β-Lactoglobulin - Wikipedia
β-Lactoglobulin (beta-lactoglobulin, BLG, Bos d 5) is the major whey protein of cow and sheep's milk (~3 g/L), and is also present in many other mammalian species; a notable exception …
Beta-Lactoglobulin - an overview | ScienceDirect Topics
Beta lactoglobulin (β-LG), whose example structure is shown in Fig. 1, is a milk protein widely used within the food products industry. β-LG is the main component of whey protein that can …
Beta-Lactoglobulin as a Model Food Protein: How to Promote, …
Bovine milk beta-lactoglobulin (BLG) is a small whey protein that is a common ingredient in many foods. Many of the properties of BLG relevant to the food industry are related to its unfolding …
β-乳球蛋白 - 百度百科
β-乳球蛋白（β-lactoglobulin）是鲜奶当中蛋白质的一种，约占鲜奶蛋白质的7~12%。
β-Lactoglobulin Influences Human Immunity and Promotes Cell ...
β-Lactoglobulin (LG) is suspected to enhance or modulate human immune responses. Moreover, LG is also hypothesized to increase human cell proliferation. However, these potential …
Dairy bioactive proteins and peptides: a narrative review
While no definitive role for β-Lg has been identified, the most compelling evidence supports its role in molecular transport. Beta-lactoglobulin can bind a variety of lipids, including retinol, long …
Invited Review: β-Lactoglobulin: Binding Properties, Structure, and ...
2004年4月1日 · β-Lactoglobulin binds both fatty acids and retinol, and the structure is similar to the known transporter, plasma RBP. The nature of the ligand transported, apart from being …
Beta-Lactoglobulin - an overview | ScienceDirect Topics
Beta-lactoglobulin is a globular protein of the lipocalin family (Fig. 3.1). It has a molecular weight of 18,300 and comprises 162 amino acid residues, including a relatively high proportion of …
Invited review: beta-lactoglobulin: binding properties, structure, …
beta-Lactoglobulin (beta-LG) is the major whey protein of ruminant species and is also present in the milks of many, but not all, other species.
β-Lactoglobulin | SpringerLink
In the past decade since the review in the 2nd edition of this book (Hambling et al., 1992), significant advances in our understanding of the structure and properties of β-lactoglobulin (β …