5303a2740f144771c9f56d85bd3f70b3 dairy-03-00036.pdf 638fa40a2601edc43be8790c6e88a619184fea95 dairy-03-00036.pdf c8bf2a3798d0eb3bb4a5c293f987a96a4295d19e8d45178f024de8e509b3893f dairy-03-00036.pdf Title: Thermal Denaturation of Milk Whey Proteins: A Comprehensive Review on Rapid Quantification Methods Being Studied, Developed and Implemented Subject: Heat treatment of milk signifies a certain degree of protein denaturation, which modifies the functional properties of dairy products. Traditional methods for detecting and quantifying the denaturation of whey proteins are slow, complex and require sample preparation and qualified staff. The world’s current trend is to develop rapid, real-time analytical methods that do not destroy the sample and can be applied on/in-line during processing. This review presents the rapid methods that are being studied, developed and/or applied to determine and quantify the thermal denaturation of whey proteins, including spectroscopic, electrochemical and miniaturized methods. The selected methods save a significant amount of time and money compared to the traditional ones. In addition, the review emphasizes the methods being applied directly to milk and/or that have potential for on/in/at-line application. There are interesting options to quantify thermal denaturation of whey proteins such as biosensors, nanosensors and microchips, which have fast responses and could be automated. In addition, electrochemical sensors are simple to use and portable, while spectroscopy alternatives are suitable for on/in/at-line process. Keywords: whey proteins; denaturation; heat treatment; rapid method; on-line; in-line Author: Paulina Freire, Allison Zambrano, Anna Zamora and Manuel Castillo Creator: LaTeX with hyperref Producer: pdfTeX-1.40.21 CreationDate: Mon Jul 18 13:12:38 2022 CEST ModDate: Mon Jul 18 13:21:40 2022 CEST Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 13 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 2159753 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- HQWIKS+VnURWPalladioL Type 1 Custom yes yes no 10 0 QFXGAU+URWPalladioL-Bold Type 1 Custom yes yes no 15 0 QDCQKG+URWPalladioL-Roma Type 1 Custom yes yes no 20 0 ZBGHIY+URWPalladioL-Ital Type 1 Custom yes yes no 24 0 ZBJSWP+CMSY10 Type 1 Builtin yes yes no 28 0 WRDQLY+EURM10 Type 1 Builtin yes yes no 32 0 BCDEEE+PalatinoLinotype-Bold TrueType WinAnsi yes yes no 86 0 BCDFEE+PalatinoLinotype-Roman TrueType WinAnsi yes yes no 90 0 BCDGEE+PalatinoLinotype-Italic TrueType WinAnsi yes yes no 94 0 BCDHEE+PalatinoLinotype-Roman CID TrueType Identity-H yes yes yes 98 0 BCDEEE+PalatinoLinotype-Bold TrueType WinAnsi yes yes no 114 0 BCDFEE+PalatinoLinotype-Roman TrueType WinAnsi yes yes no 118 0 BCDGEE+PalatinoLinotype-Italic TrueType WinAnsi yes yes no 122 0 BCDHEE+PalatinoLinotype-Roman CID TrueType Identity-H yes yes yes 126 0 BCDEEE+PalatinoLinotype-Bold TrueType WinAnsi yes yes no 142 0 BCDFEE+PalatinoLinotype-Roman TrueType WinAnsi yes yes no 146 0 BCDGEE+PalatinoLinotype-Italic TrueType WinAnsi yes yes no 150 0 BCDHEE+PalatinoLinotype-Roman CID TrueType Identity-H yes yes yes 154 0 GKCFOK+URWPalladioL-BoldItal Type 1 Custom yes yes no 166 0 BCDEEE+PalatinoLinotype-Bold TrueType WinAnsi yes yes no 174 0 BCDFEE+PalatinoLinotype-Roman TrueType WinAnsi yes yes no 178 0 BCDGEE+PalatinoLinotype-Italic TrueType WinAnsi yes yes no 182 0 BCDHEE+PalatinoLinotype-Roman CID TrueType Identity-H yes yes yes 186 0 ArialMT TrueType WinAnsi no no no 193 0 BCDJEE+PalatinoLinotype-BoldItalic TrueType WinAnsi yes yes no 196 0 BCDEEE+PalatinoLinotype-Bold TrueType WinAnsi yes yes no 209 0 BCDFEE+PalatinoLinotype-Roman TrueType WinAnsi yes yes no 213 0 BCDGEE+PalatinoLinotype-Italic TrueType WinAnsi yes yes no 217 0 BCDHEE+PalatinoLinotype-Roman CID TrueType Identity-H yes yes yes 221 0 ArialMT TrueType WinAnsi no no no 228 0 BCDJEE+PalatinoLinotype-BoldItalic TrueType WinAnsi yes yes no 231 0 BCDEEE+PalatinoLinotype-Bold TrueType WinAnsi yes yes no 244 0 BCDFEE+PalatinoLinotype-Roman TrueType WinAnsi yes yes no 248 0 BCDGEE+PalatinoLinotype-Italic TrueType WinAnsi yes yes no 252 0 BCDHEE+PalatinoLinotype-Roman CID TrueType Identity-H yes yes yes 256 0 BOLMEN+SFRM0900 Type 1 Custom yes yes no 270 0 Jhove (Rel. 1.22.1, 2019-04-17) Date: 2022-12-01 02:31:16 CET RepresentationInformation: dairy-03-00036.pdf ReportingModule: PDF-hul, Rel. 1.12.1 (2019-04-17) LastModified: 2022-11-08 11:03:26 CET Size: 2159753 Format: PDF Version: 1.7 Status: Well-Formed and valid SignatureMatches: PDF-hul MIMEtype: application/pdf PDFMetadata: Objects: 475 FreeObjects: 1 IncrementalUpdates: 0 DocumentCatalog: PageLayout: SinglePage PageMode: UseNone Outlines: Item: Title: Introduction Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@4923ab24 Item: Title: Rapid Methods for Determining the Thermal Denaturation of Whey Proteins in Milk Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@44c8afef Children: Item: Title: Biosensors, Nanosensors and Microchips Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@7b69c6ba Item: Title: Electrochemical Sensors Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@46daef40 Item: Title: Spectroscopy Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@12f41634 Children: Item: Title: Infrared Spectroscopy (from 780 to 50,000 nm) Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@13c27452 Item: Title: UV-Visible Spectroscopy Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@262b2c86 Item: Title: Conclusions Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@371a67ec Item: Title: References Destination: edu.harvard.hul.ois.jhove.module.pdf.PdfSimpleObject@5ed828d Info: Title: Thermal Denaturation of Milk Whey Proteins: A Comprehensive Review on Rapid Quantification Methods Being Studied, Developed and Implemented Author: Paulina Freire, Allison Zambrano, Anna Zamora and Manuel Castillo Subject: Heat treatment of milk signifies a certain degree of protein denaturation, which modifies the functional properties of dairy products. Traditional methods for detecting and quantifying the denaturation of whey proteins are slow, complex and require sample preparation and qualified staff. The world’s current trend is to develop rapid, real-time analytical methods that do not destroy the sample and can be applied on/in-line during processing. This review presents the rapid methods that are being studied, developed and/or applied to determine and quantify the thermal denaturation of whey proteins, including spectroscopic, electrochemical and miniaturized methods. The selected methods save a significant amount of time and money compared to the traditional ones. In addition, the review emphasizes the methods being applied directly to milk and/or that have potential for on/in/at-line application. There are interesting options to quantify thermal denaturation of whey proteins such as biosensors, nanosensors and microchips, which have fast responses and could be automated. In addition, electrochemical sensors are simple to use and portable, while spectroscopy alternatives are suitable for on/in/at-line process. 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