3rd Annual Research Spotlight Meeting

Research Spotlight

Research Spotlight Meeting 2021

The Plant Protein Innovation Center (PPIC) hosted its Third Annual Research Spotlight Meeting on December 8, 2021, at the University of Minnesota's St. Paul Campus.  This year, PPIC welcomed 118 individuals from 46 companies and organizations involved in alternate protein research.   

The Research Spotlight meeting highlighted the latest in alternative proteins research as presented by a number of scientists in field.  Keynote speaker Dr. Karolina Östbring, Associate Professor, Lund University, Sweden, led attendees through her research entitled “Protein Isolation Strategies for High Moisture Rapeseed and Hemp Protein Meat Analogues.”  According to Dr. Östbring, “Although the activity in the field of high-moisture meat analogs is intense, the field is still young. The basic understanding of how raw material characteristics and extruder parameters affect the texture on a molecular level is still to a large extent unknown.”  In addition to this presentation, researchers from six U.S. universities presented summaries on projects focused on functionality, flavor interactions, nutrition, and breeding of various protein sources including peas, chickpeas, quinoa, hemp, mung beans, oats, and microalgae. 

Attendees also engaged in interactive poster sessions.  Posters featuring current PPIC funded as well as other research projects were presented.  The sessions allowed guests to meet students and post-doctoral researchers and learn about their progress.  “These poster sessions are a great benefit to both the student researchers and industry,” notes PPIC Director Prof. B. Pam Ismail.  “Students get the opportunity to showcase their work, while industry participants get to ask questions about the research and connect with future research talent for hire.” 

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Professor Job presenting
Company booths
Research Posters
Poster Visuals
Crowded posters


Karolina Östbring, Associate Professor, Lund University


Keynote Speaker


Dr. Karolina Östbring is an Associate Professor at the Department of Food Technology, Engineering and Nutrition at Lund University, Sweden. She received her PhD in Experimental Medical Science (Lund University) in 2015 focusing on the extraction of green leaf proteins and their effect on appetite. Thereafter her interest in the isolation of plant proteins has been broadened to also include rapeseed, hemp, oat, pea and faba bean protein. She is particularly interested in isolation and separation aspects on the semi-pilot scale and its effect on process efficiency and functional properties. In the last years, high moisture extrusion cooking has been the main theme with the goal to increase the use of crops that are (or could be) cultivated in the Nordic hemisphere.

Presentation: Protein isolation strategies  for high moisture rapeseed and hemp protein meat analogues

In light of the climate crisis, both the consumers and the food industry in Europe are interested in plant-based alternatives to meat. But which crops should be used? In our research, we are investigating legumes such as pea and faba bean but also agricultural by-streams that are not currently used for food purposes but go to animal feed and are sold at a very low price. Rapeseed press cake and hemp press cake are by-products from the production of rapeseed- and hemp oil and the press cake contains 30-40% protein on a dry basis. To be able to produce meat analogs from plant proteins, the protein needs to be isolated, concentrated and the anti-nutrients need to be removed or be inactivated during the process. Also, the bitter flavor needs to be reduced to meet the consumers' requirement of well-tasting food. This presentation will outline critical process parameters in the isolation and concentration of rapeseed and hemp protein on the semi-pilot scale as well as presenting results from high moisture meat analog studies where different crops are co-extruded. Although the activity in the field of high moisture meat analogs is intense, the field is still young and most of the knowledge and experience are kept as secrets within companies. The basic understanding of how raw material characteristics and extruder parameters affect the texture on a molecular level is still to a large extent unknown. This knowledge is needed to formulate attractive and nutritious plant-based meat analogs as an alternative to meat.

Job Ubbink, Professor & Head of Department, University of Minnesota


Dr. Job Ubbink is Professor and Head of the Food Science and Nutrition Department at the University of Minnesota. He was trained as a physical and polymer chemist at the University of Leiden (The Netherlands) and he obtained his PhD in Chemical Engineering and Materials Science at Delft University of Technology (The Netherlands). He has worked for over 15 years in R&D positions in the food industry, including 11 years at the Nestlé Research Center (Lausanne, Switzerland). Prior to joining the University of Minnesota, Dr. Ubbink was associated with the California Polytechnic State University (San Luis Obispo), the University of Bristol (UK) and the ETH Zurich (Switzerland). He was visiting scientist at Moscow State University (Russia) and he has taught as visiting professor at the School of Food Engineering, University of Campinas (Brazil). He has used extrusion for a variety of food systems, including cereals and snacks, petfood, instant beverages, meat- and pasta analogues, and controlled release systems for flavors and bioactives. His further research interests include the glassy state in foods, rheology of highly concentrated systems, delivery of active ingredients and the science of cooking.

Presentation: Phase behavior of plant proteins: relation to extrusion processing, textural attributes and shelf life

The development of sustainable food products based on plant proteins is critically dependent on the ability to transform a variety of plant proteins into structured matrices that combine a desirable texture with a beneficial nutrition. The structuring of plant protein matrices is determined by a sensitive balance between processing conditions, including shear forces, water content and temperature modulation, and molecular properties of the protein isolate, specifically phase behavior and interactions, reactivity and relaxation times. In this lecture, I am reporting on ongoing research on the characterization the pea and chickpea protein isolates and the mapping of their thermomechanical transformation in the framework of the supplemented state diagram. I will furthermore be discussing the opportunities to employ microcompounding as technique to investigate the conversion of very small protein samples, typically fractionated samples that are prepared at the labscale, and present exploratory results on the properties of structured matrices based on pea protein isolates that are prepared by microcompounding and twin-screw extrusion.

Youling Xiong, Professor, University of Kentucky

Youling Xiong

Dr. Youling Xiong, a food science professor at the University of Kentucky, is an expert on protein chemistry, functionality, and applications. His research focuses on the interaction of meat and plant proteins with various natural food compounds for healthy food production. He has mentored over 70 graduate students and postdocs, published more than 300 research articles in scientific journals, and given over 140 invited/keynote presentations throughout the world. Dr. Xiong has received many professional accolades, notably American Chemical Society’s Young Scientist Award, American Meat Science Association’s Distinguished Research Award and Signal Service Award, IFT Food Chemistry Lectureship Award, Royal Swedish Academy of Agriculture and Forestry’s Bertebos Prize, and University Research Professor award. He is an elected Fellow of IFT, ACS AGFD, IUFoST and AMSA, editor of Food Bioscience, and former scientific editor of Journal of Food Science.

Presentation: Ultrasound-assisted modification of mung bean and oat proteins for functionality improvement and food product development

Mung bean and oat are two special crops and their seeds are considered exceptionally nutritious and of health promoting activities. Compared with soy, pea, and other pulses, the techno-functionality of proteins from mung bean and oat has not been well studied. Globulins are the principal fraction of functional proteins, and limited research has demonstrated great potential of both emerging protein sources. Aimed at improving the solubility and interfacial activity, our lab has applied structure-modifying ultrasound technology to treat both mung bean and oat proteins. Through the disruption of compact native structures and complexes by cavitation, we are able to significantly increase the solubility, foaming capacity, and emulsifying activity of these and other legume proteins, which may benefit the preparation of foam and emulsion food products.

B. Pam Ismail, PPIC Founder & Director and Professor, University of Minnesota

Pam Ismail

Dr. Pam Ismail is the Founder and Director of the Plant Protein Innovation Center and is a Professor at the Department of Food Science and Nutrition, University of Minnesota. Dr. Ismail has over 25 years of experience in Food Chemistry research focused on analytical chemistry, protein chemistry, and chemistry and fate of bioactive food constituents. Her research focuses on structural characterization and enhancement of functionality, safety, bioavailability, and bioactivity of food proteins, following novel processing and analytical approaches. She is the recipient of a “Distinguished Teaching Award” and an “Outstanding Professor Award”.

Presentation: Enhancing the Viability of Plant Proteins through Various Innovative Approaches

The demonstration of equivalent or superior/new functionality of plant proteins compared to existing alternatives is essential to both the consumer and food industry. Food producers are seeking information on the nutritional, physiological, and functional characteristics of plant proteins. While plant protein is gaining traction, functionality limitations is hindering its market growth. Improving plant protein functionality will enable successful utilization in various food applications. There are several reports on plant protein functionality and applications, but much is still not known about the effect of different processing and modifications on the structural and associated functional changes. This presentation will cover our efforts to enhance the viability of plant proteins through various innovative approaches. Functionalization using cold plasma, enzymes, and blending will be covered. Changes in the protein tertiary, secondary and primary structure will be elucidated. The impact of structural change on protein functionality will be highlighted. Additionally, targeting the inherent protein characteristics through breeding will also be introduced.

Clifford Hall, Professor, South Dakota State University

Cliff Hall

Clifford Hall III is currently a professor in the in the Dairy and Food Science Department at South Dakota State University (SDSU). He oversees research on pulse quality and utilization of pulses in food systems and oversees the annual U.S. Pulse Quality Survey. His primary research areas include the utilization of non-traditional crops in food products. Examples include omega-3 fortification from flaxseed in extruded bean snacks, use of pulse proteins as egg replacers, effects of extrusion on pulse components and sensory and stability characteristics of pulses, pulse flours and pulse fortified products. In addition, methods for deflavoring of pulse flours and impact of storage on pulse composition has most recently been areas of research.

Presentation: Deflavoring of Pea Flour

Dry pea (Pisum sativum L.) is an important ingredient in plant-based food and gluten-free markets. However, the strong pea flavor and bitterness limits pea ingredient utilization in the food industry.This presentation will focus on supercritical carbon dioxide (SC-CO2) and ethanol (EtOH) extraction as deflavoring method. Pea flour was subjected to a series of conditions involving different blends of SC-CO2 and EtOH. Headspace solid-phase microextraction-gas chromatography (HS-GC), GC-olfactometry (GC-O), and quantitative descriptive analysis (QDA) were used to determine the degree of reduction in the intensity of pea flavor and bitterness. Ethanol (22%), temperature (86 °C), and pressure (42.71 MPa) operating conditions for SC-CO2+EtOH extraction were optimal for deflavoring. Total volatile contents of non-deflavored (NDPF) and deflavored (DPF) pea flours were 18.1 and 2.0 µg/g, respectively. Similar reductions in total volatile intensities as measure by GC-O were observed for NDPF and DPF (19 and 2, respectively). Off-aroma compounds included 1-hexanol, 1-octanol, 1-nonanol, nonanal, and 2-alkyl methoxypyrazines, which were below the detection limit in SC-CO2 extracted pea flours. Less pea intensity (18 vs. 112 mm) and bitterness (4.5 vs. 53.4 mm) was observed in DPF compared to NDPF. SC-CO2+EtOH extraction can be a potential technology to improve the organoleptic properties of pea flour. 

Gary Reineccius, Emeritus Professor, University of Minnesota


Gary Reineccius, is an Emeritus Professor in the Department of FScN at the University of Minnesota. He has published ca. 250 research articles focused on flavor. He has spent three sabbatical leaves in the industry with internationally known flavor companies. Dr. Reineccius has taught courses in Food Processing, Food Chemistry, Food Analysis, and Flavor Chemistry and Technology. He has written a college textbook on food flavors, and has authored the Source Book of Flavors. Dr. Reineccius’ achievements have been recognized by numerous local and international organizations. His current research focus is on flavor encapsulation and flavor interactions with proteins.

Presentation:  Analysis of covalent flavor reactions with pea protein

In a dairy related project we have developed a mass spectrometric method to measure covalent reactions between flavor compounds and beta lactoglobulin. Unfortunately the much larger size of plant proteins precludes the use of this technique for studying flavor reactions with plant proteins. Thus, we have had to take a different approach for measuring these reactions. To that end we have developed a radioisotope methodology applicable for monitoring flavor reactions with Pea Proteins. In brief, a C14 isotope of the flavor compound of interest is added to an aqueous solution of pea protein isolate and allowed to react at a chosen temperature, pH and time. The reacted solution is solvent extracted to remove the unreacted flavor isotope and the residual C14 flavor:protein solution is placed in a scintillation counter. The gained radioactivity reflects the flavor:protein bound material. While this approach sounds simple, it is not. This presentation will delve into the unique challenges faced in developing this method and cover some initial data.

Lutz Grossmann, Assistant Professor, University of Massachusetts Amherst

Lutz Grossman

Lutz Grossmann is an Assistant Professor at the Food Science Department at UMass Amherst since 2021. He graduated with a Ph.D. in food science from the University of Hohenheim in Germany. His research focuses on facilitating a sustainable food system transition by designing holistic approaches to increase the consumption of plant- and microbial protein-rich foods. He is especially interested in combining downstream processing technology with molecular, physicochemical, and engineering concepts to create food textures that are nutritious, sustainable, and tasty.

Presentation: Utilizing microalgae as a source for technofunctional proteins

Microalgae are single-cell microorganisms that accumulate proteins during phototrophic and heterotrophic cultivation. The cells and their proteins can be used in foods mainly in three ways: (i) as a dietary supplement, (ii) as protein extract, and (iii) as a whole-cell ingredient (inactive filler). When extracted, proteins from microalgae may have unique technofunctional properties in foods, which go beyond their nutritional value. These functionalities include gelation, emulsifying, solubility, and coloring properties, but gentle extraction techniques are needed to retain the functionality of the protein. Less-refined downstream processing approaches showed to be a promising technique to produce such functional protein fractions from whole-cell microalgae that have been cultivated by different cultivation methods. These proteins showed high functionality, especially excellent solubility profiles and emulsifying properties. For example, proteins from Chlorella protothecoides have a solubility of >84 % in the pH range 2 to 12. These microalgae proteins may not only possess a high functionality but specific microalgae also contain valuable proteinaceous coloring compounds that can be extracted by less-refined processing approaches and serve as natural food colorants. In conclusion, microalgae can be a biofactory of various functional proteins that can be utilized in food formulations. 

Kevin Murphy, Associate Professor, Washington State University

Kevin Murphy

Kevin Murphy is an Associate Professor in the Dept. of Crop and Soil Sciences at Washington State University, where he leads the specialty crop breeding and agronomy program. The goal of his Sustainable Seed Systems Lab is to increase the genetic- and nutritional-diversity of cropping systems across Washington State through the development of biofortified cultivars and implementation of ecologically-rooted production practices. His group focuses on breeding and/or cropping systems research in quinoa, spelt, buckwheat, perennial grains, proso millet, and barley. His research emphasizes crops, varieties, and/or farming systems that optimize nutritional value and provide tolerance to heat, drought, and diseases while improving yield, flavor and end-use quality of the target crops. Internationally, Kevin and his team conduct participatory breeding and agronomic research on quinoa, barley, and millets in Rwanda, Malawi, and Ecuador. 

Presentation: Breeding for Protein Quality in Quinoa

Quinoa (Chenopodium quinoa Willd.) is a Andean grain well known for its exceptional nutritional content, including protein quality. My research program focuses on quinoa breeding and developing appropriate agronomic practices that targets improving yield while optimizing nutritional traits of interest. In 2019, we evaluated 100 genotypes grown in Washington State for total protein and essential amino acid content, and identified a) genotypes that could be considered a complete protein and b) amino acids that were limiting in a majority of genotypes. We are currently conducting a genome-wide association study using 250 accessions from a quinoa world core collection grown over four site-years in Germany and the United States. During this talk I will describe the results from these two studies as well as our ongoing project ‘Enhancing Human Health and Nutrition from Soil to Society’.

Tom Michaels, Professor, University of Minnesota

Tom Michaels

Tom Michaels is a Professor of Horticultural Science at the University of Minnesota - Twin Cities.  He studies classical plant breeding and genetics with current research projects focused on improvement of industrial hemp, sweet sorghum and dry edible beans.  Tom collects, evaluates and selects within naturalized Cannabis populations found across Minnesota and develops breeding lines with genetics useful to hemp farmers growing for grain, fiber or legal cannabinoids.  He is a founding director of the Open Source Seed Initiative, an organization maintaining fair and open access to plant genetic resources.

Presentation: Evaluating and improving functionality of hemp seed protein

An inaugural project supported by the PPIC to evaluate and improve functionality of hemp seed protein recently concluded with remarkable outcomes.  The Ismail lab successfully isolated hemp protein with high purity and yield (>80%) from multiple cultivars. The isolates exhibited acceptable color, promising gelation and water holding capacity at neutral pH, and protein solubility at acidic pH. The House Lab confirmed hemp protein PDCAAS is hampered by low lysine across current cultivars.  The Michaels group developed grain-type hybrids for future evaluation using novel breeding lines selected from Minnesota populations of naturalized hemp.  This presentation will review these and additional outcomes in the broader context of hemp production, utilization and improvement in upper Midwest food systems.

Kaustav Majumder, Assistant Professor, University of Nebraska

Kaustav Majumder

Dr. Kaustav Majumder is an Assistant Professor at the Department of Food Science and Technology, University of Nebraska, Lincoln (UNL). He obtained his Ph.D. from the University of Alberta, Canada, and Postdoctoral training from University of Guelph, Canada. The overarching goal of his research program in UNL is to understand the impact of dietary proteins and peptides on human health, and to develop peptide-based functional foods for the prevention and management of cardio-metabolic disorders. His laboratory also interested in developing green technologies to produce novel plant-peptides based flavor ingredients for functional foods. He has published over 40 peer-reviewed articles, 10 book chapters, and presented in various national and international conferences.

Presentation: Pulse-protein Derived Peptides in Modulating Taste to Human Health

Great northern beans (GNBs) are a major agricultural commodity for the state of Nebraska and our research have identified naturally occurring peptides γ-glutamyl peptides in GNBs. These γ-glutamyl peptides can exert kokumi sensation via allosteric activation of the calcium-sensing receptor (CaSR). CaSR activation via γ-glutamyl peptides can reduce inflammatory responses. Chronic vascular inflammation contributes to the pathogenesis of various cardiovascular diseases (CVDs) such as atherosclerosis. Our study has developed an aqueous extraction method for isolating γ-glutamyl peptides from GNBs. GNB-derived γ-glutamyl peptides can significantly reduce tumor necrosis factor-ɑ (TNF-ɑ) induced vascular inflammation. The bioactive fraction can retain its biological activity after gastrointestinal digestion. The most abundant γ-glutamyl peptide, γ-glutamyl valine (γ-EV), can also exhibited the similar biological effect in both in-vitro and in-vivo studies, and it can be transported via intestinal epithelial cells. Fermentation with specific lactic acid bacteria can be utilized to enhance the concentration of γ-glutamyl peptides from GNB flour to develop food products with unique flavor profile and potential health benefits. Thus, the study concluded that the kokumi-active, dietary γ-glutamyl peptides could significantly reduce vascular inflammation and GNB flour could be used to develop functional foods for the prevention and management of CVDs. 

Dan Gallaher, Professor, University of Minnesota

Dan Gallaher

Dr. Dan Gallaher is a professor in the Department of Food Science and Nutrition at the University of Minnesota. His research interests include dietary influences on colon cancer and diabetes, particularly the effects of whole grains, as well as protein quality of plant proteins. He is a member of the University of Minnesota Cancer Center, the Minnesota Obesity Prevention Center, is on the advisory board for the Healthy Foods, Healthy Lives Institute, and on the editorial board for the Journal of Food Science.

Presentation: Determining Nutritional Protein Quality: Does the In Vitro Approach Measure Up?

A common method for determining protein quality, in the nutritional sense, is the Protein Digestibility-Corrected Amino Acid Score (PDCAAS). PDCAAS is the accepted protein quality method in the United States for purposes of food labeling. It is calculated as the product of the amino acid score, determined by comparing the amino acid composition of a protein to reference values of human amino acid requirements and using the limiting value, and the protein digestibility. Currently, protein digestibility is determined by an animal feeding trial using rats. This is slow, expensive, and only a few proteins can be assayed for digestibility at a time. Thus, an in vitro method to determine protein digestibility would be highly desirable. Many in vitro methods have been proposed, but none have been widely accepted. Recently, however, a new method has been developed which is showing promise. The method, which is commercially available from Neogen, has shown a good correlation with protein digestibility measured in rats for a number of plant proteins. However, for several plant proteins there is not a good correspondence between the in vivo and this new in vitro method. Possible reasons for this lack of correspondence will be discussed.


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