencing was performed by automatic Edman degradation. Most of the peptides originated from alpha s1-casein (CN), especially from the N-terminal half of the molecule. Two peptides originated from the C-terminal domain of beta-CN. Only one peptide, which was rich in histidine, originated from kappa-CN. beta-Lactoglobulin and alpha-lactalbumin were also identified in the water extract of Feta cheese. The origin of most of these peptides could be explained on the basis of known specificities of chymosin and lactococcal cell-wall proteinases.
通过反相高效液相色谱法，分三个连续步骤从费塔奶酪的水溶性部分中分离出肽段。采用自动埃德曼降解法进行肽段测序。大多数肽段源自αs1-酪蛋白（CN），尤其是分子的N端一半区域。有两个肽段源自β-酪蛋白的C端结构域。仅有一个富含组氨酸的肽段源自κ-酪蛋白。在费塔奶酪的水提取物中也鉴定出了β-乳球蛋白和α-乳白蛋白。这些肽段中大多数的来源可以根据凝乳酶和乳球菌细胞壁蛋白酶的已知特异性来解释。
