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Interfacial and Bulk Properties of Potato and Faba Protein in Connection with Physical Emulsion Stability at Various pH Values and High Salt Concentrations.
Foods
November 2024
Laboratory of Food Process Engineering, Wageningen University and Research, Bornse Weilanden 9, 6708 WG Wageningen, The Netherlands.
The protein transition motivates the use of plant proteins, but their application in food emulsions is challenging, especially when high concentrations of oil and salt are needed for formulation and sensory properties. In the present work, we connect the iso-electric point of two potato protein isolates (patatin-rich, POPI-200; protease inhibitor-rich, POPI-300) and a faba protein isolate (FPI) to the behavior in the bulk phase and at the interface, and relate this to the physical stability of 45 wt% oil-in-water (O/W) emulsions in the presence of NaCl at pH 4.0-7.
View Article and Find Full Text PDFA new paradigm for optimized experimental design in cIEF platforms aimed at an accurate robust and reliable mAbs charge-variant assessment.
Sci Rep
November 2024
National Centre for the Control and Evaluation of Medicines (CNCF), Istituto Superiore di Sanità, Viale, Regina Elena 299, 00161, Rome, Italy.
The success of therapeutic monoclonal antibodies (mAbs) and their biosimilars, highlights the challenge to control their purity, identity, and stability. For this purpose, among several orthogonal methodologies, imaged capillary Iso Electric Focusing (icIEF) is one of the leading techniques. Despite the isoelectric point (pI) being a univocal parameter relying on the protein's primary sequence and its post-translational modifications (PTMs), the current Charge Variants Profile Assessment (CVPA) carried out by cIEF relies on relative comparisons with corresponding reference standards, this is because the inconsistent outputs for the same sample across different instruments preclude the uniqueness of the measured parameters.
View Article and Find Full Text PDFCharge heterogeneity of therapeutic monoclonal antibodies by different cIEF systems: views on the current situation.
MAbs
February 2024
National Centre for the Control and Evaluation of Medicines, Istituto Superiore di Sanità, Rome, Italy.
Therapeutic mAbs show a specific "charge fingerprint" that may affect safety and efficacy, and, as such, it is often identified as a critical quality attribute (CQA). Capillary iso-electric focusing (cIEF), commonly used for the evaluation of such CQA, provides an analytical tool to investigate mAb purity and identity across the product lifecycle. Here, we discuss the results of an analysis of a panel of antibody products by conventional and whole-column imaging cIEF systems performed as part of European Pharmacopoeia activities related to development of "horizontal standards" for the quality control of monoclonal antibodies (mAbs).
View Article and Find Full Text PDFAt present, enzyme immobilization is a big issue. It improves enzyme stability, activity, specificity, or selectivity, particularly the enantioselectivity compared to the native enzymes, and by solving the separation problem, it helps in recovering the catalyst with good reusability as desired in vitro. Motivated by these facts, in this work, Jack bean urease (JBU) is immobilized on three-dimensional (3D)-network silica gel (SG) via multipoint covalent bonding employing dimethyldichlorosilane (DMDCS) and -nitrophenol, respectively, as the second-generation silane-coupling reagent and spacer.
View Article and Find Full Text PDFConformational modifications of lysozyme caused by interaction with humic acid studied with spectroscopy.
Sci Total Environ
May 2021
College of Resources and Environment, Huazhong Agricultural University, Wuhan 430070, China. Electronic address:
Modification of enzyme/protein conformation will affect the activities and functionality of enzymes. Previous studies have shown that the activity of lysozyme (LSZ) in the presence of humic acid (HA) is largely determined by the mass ratio of HA/LSZ (f = mHA/mLSZ), pH and ionic strength. Here the interaction and conformation of LSZ in HA/LSZ-complex/aggregate (HA/LSZ-c/a) were investigated by spectroscopic techniques at (initial) pH 5 and 8 and ionic strength 5 mmol/L.
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