摘要
酪蛋白磷酸肽(Casein Phosphopeptides,CPPs)是一类具有二价金属元素螯合活性的多肽集,而定向获得特异性营养元素螯合活性的酪蛋白磷酸肽具有理论和实际意义。采用Q强阴离子交换色谱和高效反相制备色谱(RP-HPLC)连续色谱方案分离碱性蛋白酶酶解得到的CPPs,获得锌高螯合活性的CPPs,并运用氨基酸组成、紫外光谱、红外光谱、固体核磁共振^(13)C谱、~1H谱、^(31)P谱表征分析酪蛋白磷酸肽螯合锌(CPP-Zn)的螯合性质。结果表明:CPPs经连续色谱分离可得具有高锌螯合活性的肽,其锌螯合活性可达88.68μg/mg。螯合前后CPPs的结构及氨基酸组成发生了明显变化,其中的磷酸基团参与了螯合,推测其主要结合位点是—COOH、—NH_2及P—OH中的—OH。
Casein Phosphopeptides （Casein Phosphopeptides, referred to as CPPs） is a class of polypeptides which has divalent metal chelating activity. The theory and practical significance of CPPs is its specific nutrient chela- ted. CPPs was obtained by enzymatic hydrolysis, and separated Q strong anion exchange chromatography and reverse phase preparative chromatography （RP-HPLC） ; it had highly active zinc chelate peptide（CPP-Zn）. Its structural was analyzed by proportion of amino acids,UV-VIS spectra,infrared spectroscopy,13C NMR spectra,Ill NMR spectra and 31p NMR spectra. Result： CPP purified from continuous chromatographic separation had strong zinc chelating ability of 88.68ug / rag. Structure analysis showed CPP structure and proportion of amino acids before and after chelation significantly changed. The phosphate groups are involved in the chelation, --COOH,--NH2 and --OH in P--OH were the primary binding site.
出处
《食品与发酵工业》
CAS
CSCD
北大核心
2017年第7期93-97,共5页
Food and Fermentation Industries
关键词
酪蛋白磷酸肽
分离
锌
螯合
结构
Casein Phosphopeptides
isolated
zinc
chelate
structure
