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peak fit 4 12 software  (SYSTAT)


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    Structured Review

    SYSTAT peak fit 4 12 software
    Peak Fit 4 12 Software, supplied by SYSTAT, used in various techniques. Bioz Stars score: 97/100, based on 1324 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/peak+fit+4+12/PeakFit+v4%2E12/10__1016_slash_j__foodhyd__2024__110959-125-9-12
    Average 97 stars, based on 1324 article reviews
    peak fit 4 12 software - by Bioz Stars, 2026-10
    97/100 stars

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    Article Title: Arthrospira cell residue valorization: A study on protein hydrolysate production by limited enzymatic hydrolysis
    Article Snippet: Arthrospira cell residue (ACR) is a byproduct of the spirulina industry that can be valorized into protein hydrolysates.. In this study, we used alkaline protease to hydrolyze ACR and evaluated the effects of hydrolysis time on the properties and functionalities of the hydrolysates.. We measured the degree of hydrolysis (DH), particle size, fluorescence, UV‒visible absorption, surface hydrophobicity, emulsification, solubility, and antioxidant activity of the hydrolysates.

    Article Title: Enhanced hydrophobicity of soybean protein isolate by low-pH shifting treatment for the sub-micron gel particles preparation
    Article Snippet: In the present study, the soybean protein isolate (SPI) was treated by pH shifting process, as the protein was incubated in low pH solutions (pH 1.5–3.5) for 12 h, following neutralized to pH 7.0 and held for 4 h, which resulted in a conformation unfolding/refolding confirmed by the fluorescence spectra and a substantial increase in α-helix content revealed by circular dichroism (CD) spectra, along with the increased exposure of hydrophobic and sulfhydryl groups.. In addition, the heat-induced gelation process and enhanced gel strength of pH 3.0 and 3.5 shifted SPIs were observed.. Maillard reaction was then applied and the glycosylated SPI was further applied to the sub-micron gel particles formation.

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    Article Title: Whey protein isolate nanofibrils formed with phosphoric acid: Formation, structural characteristics, and emulsion stability
    Article Snippet: In this study, phosphoric acid was used to replace hydrochloric acid which is widely reported in the production of whey protein isolate fibrils (WPF).. The pH, temperature, and protein concentration for the phosphoric acidinduced fibrillation were optimized (4% w/v, pH 2.5, 90 C).. Under this condition, the mean particle size and molecular weight decreased significantly while the ζ-potential increased slightly, it suggested that the fibrillation was accompanied by hydrolysis.

    Article Title: Effect of high intensity ultrasonic treatment on structural, rheological, and gelling properties of potato protein isolate and its co-gelation properties with egg white protein.
    Article Snippet: 1Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Comprehensive Key Laboratory of Agro-products Processing, Ministry of Agriculture and Rural Affairs, Beijing, China 2State Key Laboratory of Food Nutrition and Safety, Food Biotechnology Engineering Research Center of, Ministry of Education, College of food Science and Engineering, Tianjin University of Science & Technology, Tianjin, China

    Article Title: Molecular Spectroscopy Analysis of Different pH-Cycle Self-Assembly Between Rice Glutelin and Egg White Protein Under Neutral Conditions
    Article Snippet: Self-assembly and molecular spectroscopy are widely used in protein research.. However, studies underreported the interaction of rice glutelin (RG) and egg white protein (EWP) under pH-cycle treatments, which had differences between initial and final environment.. Herein, the possible interaction mechanism of RG-EWP self-assembly behavior was demonstrated by spectroscopy or other characterization methods under different conditions and proportions.

    Article Title: Effects of ultrasound combined with pH shift modification on functional and structural properties of peanut proteins.
    Article Snippet: The parameters for ultrasound and pH shift co-modification of peanut proteins (PP) were optimized, and the functional properties, structures of PP were investigated.. The results showed that under the optimum ultrasoundassisted pH-shift modification (UP-PPI), the solubility of PP increased by 40.5 % and 111.4 %, respectively, compared with the pH shift (pH-PPI) and the control (D-PPI).. The emulsifying and foaming properties of pH-PPI and UP-PPI were significantly (P < 0.05) higher than those of D-PPI. pH shift reduced the particle size of D-PPI from 805.14 ± 13.80 nm to 563.73 ± 35.92 nm, and ultrasound further enhanced this process, with a sizer of 392.67 ± 7.81 nm while increasing the absolute value of zeta potential.

    Article Title: Structural Characterization and Pro-inflammatory Activity of a Thaumatin-Like Protein from Pulp Tissues of Litchi chinensis
    Article Snippet: Subscriber access provided by Uppsala universitetsbibliotek is published by the American Chemical Society.. 1155 Sixteenth Street N.W., Washington, DC 20036 Published by American Chemical Society.. Copyright © American Chemical Society.

    Analysis:

    Article Title: Structural Characterization and Pro-inflammatory Activity of a Thaumatin-Like Protein from Pulp Tissues of Litchi chinensis
    Article Snippet: Subscriber access provided by Uppsala universitetsbibliotek is published by the American Chemical Society.. 1155 Sixteenth Street N.W., Washington, DC 20036 Published by American Chemical Society.. Copyright © American Chemical Society.



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