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TA Instruments universal analysis 2000 version 4.1d
Universal Analysis 2000 Version 4.1d, supplied by TA Instruments, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/universal+analysis+2000+version+4%2E1d/universal+analysis+2000+software/pm36029675-77-5-10
Average 90 stars, based on 1 article reviews
universal analysis 2000 version 4.1d - by Bioz Stars, 2026-10
90/100 stars

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Article Title: Structure and thermal properties of arachin from six varieties: effect of 35.5 kDa subunit
Article Snippet: The initial denaturation temperature (Tonset), midpoint denaturation temperature (Td value) and the amount of heat flow (enthalpy of transition, ΔH) were determined from the thermograms by the accompanied software (Universal Analysis 2000, Version 4.1D, TA Instruments– Waters LLC).

Article Title: Pea, Chickpea and Lentil Protein Isolates: Physicochemical Characterization and Emulsifying Properties
Article Snippet: This work is focused on physicochemical and emulsifying properties of pea (PP), chickpea (CP) and lentil (LP) proteins.. We evaluated the molecular weight distributions, surface net charge, free sulfhydryl group (SH) and disulfide bond (SS) contents, protein solubility and thermal stability of the protein isolates.. Their emulsifying properties (droplet size distribution, flocculation, coalescence and creaming) were also determined as function of pH values.

Article Title: Nanocomplexation between curcumin and soy protein isolate: influence on curcumin stability/bioaccessibility and in vitro protein digestibility.
Article Snippet: Journal of Agricultural and Food Chemistry is published by the American Chemical Society.. 1155 Sixteenth Street N.W., Washington, DC 20036 Published by American Chemical Society.. Copyright © American Chemical Society.

Article Title: Microfluidization as a potential technique to modify surface properties of soy protein isolate
Article Snippet: Contents lists available at SciVerse ScienceDirect Food Research International j ourna l homepage: www.e lsev ie r .com/ locate / foodres Microfluidization as a potential technique to modify surface properties of soy protein isolate Lan Shen a, Chuan-He Tang a,b,⁎ a Department of Food Science and Technology, South China University of Technology, Guangzhou 510640, People's Republic of China b State Key Laboratory of Pulp and Paper Engineering, South China University of Technology, Guangzhou 510640, People's Republic of China ⁎ Corresponding author at: Department of Food Sc China University of Technology, Guangzhou 510640 Tel.. +86 20 87111707; fax: +86 20 87114263.. E-mail address: chtang@scut.edu.cn (C.-H. Tang).

Article Title: Benzisoxazole derivative
Article Snippet: The data analysis was carried out with Universal Analysis 2000 Version 4.1D (TA Instruments, New Castle, Del., USA).

Article Title: Structure–physicochemical function relationships of 7S globulins (vicilins) from red bean (Phaseolus angularis) with different polypeptide constituents
Article Snippet: Red bean 7S globulins (vicilins) with different polypeptide constituents or heterogeneity were fractionated using acidic extraction (at 0.5 M NaCl) and anion-exchange column chromatography.. The physicochemical and conformational properties, including amino acid composition, net charge and/or surface hydrophobicity (H0), protein solubility (PS), thermal and emulsifying properties, as well as secondary, tertiary and/or quaternary conformations, were evaluated.. There were distinct differences in zeta potential, H0, DSC characteristics, emulsifying activities and tertiary and/or quaternary conformations among the vicilins with different polypeptide constituents, but the PS and secondary conformation were slightly different.

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Article Title: Dithiothreitol-induced reassembly of soybean lipophilic protein as a carrier for resveratrol: Preparation, structural characterization, and functional properties.
Article Snippet: We employed dithiothreitol (DTT) to reassemble soy lipophilic protein (LP) and increased its solubility for encapsulating resveratrol (Res); we subsequently added hydroxypropyl methylcellulose (HPMC) to further stabilize Res.. Physicochemical characterization, sodium dodecyl sulfate–polyacrylamide gel electrophoresis, and spectral analysis revealed that DTT triggered the breakage and reassembly of the disulfide bond.. Consequently, the solubility of LP increased from 38.64 % to 71.49 %, and the number of free sulfhydryl groups increased to 7.84 mol⋅g 1.



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