BEGIN:VCALENDAR VERSION:2.0 PRODID:-//CERN//INDICO//EN BEGIN:VEVENT SUMMARY:Panel discussion DTSTART;VALUE=DATE-TIME:20210610T124500Z DTEND;VALUE=DATE-TIME:20210610T140000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1116@lindico453.srv.lu.se DESCRIPTION:Moderator: Pia Kinhult\, ESS\n\nPanel: Elisabet Nielsen (Vinno va)\, Johanna van Schaik Dernfalk (Formas)\, Carina Knorpp (Näringsdepart ementet)\, Rickard Öste (Aventure/Oatly)\, Tommy Nylander (LU-LINXS)\n\nh ttps://lindico453.srv.lu.se/event/159/contributions/1116/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1116/ END:VEVENT BEGIN:VEVENT SUMMARY:Keynote talk - The hidden structures of the processed plant foods DTSTART;VALUE=DATE-TIME:20210611T074000Z DTEND;VALUE=DATE-TIME:20210611T081000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1118@lindico453.srv.lu.se DESCRIPTION:Speakers: Ramune Kuktaite (Swedish University of Agricultural Sciences\, Sweden)\nProtein-rich cereals and legumes such as\, quinoa\, wh eat and lupin\, during latest years have got a lot of attention in food se ctor because of their potential to substitute imported soy. Quinoa seeds o riginating from the Andean region are known for its superior nutritional c haracteristics that include attractive amino acid composition\, vitamins a nd minerals\, highly suitable for development of innovative foods. While l upin\, in a form of isolates and concentrates (Muranyi et al. 2016)\, and wheat gluten protein gliadin\, due to its ability to deliver different fun ctionalities and structures (Kuktaite et al. 2016\; Muneer et al. 2016)\, can be suitable ingredients in developing new food products. The study is focusing on investigating micro-/and nano-structures and properties of pro teins (but also starch and fibers) in quinoa flour\, lupin protein isolate s and gliadins transformed into different foods/fibers using various proce ssing methods (Kuktaite et al. 2021\; Ceresino et al. 2020\; 2021\; unpubl ished results). The structures resolved using scattering techniques such a s\, SAXS\, WAXS in combination with X-ray tomography\, SEM\, FTIR and HPLC \, elucidated new interactions between the proteins (and other seed compon ents) and food grade additives\, not previously observed in the processed foods. From the main results\, the synergistic interactions of gliadin and linoleic acid led to the formation of lamellar structures in the foams ob served by SAXS (Ceresino et al. 2020). While in the lupin foams\, a hexago nal arrangement 1: √3 was observed by SAXS in the presence of lecithin i n the blend (Ceresino et al. 2021). \nWith this study we conclude\, that t he plant protein and other components structures in the studied cereal and legume food/fiber products can be more influenced when the additives and more refined proteins (e.g. isolates) are used compared with the whole flo ur.\n\nhttps://lindico453.srv.lu.se/event/159/contributions/1118/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1118/ END:VEVENT BEGIN:VEVENT SUMMARY:Keynote talk - Structuring foods by proteins and their supramolecu lar aggregates: the critical role of complementary techniques to observe s tructure dynamics in relevant environments. DTSTART;VALUE=DATE-TIME:20210611T070000Z DTEND;VALUE=DATE-TIME:20210611T074000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1117@lindico453.srv.lu.se DESCRIPTION:Speakers: Milena Corredig (Aarhus University\, Denmark)\nThere is an increased need to change the way we manufacture foods to achieve ca rbon-neutral value chains. This may include the use of new ingredients fro m less known sources\, fine tune processing conditions and formulations\, and closely control the formation of structure to avoid overprocessing or to optimize the nutritional functionality of the food. A few systems hav e been studied in great detail at various length scales\, and have demonst rated how it is possible to provide useful information by designing experi mental environments as close as possible to relevant processes. \nThis pr esentation will review some examples of successful application of non disr uptive\, in situ studies using X-ray and neutrons that may serve as inspi ration for future work on novel food systems. We will point out to some of the challenges we face when studying the formation of structures in compl ex environments\; furthermore\, the importance of a multidisciplinary effo rt in studying these food systems in their complexity can not be stressed enough\, as a full characterization of the samples and their structuring d ynamics using complementary traditional techniques is often needed.\n\nhtt ps://lindico453.srv.lu.se/event/159/contributions/1117/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1117/ END:VEVENT BEGIN:VEVENT SUMMARY:Keynote talk - Structuring Oils via Enzymatic Glycerolysis DTSTART;VALUE=DATE-TIME:20210609T132000Z DTEND;VALUE=DATE-TIME:20210609T140000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1104@lindico453.srv.lu.se DESCRIPTION:Speakers: Alejandro Marangoni (University of Guelph\, Canada)\ nCurrent trans fat replacement strategies provide food products with accep table textural and sensory properties on a large scale\, and at a reasonab le price\, but carry health and environmental burdens. Palm oil is used ex tensively because of its high solidity and functionality\, however\, incre ased production has led to deforestation throughout the world’s tropical regions. To reduce dependence on palm oil it is necessary to find a means of structuring a variety of readily available vegetable oils. Using cotto nseed and peanut oils\, and another 8 oils\, we show that enzymatic glycer olysis can structure liquid oils into solids fats through monoacylglycerol and diacylglycerol production from their native triacylglycerols without the addition of saturated or hydrogenated fat\, thus not altering fatty ac id composition. Solid fat contents of cottonseed and peanut oils\, for exa mple\, were increased from 8% to 29% and 9% to 30% at 5°C\, respectively\ , and 21% and 10% at 20°C\, respectively. Additionally\, oil-binding cap acity was enhanced significantly. These novel oils were used to produce ma rgarine and peanut butter with similar textural properties to commercial p roducts but\, importantly\, represent a healthy and sustainable means to r eplace hydrogenated or saturated fats.\n\nhttps://lindico453.srv.lu.se/eve nt/159/contributions/1104/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1104/ END:VEVENT BEGIN:VEVENT SUMMARY:Francisco Vilaplana - KTH - Hemicelluloses: Molecular structure\, assembly in plant cell walls and food applications DTSTART;VALUE=DATE-TIME:20210610T084000Z DTEND;VALUE=DATE-TIME:20210610T090000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1111@lindico453.srv.lu.se DESCRIPTION:Plant cell walls constitute the main renewable resource for th e development of bio-based energy and materials\, and they are a fundament al source of dietary fibre in our diets (e.g. in\ncereals\, pulses\, fruit s and vegetables). The heterogeneity and recalcitrance of plant cell walls is fundamental to the biological function\, but these pose large challeng es for their exploitation\nin material and nutritional applications. Plant cell walls constitute a fascinating biological material with controlled h ierarchical organization from the molecular to the macroscopic level\,\nco nsisting mainly of polysaccharides (cellulose\, hemicelluloses and pectins )\, proteins and polyphenolic compounds. Hemicelluloses act as a link betw een the cellulose\, protein and\nphenolic components in cell walls and reg ulate the aggregation of cellulose microfibrils. Hemicelluloses are a fami ly of complex biopolymers with a b-(1®4) backbone of neutral sugars\n(glu cose\, xylose and mannose)\, but decorated with an array of neutral sugar and uronic acid substitutions and can be chemically-modified by acetylatio n. In this presentation we will cover the recent advances in understanding the molecular structure of hemicelluloses and their role in the organizat ion of plant cell walls\, with a focus on cereal cell walls. This requires the combination of advanced biochemical methods based on mass spectrometr y\, with solid-state biophysical approaches\, including small angle scatte ring techniques. This fundamental\ninformation on the structure and assemb ly of hemicelluloses can be used for the development of new sustainable pr ocesses for their extraction and their subsequent use in functional food\n ingredients with tailored properties and structures. This can be directly applied to the valorization of by-products from the agricultural sector (e .g. cereal bran and fruit pulps)\, which\nconstitute a rich source of diet ary fibres with bioactive properties for their engineering in new food pro ducts.\n\nhttps://lindico453.srv.lu.se/event/159/contributions/1111/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1111/ END:VEVENT BEGIN:VEVENT SUMMARY:Contr. talk - Understanding gelation of gluten proteins thanks to neutron and X-ray scattering DTSTART;VALUE=DATE-TIME:20210610T080000Z DTEND;VALUE=DATE-TIME:20210610T082000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1110@lindico453.srv.lu.se DESCRIPTION:Speakers: Laurence Ramos ()\nThe origin of the unique rheologi cal properties of wheat gluten\, the water-insoluble protein fraction of w heat grain\, is crucial in bread-making processes and questions scientists since the 18th\ncentury. Gluten is a complex mixture of two families of p roteins\, monomeric gliadins (Gli) and polymeric glutenins (Glu). To bette r understand the respective role of the different classes of proteins in t he supramolecular structure of gluten and its link to the material propert ies\, we have developed model gluten systems comprising controlled amounts of Gli and Glu in food-grade binary solvents [1]. Using contrast variatio n techniques and small-angle neutron scattering\, we have evidenced in\ngl uten gels the presence of distinct regions of typical size several tens of nm\, which arise from the preferential interaction of Glu polymers throug h a tight network of non-exchangeable intermolecular hydrogen bonds\, at t he origin of the gelation of gluten [3]. In addition\, we have used time-r esolved synchrotron ultra-small X-ray scattering to quantitatively probe t he dynamics of liquid-liquid phase separation (LLPS) in gluten protein sus pensions following a temperature quench [4]. Fluid viscoelastic samples de pleted in polymer Glu phase separate\nfollowing a spinodal decomposition p rocess\, with a coarsening resulting from a competition between thermodyna mics and transport. Anomalous phase-separation dynamics is by contrast mea sured for gluten gels rich in Glu\, due to elastic constraints\, illustrat ing the role of viscoelasticity in the dynamics of LLPS in protein dispers ions. Additional experiments conducted by changing the solvent\, from pure water (a bad solvent for gluten proteins) to ethanol/water (60/40 v/v) (a good solvent for gluten proteins) confirm the subtle interplay between ph ase-separation and viscoelasticity in gluten proteins gels [5].\n[1] Dahes h et al. Polymeric assembly of gluten proteins in an aqueous ethanol solve nt. J Phys Chem B 118\, 11065 (2014).\n[2] Banc et al. Small angle neutron scattering contrast variation reveals heterogeneities of interactions in protein gels. Soft Matter 12\, 5340 (2016).\n[3] Dahesh et al. Spontaneous gelation of wheat gluten proteins in a food grade solvent. Food Hydrocoll oids\, 52\, 1 (2016).\n[4] Banc et al. Phase separation dynamics of gluten protein mixtures. Soft Matter 15\, 6160 (2019).\n[5] Costanzo et al. Tail oring the viscoelasticity of polymer gels of gluten proteins through solve nt quality. Submitted (2020)\n\nhttps://lindico453.srv.lu.se/event/159/con tributions/1110/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1110/ END:VEVENT BEGIN:VEVENT SUMMARY:Contr. talk - Towards Correlative X-Ray Tomographic Imaging Of Mem branes For Improving Food Processing DTSTART;VALUE=DATE-TIME:20210610T074000Z DTEND;VALUE=DATE-TIME:20210610T080000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1109@lindico453.srv.lu.se DESCRIPTION:Speakers: Emanuel Larsson (Division of Solid Mechanics & LUNAR C\, Faculty of Engineering\, Lund University)\, Gregor Rudolph (Department of Chemical Engineering\, Lund University)\nIn recent years the need for shifting our food system towards more plant-based proteins has become more and more apparent. The key reason for this shift is the economic and sust ainable recovery of plant proteins from valuable\, yet underutilized agric ultural waste streams for use in food\napplications. For highly selective energy and resource-efficient separation processes\, membrane filtration c an play an important role in realizing this shift. \nThe first successful membrane technology in the food industry was the recovery of proteins from whey\, which was until the 1970’s a major disposal challenge for the da iry industry. Using ultrafiltration (UF) membranes\, it was suddenly possi ble to concentrate and desalt whey proteins. Based on this success story\, membrane processes established themselves for the concentration and purif ication of many products in the food industry. However\, clogging of the m embrane during the filtration process\, so-called membrane fouling\, is st ill a major challenge.\nMembrane fouling alters the separation performance during operation. It may be caused by the deposition of suspended and dis solved substances on the membrane surface\, thereby forming a cake or gel layer\, thus blocking the pore openings\, or causing adsorption on the sur face and on the pore walls. Membrane fouling can only be overcome by regul ar chemical cleaning\, which in turn leads to plant down time\, membrane a ging\, consumption of high-quality drinking water and the generation of hu ge amounts of waste water. \nThus\, a comprehensive understanding on membr ane fouling on a fundamental level is needed. One approach to generate in depth knowledge\, is to examine changes due to fouling and cleaning of the inner structure of the membranes on a micrometer to nanometer scale using correlative X-ray tomographic imaging techniques\, including microtomogra phy\, full-field nanotomography\, holographic nanotomography and ptycho-to mography. This presentation will give an overview\nof the possibilities of X-ray tomographic imaging methods for membrane technology to improve the operation of membrane processes in the food industry More specifically an example of UF for the separation of rapeseed proteins from the press cake of the rapeseed oil production will be presented\, including the need for sample preparation by Focused Ion Beam (FIB).\n\nhttps://lindico453.srv.lu .se/event/159/contributions/1109/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1109/ END:VEVENT BEGIN:VEVENT SUMMARY:Contr. talk - Comparative X-ray microtomography and SEM to investi gate the encapsulating matrix of freeze-dried probiotics DTSTART;VALUE=DATE-TIME:20210609T140000Z DTEND;VALUE=DATE-TIME:20210609T142000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1105@lindico453.srv.lu.se DESCRIPTION:Speakers: Shuai Bai (Lunds universitet)\nThe health effects of probiotics are exerted by live and viable microorganisms delivered to the ir site of action in the intestine. Thus\, formulating a probiotic product that ensures viable cells with long shelf life is one of the main challen ges for the industry. A common way to enhance the shelf life is to freeze dry the probiotics with lyo-protectants\, and a large research effort is d irected towards finding the best lyo-protectant formulation and drying pro cess. Unfortunately\, there is almost no focus on how the structure of the freeze dried material can influence the shelf life. Traditional pharmaceu tical formulations often demand elegant porous freeze dried cake without c ollapse. This kind\nof freeze dried materials often have thin walls and re sult in a poor encapsulation of the cells\, which may be detrimental for t he stability. The study to be presented aims at understanding how the form ulation and drying process together influence the three-dimensional struct ure of the freeze-dried material and the cell encapsulation. X-ray micro t omography (μCT) is an excellent tool to study freeze-dried material\, inc luding the impact of various freeze-drying protocols\, by generating a thr ee-dimensional image\, which can be used for further investigating quantit ative 3D-parameters\, e.g. the pore size\, pore connectivity\, wall thickn ess and tortuosity at a sub-micrometer resolution.\nHere\, μCT is combine d with Scanning Electron Microscopy (SEM) and analysis of the specific sur face area to give a broader understanding of the structure development and how this is reflected in mass transfer resistance during drying and encap sulation of the bacterial cells.\n\nhttps://lindico453.srv.lu.se/event/159 /contributions/1105/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1105/ END:VEVENT BEGIN:VEVENT SUMMARY:Contr. talk - Dephosphorylation of the casein micelle DTSTART;VALUE=DATE-TIME:20210609T142000Z DTEND;VALUE=DATE-TIME:20210609T144000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1106@lindico453.srv.lu.se DESCRIPTION:Speakers: Thea Lykkegaard Møller (Department of Food Science\ , Aarhus University)\nDephosphorylation of caseins has been evaluated on t heir monomeric forms\, and dephosphorylation extents up to nearly 100% hav e been reported. However\, the effect of dephosphorylation on casein micel les has yet to be fully understood. The aim of this work is to study the d ephosphorylation of the native casein micelle under native\nand dissociati ng conditions to determine the kinetics of micellar dephosphorylation and to study the micellar structure as a function of its phosphorylation degre e. We hypothesize that the structure of the casein micelle is the limiting factor when enzymatically dephosphorylating it. To test the hypothesis\, dephosphorylation\, by Calf Intestinal Phosphatase and Potato Acid Phospha tase\, is conducted under varying conditions\, and the degree of dephospho rylation compared. The structural changes affecting the micelle are then e valuated by determining differences in micellar protein composition\, part icle size by light scattering\, and structural analysis using SAXS\, to st udy possible changes to the outer and inner structure of the casein micell e before and after dephosphorylation treatment. This work allows to furthe r elucidate the organization of the casein micelle\, by determining the ac cessibility of the enzyme within the supramolecular structure\, and under which conditions we see specific changes in the pattern of dephosphorylati on.\n\nhttps://lindico453.srv.lu.se/event/159/contributions/1106/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1106/ END:VEVENT BEGIN:VEVENT SUMMARY:Contr. talk - Study on Bending of Laminar Packaging Material from Tetra Pak DTSTART;VALUE=DATE-TIME:20210609T125000Z DTEND;VALUE=DATE-TIME:20210609T131000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1103@lindico453.srv.lu.se DESCRIPTION:Speakers: Behnaz Pirzamanbein (Technical University of Denmark (DTU) & Lund University)\nhttps://lindico453.srv.lu.se/event/159/contribu tions/1103/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1103/ END:VEVENT BEGIN:VEVENT SUMMARY:Arla Foods\, Denmark - Scale of the Problem DTSTART;VALUE=DATE-TIME:20210610T120000Z DTEND;VALUE=DATE-TIME:20210610T123000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1115@lindico453.srv.lu.se DESCRIPTION:Speakers: Peter L. Wejse (Arla\, Denmark)\nMost foods are inhe rently complex due to their biological origin. They are chemically and phy sically organised at a vast range of length scales. Much of our current un derstanding of food\ncharacteristics stem from simplified systems and food models as well as from highly controlled laboratory experiments. Such kno wledge is invaluable when developing new food products as well as for impr oving and troubleshooting excisting production processes. However\, extrap olating the knowledge from such simplified systems into truly understandin g and describing real world applications leaves a lot of room for improvem ent. Examplified by milk fat crystallisation and casein micelle structural dynamics and their influence on dairy foods' rheological functionality ch allenges are lined up showcasing the scales of time\, size and complexity that needs to be adressed to truly understand and control food production. \n\nhttps://lindico453.srv.lu.se/event/159/contributions/1115/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1115/ END:VEVENT BEGIN:VEVENT SUMMARY:Contr. talk - What neutrons tell us about meat analogues DTSTART;VALUE=DATE-TIME:20210611T083000Z DTEND;VALUE=DATE-TIME:20210611T085000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1142@lindico453.srv.lu.se DESCRIPTION:Speakers: Wim Bouwman (Delft University of Technology\,)\nFor a rational redesign of the production of meat analogues one should underst and the formation kinetics of a good texture. Neutron scattering yields al l kind of information on the bulk of the meat analogues. We used several n eutron techniques to characterise these materials. We performed most measu rements on calcium caseinate based meat replacements [1]. Quasi-elastic ne utron scattering has showed the importance of the molecular mobility of th e proteins [2]. Small-angle neutron scattering has showed at which length scale the orientation of the fibres goes from isotropic to aligned. With n eutron refraction the air bubbles in meat analogues have been quantified \ n[3]. This knowledge will help to further improve the methods for meat ana logues production. The holy grail in this research is now to apply these m ethods in situ while processing the materials.\n1. B.Tian\, V. Garcia Saka i\, C.P. Pappas\, A.J. van der Goot\, W.G. Bouwman Chemical Engineering Sc ience 207 1270-1277 (2019)\n2. B.Tian\, Z. Wang\, L. de Campo\, E.P. Gilbe rt\, R.M. Dalgliesh\, E. Velichko\, A.J. van der Goot\, W.G. Bouwman\nFood Hydrocolloids 106 105912 (2020)\n3. B.Tian\, Z. Wang\, A.J. van der Goot\ , W.G. Bouwman\nFood Hydrocolloids 83 287-295 (2018)\n\nhttps://lindico453 .srv.lu.se/event/159/contributions/1142/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1142/ END:VEVENT BEGIN:VEVENT SUMMARY:Keynote talk - The potential of small angle scattering to study th e structure of polysaccharide-based gels DTSTART;VALUE=DATE-TIME:20210609T115000Z DTEND;VALUE=DATE-TIME:20210609T122000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1101@lindico453.srv.lu.se DESCRIPTION:Speakers: Marta Martínez Sanz (CIAL-CSIC\, Madrid\, Spain)\n Polysaccharides are of great interest within the food industry\, not only because they are the major component in foods such as fruits and vegetable s\, but also because they play a crucial role as food additives to provide different functionalities (e.g. thickeners\, gelling agents\, emulsifiers \, etc.). In particular\, seaweed polysaccharides such as agar\, carrageen an and alginate\, are widely used as gelling and thickening agents. These polysaccharides are water-soluble and under certain conditions can form hi ghly hydrated gel structures known as hydrogels. Despite their great inter est in the food industry\, the native structure of these polysaccharide hy drogels and their gelation mechanisms are still not fully understood. Scat tering techniques offer a great advantage over other characterization meth ods since they require minimal sample preparation\, avoiding the severe st ructural alterations induced by drying processes\, and allow the carrying out of temperature-resolved experiments to investigate the structural chan ges taking place during gelation and melting processes.\n\nIn this talk\, relevant results on the structure of seaweed polysaccharide-based hydrogel s aimed for different food-related applications will be presented\, showin g the potential of combining small angle scattering techniques (SAXS and S ANS) with complementary methods such as rheology\, spectroscopy and micros copy. For instance\, through SANS contrast variation and temperature-resol ved SAXS experiments\, the step-wise mechanism driving the gelation proces s in different agar-based extracts was elucidated\, determining the effect of their composition (i.e. the presence of other components such as prote ins and minerals) and molecular structure (i.e. molecular weight\, agarose content and sulphate content)\, as well as the implications on their rheo logical and mechanical properties. Another example is related to the study of the structure of -\, ɩ- and λ-carragenaan hydrogels and the relat ionship with their texture and rheological behavior. By selecting the suit able type of carragenaan and adjusting the salt content\, it was possible to produce hydrogels with very different textures\, i.e. from spreadable p astes to strong gels. Agar and carrageenans were also used as gelling matr ices for the development of emulsion-filled gels with potential as fat sub stitutes in food. The use of small angle scattering techniques was essenti al to unravel the structural role of polysaccharides in these novel struct ures and understand their rheological behavior.\n\nThese results demonstra te the potential of small angle scattering techniques\, especially when co mbined with complementary methods\, to provide valuable insights on the st ructure of polysaccharide-based hydrogels\, enabling the rational design o f new food additives with interesting functionalities for a wide range of applications.\n\nhttps://lindico453.srv.lu.se/event/159/contributions/1101 / LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1101/ END:VEVENT BEGIN:VEVENT SUMMARY:Student speed dating - Session chair Milena Corredig & Thea Lykkeg aard Møller (Aarhus University) DTSTART;VALUE=DATE-TIME:20210609T151000Z DTEND;VALUE=DATE-TIME:20210609T160000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1122@lindico453.srv.lu.se DESCRIPTION:https://lindico453.srv.lu.se/event/159/contributions/1122/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1122/ END:VEVENT BEGIN:VEVENT SUMMARY:Application and Science Pitch DTSTART;VALUE=DATE-TIME:20210610T094000Z DTEND;VALUE=DATE-TIME:20210610T101500Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1121@lindico453.srv.lu.se DESCRIPTION:https://lindico453.srv.lu.se/event/159/contributions/1121/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1121/ END:VEVENT BEGIN:VEVENT SUMMARY:Maria Öhman – Vinnova DTSTART;VALUE=DATE-TIME:20210610T092000Z DTEND;VALUE=DATE-TIME:20210610T094000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1120@lindico453.srv.lu.se DESCRIPTION:https://lindico453.srv.lu.se/event/159/contributions/1120/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1120/ END:VEVENT BEGIN:VEVENT SUMMARY:NIZO\, the Netherlands - Title: Neutron scattering and food scienc e: results and ideas DTSTART;VALUE=DATE-TIME:20210610T113000Z DTEND;VALUE=DATE-TIME:20210610T120000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1114@lindico453.srv.lu.se DESCRIPTION:Speakers: Hans Tromp (NIZO\, The Netherlands)\nhttps://lindico 453.srv.lu.se/event/159/contributions/1114/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1114/ END:VEVENT BEGIN:VEVENT SUMMARY:RISE - Enlight industrial food research questions with xray and ne utron techniques DTSTART;VALUE=DATE-TIME:20210610T110000Z DTEND;VALUE=DATE-TIME:20210610T113000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1113@lindico453.srv.lu.se DESCRIPTION:Speakers: Niklas Lorén (RISE / Chalmers)\nhttps://lindico453. srv.lu.se/event/159/contributions/1113/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1113/ END:VEVENT BEGIN:VEVENT SUMMARY:Sisse Marquina-Jonberg - Novo Nordisk Foundation\, Denmark DTSTART;VALUE=DATE-TIME:20210610T090000Z DTEND;VALUE=DATE-TIME:20210610T092000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1112@lindico453.srv.lu.se DESCRIPTION:https://lindico453.srv.lu.se/event/159/contributions/1112/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1112/ END:VEVENT BEGIN:VEVENT SUMMARY:Keynote talk - Structure and rheology of stimuli responsive nanoce llulose interfacial layers DTSTART;VALUE=DATE-TIME:20210610T070000Z DTEND;VALUE=DATE-TIME:20210610T074000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1108@lindico453.srv.lu.se DESCRIPTION:Speakers: Peter Fischer (ETH Zurich\, Switzerland)\nThe use of particles such as nanocelluloses\, i.e. cellulose nanocrystals (CNC) and nanofibrils (CNF) received increasing attention for the Pickering stabiliz ation of fluid interfaces [1]. The adsorption of nanocellulose and nanocel lulose-protein composites at oil-water or air-water interfaces facilitates the formation of stable and biocompatible emulsions and foams but depends heavily on the particles’ surface properties. In this contribution\, we review the structure of differently designed adsorption layers by neutron reflectivity and interfacial rheology measurements as a function of physi co-chemical boundaries conditions (pH\, salts\, enzymes) [2\, 3]\, surface properties of the cellulose crystals (natural\, methylation\, esterificat ion) [4\, 5]\, and protein or polysaccharide addition [6]. Native unmodifi ed CNC (hydrophilic\, negatively charged\, and anisotropic nanoparticles) showed negligible viscoelasticity that could be increased by charge screen ing due to a shift from repulsive to attractive CNC interactions. Methylat ed CNCs formed dense monolayers with higher dynamic moduli compared to nat ive CNCs and could be thermo-gelled into multilayers. The esterified CNCs formed aggregated clusters at the interface\, resulting in a Maxwellian fr equency behavior with distinctive relaxation times\, a rarely observed phe nomenon for interfacial layers. Scattering length density profiles obtaine d from neutron reflectivity measurements are used to elucidate the thickne ss and roughness of the adsorption layer\, and in case of nanocellulose-pr otein composites\, their spatial composition. Supported by in vivo digesti on experiments in humans we rationalize the design principles of nanocellu lose-stabilized emulsions and foams for food and drug delivery vehicles [7 ].\n\n[1] Bertsch P\, Fischer P: Adsorption and interfacial structure of n anocelluloses at fluid interfaces\, Advances in Colloid and Interface Scie nce 276 (2020) 102089\n[2] Bertsch P\, Fischer P: Interfacial rheology of charged anisotropic cellulose nanocrystals at the air-water interface\, La ngmuir 35 (2019) 7937.\n[3] Scheuble N\, Geue T\, Windhab EJ\, Fischer P: Tailored interfacial rheology for gastric stable adsorption layers\, Bioma cromolecules 15 (2014) 3139.\n[4] Bertsch P\, Diener M\, Adamcik J\, Scheu ble N\, Geue T\, Mezzenga R\, Fischer P: Adsorption and interfacial layer structure of unmodified nanocrystalline cellulose at air/water interfaces\ , Langmuir 34 (2018) 15195.\n[5] van den Berg MEH\, Kuster S\, Windhab EJ\ , Adamcik J\, Mezzenga\, R\, Geue T\, Sagis LMC\, Fischer P: Modifying the contact angle of anisotropic cellulose nanocrystals: Effect on interfacia l rheology and structure\, Langmuir 34 (2018) 10932.\n[6] Scheuble N\, Lus si M\, Geue T\, Carriere F\, Fischer P: Blocking gastric lipase adsorption and displacement processes with viscoelastic biopolymer adsorption Layers \, Biomacromolecules 17 (2016) 3328.\n[7] Scheuble N\, Schaffner J\, Schum acher M\, Windhab EJ\, Liu D\, Parker H\, Steingoetter A\, Fischer P: Tail oring emulsions for controlled lipid release: Establishing in vitro-in viv o correlation for digestion of lipids\, ACS Appl. Mater. Interfaces 10 (20 18) 17571.\n\nhttps://lindico453.srv.lu.se/event/159/contributions/1108/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1108/ END:VEVENT BEGIN:VEVENT SUMMARY:Contr. talk - Towards tabletop 4D imaging of low-density food prod ucts using x-ray phase contrast DTSTART;VALUE=DATE-TIME:20210609T144000Z DTEND;VALUE=DATE-TIME:20210609T150000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1107@lindico453.srv.lu.se DESCRIPTION:Speakers: William Twengström (Exciscope AB)\nDetailed imaging of the food we eat widens our understanding of its structure and helps us to optimise ingredients and production techniques. Recent and established imaging techniques within\nthe food science field are e.g. light and elec tron microscopy methods\, as well as X-Ray Computed Tomography (XCT)\, Mag netic Resonance Imaging (MRI) and Neutron Tomography (NT) [1]. In contrast to microscopy techniques\, which often require advanced and time-consumin g sample preparations\, tomographic imaging techniques\, such as XCT\, MRI and NT often have no such requirements. XCT has already been used for dec ades to non-destructively investigate\, e.g.\, muffins\,\nmarshmallows and meat\, but with limited contrast in samples with small density variations due to weak x-ray attenuation [2\,3]. On the other hand\, detecting not o nly attenuation\, but also phase shift\, enables high-resolution imaging o f low-density materials\, such as protein\, carbohydrates and fat. If imag e acquisition is fast enough\, time-resolved volume data sets can be acqui red. Synchrotron radiation 4D x-ray microtomography in combination with ph ase contrast has already been demonstrated on both bread during baking [4] and microstructural stability in ice-cream [5]\, and great technical deve lopments in 4D imaging have been shown in recent years [6]. Synchrotron be amlines are able to produce state-of-the art images\, where two access rou tes currently exist: 1) peer-review accessibility\, if the aim is to publi sh the results and 2) paid industry beamtime\, without the requirement of publishing. However\, both access routes often involve a waiting time up t o 3-6 months. If on the other hand time-resolved micro-CT of food products were to be performed in a local laboratory\, waiting time and cost can be reduced. In this study\, we used lab-based phase-contrast CT to demonstra te imaging of different low-density food products\, such as bread\, potato chips\, tomatoes and cheese doodles. Our propagation-based phase-contrast system is based on a liquid-metal-jet microfocus x-ray source\n(MetalJet D2\, Excillum\, Sweden) [7] and enables high-resolution tomography of cent imetre-sized samples in a few minutes. For example\, it can be used to dif ferentiate between fat\, carbohydrates and air in cheese doodles (Fig. 1a) \, as well as visualisation of fine internal structures and air cavities i n potato chips and bread. Results obtained with phase-contrast micro-CT we re compared to confocal laser scanning microscopy (CLSM) images of similar samples (Fig 1b)\, acquired with a Leica system (TCS SP5 AOBS\, Heidelber g\, Germany). Fat is found inside some of the pores in the cheese doodle\, predominately close to the surface. The different components in the struc ture\,\nthe corn matrix\, fat and air blisters\, correspond well between C LSM and X-ray phase-contrast CT images. By further optimisations\, the tot al micro-CT acquisition time can be reduced to 10-30 seconds per scan\, wh ich opens up for time-resolved studies of\, for example\, extrusion or mel ting processes.\nThese developments lead the way towards performing 4D ana lysis of food products closer to the production line\, thus further refini ng the processes of making tasty\, healthier and more cost-efficient food products.\n\nhttps://lindico453.srv.lu.se/event/159/contributions/1107/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1107/ END:VEVENT BEGIN:VEVENT SUMMARY:Keynote talk - Plant Forward: How unlocking Nature’s toolbox is fuelling our innovations DTSTART;VALUE=DATE-TIME:20210609T122000Z DTEND;VALUE=DATE-TIME:20210609T125000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1102@lindico453.srv.lu.se DESCRIPTION:Speakers: Krassimir Velikov (Unilever\, The Netherlands )\nhtt ps://lindico453.srv.lu.se/event/159/contributions/1102/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1102/ END:VEVENT BEGIN:VEVENT SUMMARY:Keynote talk - Aurora Australis to Northern Lights - shining light on milk and infant formula during digestion DTSTART;VALUE=DATE-TIME:20210609T111000Z DTEND;VALUE=DATE-TIME:20210609T115000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1100@lindico453.srv.lu.se DESCRIPTION:Speakers: Benjamin Boyd (Monash University)\nhttps://lindico45 3.srv.lu.se/event/159/contributions/1100/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1100/ END:VEVENT BEGIN:VEVENT SUMMARY:Closing remarks and future outlook – Niklas Lorén (RISE) & Anna Ström (Chalmers) DTSTART;VALUE=DATE-TIME:20210611T085000Z DTEND;VALUE=DATE-TIME:20210611T100000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-1098@lindico453.srv.lu.se DESCRIPTION:https://lindico453.srv.lu.se/event/159/contributions/1098/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/1098/ END:VEVENT BEGIN:VEVENT SUMMARY:Welcome by the vice chancellor of Lund University Prof Erik Renstr öm DTSTART;VALUE=DATE-TIME:20210609T110000Z DTEND;VALUE=DATE-TIME:20210609T111000Z DTSTAMP;VALUE=DATE-TIME:20260529T204340Z UID:indico-contribution-159-851@lindico453.srv.lu.se DESCRIPTION:https://lindico453.srv.lu.se/event/159/contributions/851/ LOCATION:Online on Zoom URL:https://lindico453.srv.lu.se/event/159/contributions/851/ END:VEVENT END:VCALENDAR