Proposed Non-GMO Labeling and Certification Options

Posted on:January 8, 2019
2018 PTT fwp/Proposed Non-GMO Labeling and Certification Options - Nancy Knight

Non-GMO Project is a highly recognized and trusted verification process. Of noted importance is that some of the newer technologies, such as CRISPR-Cas9 (gene editing), will not be able to be certified under the impending bioengineered standard.

WHILE NON-GMO claims are fast growing, the regulatory land- scape is unclear. Nancy Knight, Director of Quality and Regulatory Compliance, Orgain, Inc., discussed current challenges, as well as options for non-GMO labeling in her presentation “Non-GMO Transparency: Understanding Your Options.”

The final rule for the National Bioengineered (BE) Food Disclosure Law is expected to be issued later this year. The Agricultural Marketing Service of USDA comment period ends July 3, 2018. Federal law preempts state law. Knight encourages companies whose brands might be affected to read the lengthy rule.

USDA is silent in the regulation regarding third-party, non- GMO certifications. The proposed rule requires GMO ingredients to be labeled if they ARE in the product. Third-party certifications indicate that GMO ingredients AREN’T in the product. Whether the two approaches to labeling will align is still a grey area.

FDA’s guidance for voluntary labeling was issued November 2015. Certain terms are recommended, such as “not genetically engineered,” “not bioengineered” or “not genetically modified using modern biotechnology.”

The guidance emphasizes avoidance of “GMO-free” claims and to avoid intervening material in the list of ingredients, such as “non-GMO corn.” Knight reasoned that FDA views this as a gateway labeling violation. “In (and of) itself, it’s not that big of a deal,” she said, “but it may indicate that you have people on your staff who don’t know much about labeling.”

Companies seeking non-GMO verification have choices. The nonprofit Non-GMO Project is highly recognized. Their logo has earned consumer trust and retail promotion. They stand by their standards. “The Non-GMO Project thought it important that I state that they are looking at new technologies [used by the industry],” she said. CRISPR and novel technologies will not be able to be certified under the standard.

The process to achieve certification begins with selecting a technical administrator (TA) who is affiliated with an outside agency. The Non-GMO Project requires a license agreement. The TA will complete a product evaluation. Once verified, products will be eligible for marketing. Verification is renewed annually. She cautions it can take four weeks or (up to) a year and a half to get through the process.

“I can’t stress enough how the key to success is partnering with the right TA. Everyone has a different competency. If you [use] citric acid, for example, see if they have certified citric acid before.” TAs must understand how products are made, so it can avoid a lot of education and loss of time if they’ve worked with the product before.

Food Chain ID, NSF, Where Food Comes From and SCS Global are all TAs. Food Chain ID has the longest history of verification. She recommends interviewing the TAs, getting pricing and negotiating. “If you’re big enough, say you want a project manager. Tell them your timeline. The flip side is, make sure someone in your organization is up to speed on the standards and knows what type of documentation is required,” she said.

Other options to the Non-GMO Project include USDA Organic and USDA Process Verified. NutraSource I-Gen, a testing lab, is another alternative with fewer documentation requirements. NSF True North was created in collaboration with Whole Foods. Available to other companies, its advantage is ease of certification if already organic.

Some companies do not follow a certification route and use their own logos. This is acceptable, as long as it meets FDA’s definition of what is truthful and not misleading. Some retailers require third-party certification.

Nevertheless, USDA guidance is coming. “You don’t want to go down the path of a third-party certification that may be inconsistent,” she cautioned. “Some companies, like Whole Foods, are pausing until the rule is clear. They still want third-party verification, but ingredient statements might be affected by the rule.”

“Non-GMO Transparency: Understanding Your Options,” Nancy Knight, Director of Quality and Regulatory Compliance, Orgain, Inc.

This presentation was given at the 2018 Protein Trends & Technologies Seminar. To download free presentations and the Post-conference summary of this event, go to

See past and future Protein Trends & Technologies Seminars at

The Value of Protein on Muscle Health During Aging

Posted on:January 3, 2019

RECENT ADVANCES in research show protein’s potential to improve health status in aging adults, according to Douglas Paddon-Jones, Ph.D., FACSM, Department of Nutrition and Metabolism; Center for Recovery, Physical Activity and Nutrition; The University of Texas Medical Branch, Galveston, who spoke on the topic “Nutrition Strategies to Protect Muscle Health During Aging: The Value of Protein.” The most effective interventions to reduce muscle loss during aging include physical activity, overall nutrition and protein, he stated.

Paddon-Jones’s research has shown that the ingestion of sufficient protein is important for muscle protein synthesis (MPS) and maintenance of muscle mass and function. He described a study that looked at MPS in healthy young (41 years +/- 8) and elderly (70 years +/- 5) adults (Symons, TB et al. 2007. Am J Clin Nutr./ Basal MPS was measured prior to and after the consumption of a 4oz serving of lean beef containing 30g of protein. “Very encouraging results showed that decrements in MPS did not occur in the elderly,” noted Paddon-Jones. “There was a 50% increase in MPS, suggesting that aging doesn’t impair the ability of the body to build and repair muscle.”

Recognizing that typical intakes of protein are much greater than 30g, further research sought to compare changes in MPS following a single moderate serving (113g; 220Kcal; 30g protein) or large serving (340g; 660Kcal; 90g protein) of lean beef in young and elderly adults (Symons et al. 2009. J Am Diet Assoc./ Despite a threefold increase in protein and energy content, there was no further increase in MPS. “This is a powerful example that suggests an ‘intake ceiling’ of 30g of protein for optimum muscle building,” he said.

The synergistic effects of resistance exercise and a protein-rich meal on MPS has been evaluated (Symons, TB, et al. 2011. J Nutr Health Aging./ Following ingestion of 340g lean beef and resistance exercise (knee extensions) in healthy young (29 years ±3) and older (67 years ±2) adults, Paddon-Jones reported that “the results were encouraging, as muscle building increased by approximately 108% in young and older adults following the protein and resistance exercise.”

“Our research suggests that protein intake should be optimized at every meal to positively impact MPS,” noted Paddon-Jones, “If you are consuming 65g of protein at dinner, your muscle is only using 50% of this.” His research has also shown that MPS is blunted in the elderly, when the quantity of protein is less than about 20g per meal (Paddon-Jones D and Rasmussen, BB. 2009. Curr Opin Clin Nutr Metab Care. /

Bed rest has a profoundly negative effect on muscle metabolism, mass and function in adults. In one study, patients remained in bed 95% of the time over four days with no activity. The remaining 5% of the time involved only about 15 steps per minute, resulting in rapid muscle atrophy. Middle-aged adults showed few phenotypic signs of aging, yet they may be more susceptible to inactivity than younger adults (English et al. 2016, Am J Clin Nutr./ “We need to start focusing on muscle health the same way as we do bone health,” Paddon-Jones stressed.

Nutrition is one area where a difference can be made. Paddon-Jones’s research also examined whether leucine, a branch-chain amino acid and stimulator of skeletal MPS, can protect skeletal muscle health during bed rest (English et al. 2016 / Middle-aged adults (52 years ± 1) were supplemented with leucine (0.06g/kg/meal or about 4g/meal) or an alanine control during 14 days of bed rest. Bed rest decreased post-absorptive MPS by 30% ± 9% (Control group) and by 10% ± 10% (LEU group). Leucine protected knee-extensor peak torque and endurance. “Interestingly, leucine prevented an increase in body fat percentage and reduced whole-body lean mass loss after seven days,” noted Paddon-Jones, “but not at 14 days of bed rest. Perhaps leucine supplementation could partially protect muscle health during relatively brief periods of physical inactivity,” he concluded.

“Strategies to Protect Muscle Health During Aging: The Value of Protein,” Douglas Paddon-Jones, PhD, Professor, Department of Nutrition and Metabolism, The University of Texas Medical Branch

This presentation was given at the 2018 Protein Trends & Technologies Seminar. To download free presentations and the Post-conference summary of this event, go to

See past and future Protein Trends & Technologies Seminars at


Formulating with Whey Protein for Maximum Health Benefits, Functionality and Taste

Posted on:January 2, 2019


2018 PTT fwp/Formulating with Whey Protein for Maximum Health Benefits, Functionality and Taste - Chris Lockwood

The type(s) of whey product selected for a formulation depends not only on the finished flavor, nutrition profile and price goals, but on the demographic target selected, as well.
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AT THE OUTSET of his presentation, “Formulating with Whey in a Fully Transparent Market,” Chris Lockwood, Ph.D., President, Lockwood LLC, described some of the advantages that protein possesses, including its function as the only major nutrient to stimulate muscle building (muscle protein synthesis, or MPS). Just a few of the many advantages of consuming more protein, in comparison to fat or carbohydrate, is that it promotes greater thermogenic effects, hunger reduction, and body fat and weight loss when combined with a calorie-restricted diet.

Whey protein [for sports nutrition] is most often classified in one of three ways: As whey protein concentrates (WPC), whey protein isolates (WPI) or whey protein hydrolysates (WPH). Filtration and other purification processes are used to produce WPC and WPI, with WPI containing 90% or higher total protein. The final composition of WPH is influenced by enzymes and re-action conditions used, as well as the number of available bonds that are broken. Generally speaking, the greater the degree of hydrolysis (DH), the smaller the number of amino acids per peptide molecule and the more challenging the taste issues.

In an overview of its beneficial effects, Lockwood noted that whey stimulates muscle growth and elicits significant anabolic response to weight training. A study designed to assess rapidly digested proteins (i.e., whey and soy) and slowly digested proteins (i.e., casein) found whey to be 93 and 18% more effective than casein or soy, respectively, for MPS in men at rest (Tang, JE, et. al. 2009. J Appl Physiol./ ). Following exercise, whey consumption resulted in 122 and 31% greater MPS than casein or soy. “These differences have largely been attributed to how quickly the proteins are digested and the leucine content in whey,” said Lockwood. “The faster the rise in blood amino acids, the greater the peak and total MPS response,” he explained.

“Whey can improve recovery speed, so you can exercise more and recover more quickly,” noted Lockwood. He illustrated findings in a study of 10 resistance-trained men who had been supplemented with WPI, soy protein isolate (SPI) and a maltodextrin-placebo control for 14 days, and then performed an acute heavy resistance exercise test (Kraemer WJ, et al. 2013. J Am Coll Nutr./ 

Whey rapidly and significantly lowered the catabolic steroid hormone cortisol during recovery, whereas soy significantly decreased the post-exercise levels of the anabolic hormone testosterone. “The research for my Ph.D. work revealed that people consuming 30g of whey, regardless the form, twice per day, significantly increased muscle mass,” stated Lockwood. An extensively hydrolyzed WPH, also reduced body fat without significantly affecting total body weight (Lockwood CM, et al. 2017. J Am Coll Nutr./

Further work confirmed that a moderately hydrolyzed WPH vs. its intact (nonhydrolyzed) WPC significantly elevates markers of fat and carbohydrate metabolism, and reduces markers of protein breakdown (Roberts MD, et al. 2014. Appl Physiol Nutr Metab./

These effects may be explained by observations showing that plasma amino acids rise more rapidly as a result of some forms of WPH, compared to when consumed as an intact WPC (Morifuji M, et al. 2010. J Agric Food Chem./ “A study in 10 men also found that whey provided a significantly greater stimulation of insulin release than soy, and that the moderately hydrolyzed WPH tested was significantly more insulinotropic than intact whey. This collectively suggests that certain peptides and the amino acid composition unique to whey—and not just leucine or its fast absorption—as being behind this protein’s superior effects on human physiology,” Lockwood stated.

Lockwood acknowledged that there has been a movement to plant-based proteins by the food industry for many reasons. However, he stressed that “whey is the bodies first protein—it is the predominate protein in mother’s milk to support offspring development and growth.” Additionally, Lockwood indicated that whey is vegetarian; sustainable and renewable; can be certified non-GMO and/or organic; and is gluten-free.

There are many categories of whey available, and Lockwood noted that his research used a 32-degree DH derived from an 80% whey protein concentrate, “which is about as high as you’ll want to go, because the bitterness becomes overwhelming,” he noted. And, although less allergenic and seemingly more efficacious in terms of overall clinical health outcomes, the higher the DH, the more expensive the product becomes.
When a combination of a favorable taste profile plus speed to market are considerations, the best options include WPC, WPI and low-DH (<10%) WPH.

“Formulating with Whey in a Fully Transparent Market,” Chris Lockwood, Ph.D., President, Lockwood LLC

This presentation was given at the 2018 Protein Trends & Technologies Seminar. To download free presentations and the Post-conference summary of this event, go to

See past and future Protein Trends & Technologies Seminars at

Plant Protein Drives Ingredient Innovation

Posted on:December 18, 2018
2018 PTT fwp/Anusha Samaranayaka - Plant Protein Demand Drives Ingredient Innovation

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Plant proteins provide a wide array of functionalities in various applications. Properties will vary, depending on the method used to process the protein ingredient.

TRENDS DRIVING CONSUMER demand for plant proteins include health and wellbeing; the desire for plant-based and clean label products; and concerns related to food security and sustain- ability. The number of opportunities to use plant-based proteins will grow, as the number of novel protein types grows, as well. Choosing the right plant protein for a formulation depends on several factors, from source availability and cost; to functionality and taste; to nutritional considerations—as well as consumer perception and the presence of anti-nutrients.

“In comparing plant proteins with egg and other animal proteins or in trying to replace them, the first and most import- ant challenge is the taste,” said Anusha Samaranayaka, Ph.D., Senior Scientist, POS Bio-Sciences, in her presentation “Plant Proteins: Opportunities, Challenges & Tips for Successful Use in Formulations.” “No matter how functional or how the protein ingredient looks, it doesn’t fly if it doesn’t taste good,” she added.
Careful consideration about the protein source being used in the creation of an ingredient is crucial. Functionality and taste are very important; however, when processing an ingredient, co-products also merit a consideration. Cereals and pulses are composed of about 50-60% starches and fibers. If the goal is to make a protein ingredient using a raw material containing 25% or less protein, finding an application for these co-products is a must; it’s not economically feasible otherwise, Samaranayaka noted.

Variables at different stages of plant protein ingredient production affect flavor, functionality and quality of the ingredient. These stages include growing, harvesting and storage; extraction, fractionation and drying; further processing, such as fermentation, germination and physical, chemical or enzymatic modification; and formulation parameters, such as temperature, pH and mixing. For instance, “protein content deviates with the climate and soil, and even the maturity of harvesting; this affects downstream processing,” explained Samaranayaka. If it’s difficult to remove the seed coat during dehulling—for example, if the seed is not mature—off-flavor notes can occur in the final product. The extraction and fractionation techniques, and most importantly the protein drying technique, are very important in creating these functional protein ingredients, as is further processing, she added.

The molecular structure of plant vs. animal proteins differs. Cereals and pulses mainly have globular, storage proteins, while meat, egg and milk proteins have more soluble and fibrillar-like proteins. Understanding different plant proteins at the molecular level helps in creating processes to effectively extract and isolate the functional proteins of interest. It is also helpful in use of enzymatic, chemical or physical methods to further modify protein ingredients’ functionality.

“Establishment of standard methods for assessing the protein functionality and creating a functionality database of different protein ingredients available would really help food formulators in selecting protein ingredients for their specific needs,” suggested Samaranayaka.

Researchers and food companies have had some success with product modifications to see if plant proteins can replace animal proteins in products. “These process modifications additionally help remove some of the anti- nutrients and off-flavors. Processing also improves the digestibility of these proteins,” Samaranayaka stated.

One example is the creation of meat analogs or alternate meat products. Since most plant proteins have a globular structure, rather than the fibrous structure of meat muscle, they won’t provide that “bite” that is typical of a burger. What can you do? The globular structures must be unfolded, and the proteins aligned, so as to make aggregates that come close to the structure of fibril proteins. That’s what techniques like extrusion can do, continued Samaranayaka.

Plant proteins can also be used in non-dairy beverages, but protein modification via controlled enzymatic or chemical hydrolysis is often needed to improve the protein’s solubility. Improving the solubility helps make the beverage’s texture, consistency and mouthfeel more appealing to consumers.

The composition of each plant protein type differs, as does its inherent flavor and protein functionality. If changing the raw material source or the process used in protein ingredient preparation does not produce the needed flavor and texture in the final product, the food formulation stage can also be used to improve both flavor and textural issues. Approaches include incorporation of a physical or chemical process; or of additives, such as flavor masking agents, companion flavors and/or stabilizers.

Most importantly, finished formations should be presented to consumers in a way that is appealing in flavor and texture. “It’s a complicated story. Growers, food chemists, ingredient manufacturers and formulation scientists have to work together to come up with these crave-worthy creations using different plant protein sources,” Samaranayaka concluded.

“Plant Proteins: Opportunities, Challenges & Tips for Successful Use in Formulations,” Anusha Samaranayaka, Ph.D., Senior Scientist, POS Bio-Sciences

This presentation was given at the 2018 Protein Trends & Technologies Seminar. To download free presentations and the Post-conference summary of this event, go to

See past and future Protein Trends & Technologies Seminars at

Allergenic Potential of Novel Proteins

Posted on:December 6, 2018
2018 PTT. fwp/Steve Taylor - Allergenic Potential of Novel Proteins

Allergenicity of botanically related species, such as peanuts, peas and soybeans, gives researchers cause to test for the abundance of – and amino acid sequence structure of these proteins, as well as cross reactivity and digestive stability.

IN A RICHLY illustrated presentation with global and historical examples on the topic of “Food Allergies: A Challenge for Current and Emerging Proteins,” Steve Taylor, Ph.D., Co-Director of the Food Allergy Research & Resource Program at the University of Nebraska, discussed a key concern that food manufacturers need to keep in mind when using novel proteins in food products: Can novel food sources of proteins be allergenic?

“It’s inevitable,” says Taylor.

Certain foods have long been recognized as allergens. The “big 8” allergens, which include milk, eggs, fish, crustacea, wheat, soy, peanuts and tree nuts, cause about 90% of allergic food reactions in the world. Other countries include additional foods, such as sesame seed, mustard, celery, buckwheat, molluscan shellfish and lupine on their lists of allergens. While the importance of the “Big 8” allergens is not debatable, data on prevalence, potency and severity to support the inclusion of these other foods on allergen lists may be limited.

When new proteins are introduced as foods, allergenic reactions in some individuals will inevitably occur. As precedent, Taylor cited the emergence of soybeans as a novel food source in the U.S. in the 1930s. While soybeans had been consumed in Asia for thousands of years, it wasn’t until the 1950s, when soy-based infant formula was developed for milk-allergic infants, that soy allergies were recognized in the U.S. Ironically, some children with milk allergies also had allergic reactions to soy.

Reactions to multiple allergens are usually due to cross-reactivity to a similar antigen found within different foods. Sometimes the allergenic potential of novel proteins can be predicted because of their similarity to other allergenic proteins. Lupine, a legume that has historically been used in cattle feed, is botanically similar to peanuts. Because lupine has not been genetically modified, it has been widely adopted as a soy replacement in the European Union and Australia. Lupine protein can trigger allergic reactions in some individuals with peanut allergies, which raises a labeling conundrum: Do you warn those with peanut allergies not to eat the food, when only about 20% of Europeans with peanut allergies also have lupine allergies?

Cross-reactivity can also make it difficult to pinpoint the precise allergen that triggers a reaction, especially when cross- reactive allergens with differing potencies may be present. Taylor described severe allergic reactions that occurred in peanut- allergic individuals who consumed a soy-containing muscle- building supplement. Taylor’s group demonstrated that there was no peanut (a highly potent allergen) present; instead, very high levels of soy protein in the product likely caused the reactions. Soy protein has a low potency that appears to share cross-reactivity with the peanut allergen.

Proteins that demonstrate allergenic cross-reactivity may also be challenging to distinguish analytically. Pea protein is surging in popularity right now and may have allergenic cross- reactivity with peanuts. The analytical challenges in differentiating pea vs. peanut protein have elicited food recalls for potential peanut allergen presence—even though pea, not peanut, was present.

It’s important to remember that not all adverse reactions associated with novel proteins are allergic reactions. Quorn is a fungal mold product that is high in both protein and fiber and is popular in the U.K. In some individuals, the high fiber content of Quorn can trigger gastrointestinal symptoms that may be confused with allergic reactions.

As consumer appetite for protein grows, novel proteins will continue to be developed. Determining the allergenicity of new proteins can be difficult and expensive. However, knowing whether the food product has already been shown to be allergenic (in other parts of the world where it is consumed) and whether the food is related to known allergenic foods (i.e., is it a legume?) may help predict whether a novel protein could have significant allergenic potential.

“Food Allergies: A Challenge for Current and Emerging Proteins,” Steve Taylor, Ph.D., Co-Director, Food Allergy Research & Resource Program at the University of Nebraska

This presentation was given at the 2018 Protein Trends & Technologies Seminar. To download free presentations and the Post-conference summary of this event, go to

See past and future Protein Trends & Technologies Seminars at

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