Calcium binding affects in vitro gastrointestinal digestion of bovine α-lactalbumin under infant, adult and elderly conditions

Z Wang, D Liu, X Hong, X Tao, J Zhang, J Zhang… - International Dairy …, 2024 - Elsevier
Abstract α-Lactalbumin bound with negligible, one and two Ca 2+ ions (apo, holo-Ca and
holo-2Ca La) were prepared, and thermal stability and gastrointestinal digestibility under …

A comparative study of structural and digestive properties of bovine, goat and human α-Lactalbumin with different calcium binding levels

X Ge, J Zhang, J Hu, D Liu, Y Gao, X Peng, S Wang… - Food Bioscience, 2024 - Elsevier
Abstract α-Lactalbumin (α-LA), the primary whey protein in human milk, is rich in essential
amino acids and plays a crucial role in infant growth and development. This study …

[HTML][HTML] Calcium bioaccessibility increased during gastrointestinal digestion of α-lactalbumin and β-lactoglobulin

J Wang, K Aalaei, LH Skibsted, LM Ahrné - Food Research International, 2023 - Elsevier
Calcium bioaccessibility depends on the amount of soluble calcium under intestinal
digestion. The changes in calcium during in vitro static digestion of α-lactalbumin and β …

Calcium binding by α-lactalbumin in human milk and bovine milk

B Lönnerdal, C Glazier - The Journal of nutrition, 1985 - Elsevier
The metal-binding property of α-lactalbumin (α-LA) in human milk was studied and
compared to that of bovine milk α-LA. Gel filtration on Sephadex G-75 at physiological pH …

An overview of bovine α-lactalbumin structure and functionality

N Stănciuc, G Rapeanu - The Annals of the University Dunarea de Jos …, 2010 - gup.ugal.ro
Abstract α-Lactalbumin is the second major protein in bovine milk (2-5% of the total protein
in bovine milk). The human variant has several physiologic functions in the neonatal period …

Effect of sodium and calcium addition on thermal denaturation of apo-α-lactalbumin: a differential scanning calorimetric study

P Relkin, B Launay, L Eynard - Journal of Dairy Science, 1993 - Elsevier
Abstract Changes of thermodynamic parameters related to thermal denaturation (5 to 100°
C) of commercial α-lactalbumin in Ca++-depleted form have been determined by differential …

[图书][B] Thermal stability of α-lactalbumin

MK McGuffey - 2004 - search.proquest.com
The first objective of this research was to quantitatively describe the denaturation and
aggregation processes of α-Lactalbumin at neutral pH in order to understand their …

Interaction of bovine α-lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy

C Barbana, MD Pérez, L Sánchez… - International dairy …, 2006 - Elsevier
The interaction of bovine holo-and apo-α-lactalbumin with fatty acids was studied using a
partition equilibrium technique and fluorescence spectroscopy. Using there techniques …

Cloning and molecular characterization of a yak α-lactalbumin cDNA from mammary tissue

WL Bai, RH Yin, YC Zheng, ZJ Ma, JC Zhong, RL Yin… - Livestock Science, 2010 - Elsevier
α-Lactalbumin is a calcium-binding protein, and is present in all mammalian milks. It plays
an important role in regulating the biosynthesis of lactose in mammary gland. In the present …

Nutritional and physiologic significance of α-lactalbumin in infants

B Lönnerdal, EL Lien - Nutrition Reviews, 2003 - academic.oup.com
Abstract α-Lactalbumin is the major protein in breast milk (20-25% of total protein) and has
been described to have several physiologic functions in the neonatal period. In the …