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首页> 外文期刊>International Journal of Dairy Technology >A comparison of micellar casein and beta -casein as sources of basic peptides through tryptic hydrolysis and their enrichment using two-stage ultrafiltration.
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A comparison of micellar casein and beta -casein as sources of basic peptides through tryptic hydrolysis and their enrichment using two-stage ultrafiltration.

机译:胶束酪蛋白和β-酪蛋白通过胰蛋白酶解及其通过两步超滤富集作为碱性肽来源的比较。

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摘要

For the application of functional peptides in innovative products, these peptides have to be individually available. This may be accomplished by a well-considered combination of a pure protein precursor, a selective cleaving enzyme, and an advanced separation technology. In this proof-of-principle approach, micellar casein and beta -casein were subjected to tryptic hydrolysis and the generated casein peptides were identified and characterised. The basic target peptides, beta -casein f(177-183) and beta -casein f(170-176), were then enriched. A permeate containing 35% of the target peptides was produced after two-stage ultrafiltration of micellar casein tryptic hydrolysate. In comparison, enrichment up to 58% was achieved starting from beta -casein tryptic hydrolysate.
机译:为了将功能性肽应用于创新产品,这些肽必须单独获得。这可以通过考虑周全的纯蛋白质前体,选择性切割酶和先进的分离技术的组合来实现。在这种原理证明方法中,胶束酪蛋白和β-酪蛋白进行了胰蛋白酶水解,并鉴定和表征了产生的酪蛋白肽。然后富集基本的靶肽,β-酪蛋白f(177-183)和β-酪蛋白f(170-176)。在胶束酪蛋白胰蛋白酶解产物的两步超滤后,产生了含有35%目标肽的渗透液。相比之下,从β-酪蛋白胰蛋白酶解产物开始,可实现高达58%的富集。

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