PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9891258-6 1998 beta-Lactoglobulin and alpha-lactalbumin were also identified in the water extract of Feta cheese. Water 69-74 lactalbumin alpha Homo sapiens 23-40 16256563-3 2003 As a small amount of alpha-lactalbumin is added to the mixture, there is a substantial increase (up to 80%) in the maximum water solubility in the water-in-oil microemulsion phase. Water 123-128 lactalbumin alpha Homo sapiens 21-38 16256563-3 2003 As a small amount of alpha-lactalbumin is added to the mixture, there is a substantial increase (up to 80%) in the maximum water solubility in the water-in-oil microemulsion phase. Water 147-152 lactalbumin alpha Homo sapiens 21-38 16256563-5 2003 As the molar ratio of alpha-lactalbumin to AOT surpasses approximately 1:300, the partitioning of water, protein, and surfactant shifts to the excess aqueous phase, where soluble assemblies with positive curvature are detected by dynamic light scattering. Water 98-103 lactalbumin alpha Homo sapiens 22-39 10611403-1 1999 To model the molten globule structure of alpha-lactalbumin, molecular dynamics (MD) simulations were carried out for the protein in explicit water at high temperature. Water 141-146 lactalbumin alpha Homo sapiens 41-58 10339354-0 1999 Adsorption Dynamics of alpha-Lactalbumin and beta-Lactoglobulin at Air-Water Interfaces. Water 71-76 lactalbumin alpha Homo sapiens 23-40 10339354-1 1999 Dynamics of adsorption of 14C radiolabeled beta-lactoglobulin and alpha-lactalbumin at the air-water interface was investigated through the measurement of surface pressure (pi) and surface concentration (Gamma) via a radiotracer technique. Water 95-100 lactalbumin alpha Homo sapiens 66-83 10339354-10 1999 The model calculations seem to indicate that alpha-lactalbumin changes its orientation at the air-water interface from side-on to other orientations at higher surface concentrations. Water 98-103 lactalbumin alpha Homo sapiens 45-62 1931971-9 1991 These results can be seen to be consistent with UVCD and resolution-enhanced FTIR spectra of alpha-lactalbumin and lysozyme in both D2O and H2O environments. Water 140-143 lactalbumin alpha Homo sapiens 93-110 9715667-5 1998 However, calorimetric measurements provide data revealing only the two-state mechanism of alpha-lactalbumin unfolding in both water and in aqueous ethanol solutions. Water 126-131 lactalbumin alpha Homo sapiens 90-107 3349046-7 1988 Characterization of four Trp"s in alpha-lactalbumin shows that the two outer Trp"s are moderately H bonded to solvent water and closely surrounded by aliphatic side chains while the inner two are not H bonded nor closely surrounded by aliphatic side chains. Water 118-123 lactalbumin alpha Homo sapiens 34-51 2059662-5 1991 The interaction of apo-alpha-lactalbumin with melittin causes some changes in the environment of its aromatic amino acid residues and drastically alters the conformation of melittin, increasing its alpha-helical content but leaving its single tryptophan residue accessible to water. Water 276-281 lactalbumin alpha Homo sapiens 23-40 33125963-0 2021 Laccase cross-linking of sonicated alpha-Lactalbumin improves physical and oxidative stability of CLA oil in water emulsion. Water 109-114 lactalbumin alpha Homo sapiens 35-52 3492924-8 1987 Taking a value of 0.35 for the solvent drag reflection coefficient for alpha-lactalbumin, we conclude that the increased solute flux represents solvent drag through a water pathway with a hydraulic conductivity of 3.6 X 10(-7) cm X s-1 X cmH2O-1. Water 167-172 lactalbumin alpha Homo sapiens 71-88 3492924-9 1987 Our data conforms to the hypothesis that alpha-lactalbumin is transported across the capillary wall by restricted diffusion and solvent drag in a pathway that carries 90% of the transcapillary water flow (the principle water pathway). Water 193-198 lactalbumin alpha Homo sapiens 41-58 3492924-9 1987 Our data conforms to the hypothesis that alpha-lactalbumin is transported across the capillary wall by restricted diffusion and solvent drag in a pathway that carries 90% of the transcapillary water flow (the principle water pathway). Water 219-224 lactalbumin alpha Homo sapiens 41-58 33555192-0 2021 alpha-Lactalbumin Self-Assembled Nanoparticles with Various Morphologies, Stiffnesses, and Sizes as Pickering Stabilizers for Oil-in-Water Emulsions and Delivery of Curcumin. Water 133-138 lactalbumin alpha Homo sapiens 0-17 29763567-2 2018 In this study, we used super-temporal-resolved microscopy (STReM) to study the interfacial kinetics of a globular protein, alpha-lactalbumin (alpha-LA), adsorbing at the water-nylon 6,6 interface. Water 170-175 lactalbumin alpha Homo sapiens 123-140 29763567-2 2018 In this study, we used super-temporal-resolved microscopy (STReM) to study the interfacial kinetics of a globular protein, alpha-lactalbumin (alpha-LA), adsorbing at the water-nylon 6,6 interface. Water 170-175 lactalbumin alpha Homo sapiens 142-150 29166117-0 2017 Adsorption and conformations of lysozyme and alpha-lactalbumin at a water-octane interface. Water 68-73 lactalbumin alpha Homo sapiens 45-62 29617841-5 2018 Likewise, because of its physical characteristics, which include water solubility and heat stability, alpha-lactalbumin has the potential to be added to food products as a supplemental protein. Water 65-70 lactalbumin alpha Homo sapiens 102-119 29166117-5 2017 In this paper, molecular dynamics simulations are used to investigate the adsorption and conformation of two similar proteins, lysozyme and alpha-lactalbumin, at a water-octane interface. Water 164-169 lactalbumin alpha Homo sapiens 140-157 29166117-8 2017 Decomposing the different contributions to the protein energy at oil-water interfaces suggests that conformational change for alpha-lactalbumin, unlike lysozyme, is driven by favourable protein-oil interactions. Water 69-74 lactalbumin alpha Homo sapiens 126-143 25466060-1 2015 In this study the impact of covalent complexes of alpha-lactalbumin (alpha-La) with (-)-epigallocatechin gallate (EGCG) or chlorogenic acid (CA) was investigated on the physicochemical properties of beta-carotene oil-in-water emulsions. Water 220-225 lactalbumin alpha Homo sapiens 50-67 28857104-5 2017 Unconstrained molecular dynamics simulation of 50 molecules of TNS with the native state of BSA, native and two partially unfolded states of RNase A and alpha-lactalbumin in water was carried out. Water 174-179 lactalbumin alpha Homo sapiens 153-170 27006216-0 2016 Characterization of catechin-alpha-lactalbumin conjugates and the improvement in beta-carotene retention in an oil-in-water nanoemulsion. Water 118-123 lactalbumin alpha Homo sapiens 29-46 26898857-1 2016 We study the orientation of water and urea molecules and protein amide vibrations at aqueous alpha-lactalbumin and alpha-lactalbumin/urea interfaces using heterodyne-detected vibrational sum frequency generation. Water 28-33 lactalbumin alpha Homo sapiens 115-132 25466060-1 2015 In this study the impact of covalent complexes of alpha-lactalbumin (alpha-La) with (-)-epigallocatechin gallate (EGCG) or chlorogenic acid (CA) was investigated on the physicochemical properties of beta-carotene oil-in-water emulsions. Water 220-225 lactalbumin alpha Homo sapiens 69-77 25466060-4 2015 The least degradation of beta-carotene occurred in the emulsion stabilised with the alpha-La-EGCG covalent complex when stored at 25 C. These results implied that protein-polyphenol covalent complexes were able to enhance the physical stability of beta-carotene emulsion and inhibit the degradation of beta-carotene in oil-in-water emulsion, and the effect was influenced by the types of the phenolic compounds. Water 327-332 lactalbumin alpha Homo sapiens 84-92 24573329-3 2014 We have studied the effect of surface curvature on the association of two proteins, alpha-lactalbumin (alpha-LA) and beta-lactoglobulin (beta-LG), which perform their function at the oil-water interface in milk emulsions. Water 187-192 lactalbumin alpha Homo sapiens 84-101 24573329-3 2014 We have studied the effect of surface curvature on the association of two proteins, alpha-lactalbumin (alpha-LA) and beta-lactoglobulin (beta-LG), which perform their function at the oil-water interface in milk emulsions. Water 187-192 lactalbumin alpha Homo sapiens 103-111 22201548-0 2012 Conformational changes of alpha-lactalbumin adsorbed at oil-water interfaces: interplay between protein structure and emulsion stability. Water 60-65 lactalbumin alpha Homo sapiens 26-43 22201548-3 2012 The far-UV SRCD results showed that adsorption of alpha-La at oil-water interfaces created a new non-native secondary structure that was more stable to thermally induced conformational changes. Water 66-71 lactalbumin alpha Homo sapiens 50-58 22201548-6 2012 The DPI study showed that adsorption of alpha-La to a hydrophobic C18-water surface caused a change in the dimensions of alpha-La from the native globule-like shape (2.5-3.7 nm) to a compact/dense layer approximately 1.1 nm thick. Water 70-75 lactalbumin alpha Homo sapiens 40-48 22201548-1 2012 The conformation and structural dimensions of alpha-lactalbumin (alpha-La) both in solution and adsorbed at oil-water interfaces of emulsions were investigated using synchrotron radiation circular dichroism (SRCD) spectroscopy, front-face tryptophan fluorescence (FFTF) spectroscopy, and dual polarization interferometry (DPI). Water 112-117 lactalbumin alpha Homo sapiens 46-63 22201548-6 2012 The DPI study showed that adsorption of alpha-La to a hydrophobic C18-water surface caused a change in the dimensions of alpha-La from the native globule-like shape (2.5-3.7 nm) to a compact/dense layer approximately 1.1 nm thick. Water 70-75 lactalbumin alpha Homo sapiens 121-129 22201548-1 2012 The conformation and structural dimensions of alpha-lactalbumin (alpha-La) both in solution and adsorbed at oil-water interfaces of emulsions were investigated using synchrotron radiation circular dichroism (SRCD) spectroscopy, front-face tryptophan fluorescence (FFTF) spectroscopy, and dual polarization interferometry (DPI). Water 112-117 lactalbumin alpha Homo sapiens 65-73 22201548-11 2012 This study reports new information on the secondary and tertiary structural changes of alpha-La upon adsorption to oil-water interfaces. Water 119-124 lactalbumin alpha Homo sapiens 87-95 18410160-6 2008 When less than 1 wt % of alpha-lactalbumin was added into the system, the w/o droplets became nonspherical and larger in volume, corresponding to an increase in water uptake into the droplets. Water 161-166 lactalbumin alpha Homo sapiens 25-42