Challenges and Solutions When Working with Protein and FiberPosted on:November 13, 2014
November 13, 2014, Global Food Forums — The following is an excerpt from the Arla Foods’-sponsored
Protein and fiber are added to food systems for many reasons, both functional and nutritional. However, with their addition comes the need for ingredient and processing adjustments, depending on the final food and its desired characteristics.
“The approach that works for us,” explained Martha Porter of Merlin Development, “is to first identify all issues through searches of literature, marketplace, patents, competitive
products (both retail and restaurant) and analogous foods. Then robust experimental design optimizes taste, cost, process and shelflife. Finally, confirmation runs verify the design predictions.”
Porter went on to highlight key considerations when using protein in low-, intermediate- and high-moisture systems. Low-water Systems: In low-water systems, such as protein bars, texture changes over shelflife. Protein tends to increase firming over time, beyond the normal firming that takes place. Proteins are not fully hydrated immediately
and, over time, they draw moisture from syrups generally used to hold bars together. Fiber, if it is not fully hydrated, can also draw moisture from the syrup. The continuous syrup phase then becomes more concentrated, contributing to the loss of pliability.
“Strategies to overcome these issues include use of multiple sources of protein and fiber,” said Porter. In addition to protein powders, nuggets or crisps can be high in protein and also contain fiber. Coatings can be protein- or fiber-fortified.
Cereal pieces, like oats, wheat flakes, nuts, pulse flour, or pieces and seeds, are other sources of protein and fiber. Protein hydrolysates are helpful to mitigate firming. Low-DE syrups promote chewiness and help maintain pliability. They contain longer-chain carbohydrates that hold onto water better and provide cohesiveness.
Higher-DE syrups add sweetness; multiple forms of sugar (sucrose, fructose, etc.) in the same binder system can hinder recrystallization. Sugar alcohols control water activity
and browning. Typically, granola or cereal bars need a water activity below 0.65, with pH in the acidic range. Intermediate-water Systems: Intermediate-water systems like bread have sufficient water to hydrate ingredients, such as fiber and protein, but there is limited
room for their fortification due to other necessary functional components. For example, dilution of gluten creates problems with volume and texture in bread.
In bread, protein considerations include clean flavor and color, especially in white bread. Non-white breads can incorporate pigmented particulates, like nuts, seeds and other
whole-grain ingredients. Fibers can include resistant starches and maltodextrins, which are digestion-resistant, but behave like starches and maltodextrin. They can help mitigate the heavy texture seen with high-cellulosic fiber breads. A blend of different fiber sources may be necessary to achieve both nutrient content and organoleptic quality. Other formula and processing adjustments may be necessary as well, said Porter.
High-water Systems: In beverages, protein selection depends on the desired characteristics of the final product. If clarity is desired, acidified proteins are needed. The proteins used will also depend on the desired function of the beverage or nutrition claims.
Ionic strength, pH, fat and carbohydrate content, and processing parameters, such as temperature and shear, affect final product characteristics. For fiber, the focus is on nutrition, but beverages need fibers with a minimal impact on viscosity, explained Porter.
High-protein and -fiber solutions can be gritty, which can be masked by viscosity. Soluble
fibers may be more helpful, as can smaller particle size. Processing parameters in beverages that need consideration include rehydration time; heat stability of the protein;
and turbidity after heat treatment and fiber dispersibility. Homogenization and emulsion formation, batching temperatures, order of ingredient addition (critical for an acidification step) and packaging (clear or opaque) also help determine final product qualities.
In summary, determination of the rationale behind product fortification is first and foremost. Different moisture levels determine how to approach the formulation issues. Protein and fiber selection can be critical to product success. Process considerations also matter.
Martha Porter, Scientist, Merlin Development Inc., 763-475-0224, firstname.lastname@example.org, www.merlindevelopment.com
Taste Physiology and Considerations in Sweetener ChoicesPosted on:November 12, 2014
November 12, 2014, Global Food Forums — The following is an excerpt from the Ingredion-sponsored “2013 Clean Label Conference Report.”
When it comes to making foods sweeter in a “clean label way,” there are ways to do it naturally and simply, besides using sugar. Some approaches take advantage of the connection between taste and smell. The trigeminal nerve is found in the face (rather than the nose). It responds to irritants, like tingling and numbing, as well as temperature differences.
“The trigeminal sensation can also be used for sweetness enhancement, as can all of the other senses,” said Alex Woo, Managing Director of W2O Food Innovation, as he discussed recent technologies in clean labeling sweetness enhancement.
Natural high-potency sweeteners, such as stevia and monk fruit extract, offer solutions in reduced-sugar or sugar-free applications. When using these sweeteners, a bulk sweetener is also sometimes needed, such as natural non-/low-caloric erythritol, which helps achieve maximum sweetness, yet with minimal off-flavors and low cost, suggested Woo.
Stevia extract, which is labeled as such, is commonly used and has multiple suppliers. It is “natural,” non-caloric, has GRAS status with no FDA objection letter, is 200-400 times sweeter than sugar, stable to heat and a pH over 3, is non-GMO; and certifications for kosher and halal are available. Monk Fruit extract is also non-caloric and is GRAS with no FDA objection letter. It is not yet approved in the EU. Monk fruit extract, not quite as common yet, is 150-200 times sweeter than sugar, heat-stable, non-GMO, kosher-certified and is labeled as “monk fruit extract.”
“Monatin” is a unique, natural amino acid that has recently emerged, but, as yet, is not approved anywhere. It is extracted from a South African plant, Sclerochiton ilicifolius root. It is 3,000 times sweeter than sugar with a unique temporal profile. Monatin has a quick sweetness on-set and no lingering, bitter, metallic or astringent aftertaste.
Woo went on to explain that erythritol has multiple suppliers, is found in fruits and vegetables, and is the only atural polyol made by fermentation. It also has the highest
digestive tolerance among all polyols. Non-caloric, it is non-GMO-possible, 65% as sweet as sugar and has a 3.5% limit in beverages in the U.S. However, not all consider erythritol a clean label solution.
“When ‘natural’ is not enough,” Woo gave examples for sweetener enhancement that could result in shorter label declarations. He explained how to use “cross-modal
correspondences” to enhance sweetness. The brain processes information from different senses to form multisensory experiences in people’s daily lives; therefore, smell, tastes other than sweetness, sights, sounds and trigeminal sensations can all influence the perception of sweetness.
Although sweetness is detected in the mouth, there is also interaction between olfaction and gustation. Retronasal “sweet” aromas sensed in the nose increase the sweet perception in the mouth. Many sweet taste modulators are legally labeled as “natural flavors,” thus result in more consumer-friendly labels.
Woo referenced work by Professor Tepper at Rutgers University, who is investigating molecular biology as a way to “trick” the taste buds. “This approach is novel in the food industry,” stated Woo, “but it is the way of the future.” For example, fresh tomato aroma makes tomato sauce taste sweeter. Sugar distillates enhance beverage sweetness.
Vanilla, below and above threshold, enhances sweetness, according to various reports. Some FDA GRAS, natural, high-potency sweeteners are approved under FEMA GRAS as “natural flavor,” when they are used at very low levels, as sweetness and/or
flavor enhancers. Examples include thaumatin and monk fruit extract. Woo explained trigeminal-on-taste “intramodal” sweetness enhancement using the examples of carbonation, a trigeminal pain agent, which can make artificial high-potency sweeteners taste more like sugar. It is labeled as “carbonated water.”
Beverages formulated with high-potency sweeteners have also shown in panels to taste sweeter at higher temperatures. Some studies have shown that the shape of a food,
specifically a more rounded shape—as in oranges or apples—tends to be associated with sweeter stimuli. For example, round chocolates were found to taste sweeter than other shapes.
Research has found that color influences sweetness, as well. Strawberry mousse was sweeter and more liked on a white plate than on a black plate. Hot chocolate tasted sweeter and had more aroma in a dark cream cup than in a white or red cup–“Why? I don’t
know,” smiled Woo.
Clean label, reduced-sugar foods and beverages with high-potency and bulk sweeteners can be made even sweeter with cross-modal correspondences. Woo concluded: “As Ernest Starling, 1866–1927, Nobel Prize winner and discoverer of the first hormone put it: ‘The physiology of today is the medicine of tomorrow.’”
Alex Woo, Ph.D., Managing Director and Founder, W2O Food Innovation, Alex.Woo123@gmail.com, +1.425.985.8168, http://tinyurl.com/alex-woo-w2o
Applying Chemistry to Solve Protein Flavoring IssuesPosted on:November 10, 2014
November 7, 2014, Global Food Forums — The following is an excerpt from the Arla Foods’-sponsored “2014 Protein Trends & Technology Seminar Report: Formulating with Proteins”
One need not be an industry veteran to know the consumer’s bottom line is taste—and its close companion is flavor. Yet, as more proteins find their way into everything from sports beverages to energy bars, product developers face the attendant challenge of managing the flavor issues these in-demand ingredients present.
Robert J. McGorrin, Ph.D., department head and Jacobs-Root Professor, Food Science & Technology, Oregon State University, opened a door onto those challenges, as well as their underlying chemistry, and presented strategies for overcoming them, in his discussion, “Applying Chemistry to Solve Protein Flavoring Issues.”
Prefacing his talk with the acknowledgment that flavor can make or break a product’s commercial success and consumer acceptance, McGorrin quickly got down to explaining how and why product flavor goes wrong—whether by way of heat, processing, oxidation, pH fluctuations or interactions with other ingredients—namely, proteins.
It’s not that proteins themselves contribute unwanted flavors— although volatile impurities in protein ingredients (and amino acids) certainly can. Rather, it’s what happens when
proteins bind, absorb, release or otherwise react with constituents of the product matrix—flavor ingredients, in particular. The off-notes that result are infamous among product developers, and McGorrin presented an inventory of classic flavor defects attributable to common protein sources and ingredients.
For instance, alcohol- and ketone-containing flavors might form hydrophobic bonds with the beta-lactoglobulin proteins in whey. While these bonds are largely reversible, more
permanent covalent bonds can form between aldehydes, like the benzaldehyde responsible for cherry flavor, and the amino acid dipeptide aspartame in, say, an artificially
sweetened soda. When this happens, McGorrin explained, what’s known as a Schiff base forms, and over the soda’s shelflife at room temperature, both the cherry character and its sweetness can disappear.
By analogy, the same types of Schiff reactions can occur between flavors and proteins.
McGorrin also noted that sulfur-containing flavors, like mercaptans and thiols, can form disulfide bonds with the amino acids cysteine and methionine, yielding burnt-rubber and cabbage off-notes, particularly in retorted beverages. And, there are more reactions where those came from, all with sufficiently complex chemistry. As a rule of thumb, he said, flavor-binding strength and propensity are related to protein type, with soy and whey binding more readily than gelatin, casein or corn, generally speaking.
Bringing matters back to the benchtop, McGorrin turned his focus to protein-boosted products—beverages in particular. He noted they are on the more challenging end of the
formulation spectrum because of their high water activity (Aw) and being part of a “dynamic” product medium. Because protein beverages are normally thermally processed,
flavors often change during heating, or are lost by reactions with other ingredients (flavor “scalping”).
However, beverages also often have advantages in regards to flavor stability, since they are usually refrigerated. McGorrin quoted colleagues who say formulators often have to use flavors “by the bucket-load”—upwards of four to 10 times the normal amount—to counter act losses and changes that take place in beverages formulated for high-protein content. He then laid out four hypothetical challenges that high-protein formulations often face, and several strategies to address them:
1. Flavor congruency: When dealing with general protein off-flavors, consider following what McGorrin calls a flavor congruency approach—the formulation equivalent of “If you can’t beat ‘em, join ‘em.” In other words, if the challenge is an earthy pea protein or a beany soy protein, select a flavor profile that’s supposed to include those “off” notes, like peanut or nut flavors. Or simply co-opt the off-flavor as part of the intended profile.
In this case, a green note in a soy protein could round out a “jammy” strawberry into a more true-to-fruit flavor.
2. Soy’s bitterness: When soy proteins encounter low pH levels, bitterness results. McGorrin credited vanilla and peach flavors with masking both that bitterness and soy’s notorious beany notes. And, if the beverage can be processed either with high shear or
nano-processing, he added, the improved emulsion stability will contribute creaminess and improve flavoring efficiency.
3. Bitter blocking: Another way of addressing bitterness, McGorrin went on, is to counterbalance it with increased sweetness. However, in an era of calorie restriction, that may not be an option. The solution here, he said, is to use bitter blockers that “distract” the senses from the bitterness. He listed sodium chloride, monosodium glutamate and adenosine monophosphate as examples, but noted that flavor houses can build proprietary solutions.
4. Avoiding astringency: When whey beverages drop below a certain pH—3.5 is often the cutoff—they can become astringent, which is the sensation that comes from the interaction of saliva proteins with constituents in the drink. One hedge against this is to raise pH—but that introduces protein-stability and beverage clarity issues. Alternatively, McGorrin suggested adopting a tropical flavor profile, such as mango, pineapple and coconut, all of which can overcome bitterness. Peach, citrus and apple can also counteract some astringency, he added.
Regardless of the challenge or solution, McGorrin recommended working with suppliers
early and often in the R&D process. While one doesn’t have to disclose deep formulation
secrets, data about moisture content, pH, heat processing, storage conditions, percentage protein, and the addition of other vitamins, minerals and high-intensity sweeteners can help flavor partners put together a successful and efficient flavor solution that cuts time to market and makes good on both the promise of protein and a company’s promise to its consumers.
Robert J. McGorrin, Ph.D., Department Head & Jacobs-Root Professor, Food Science & Technology, Oregon State University, Robert.email@example.com., http://oregonstate.edu/foodsci/
DIAAS and How the World Will Measure Protein QualityPosted on:
October 31, 2014, Global Food Forums — The following is an excerpt from the Arla Foods’-sponsored
In a world where the population is growing by leaps and bounds, not only food, but the quality of that food, will become increasingly important. High- quality protein is essential for growth and maintaining a healthy body. In addition, it is imperative that decision-makers
have a tool to properly assess protein quality, so they can make good decisions when it comes to creating policy, establishing regulations and ensuring the public health.
In 1989, the Food and Agricultural Organization of the United Nations (FAO) proposed that the PDCAAS be utilized as a tool for evaluating protein quality, said Joyce Boye, Ph.D., Agriculture & Agri-Food Canada. This is determined by multiplying the limiting amino acid score by protein digestibility. The limiting amino acid score is defined as “The ratio of first limiting amino acid in a gram of target food to that in a reference protein or requirement.”
PDCAAS has been utilized since that time for determining protein quality. There are a number of concerns with regards to this tool, however. These include the need to establish specific analytical methods for measuring amino acids in different foods; under- or overestimating the actual bioavailability of foods, especially when it came to
addressing potential amino acid availability; and a failure to account for the difference between protein digestibility and amino acid digestibility. To address these concerns and review other tools for evaluating protein quality, the FAO established an Expert Consultation group.
This group issued its recommendations in 2013. Among these recommendations were:
• Dietary amino acids should be treated as individual nutrients;
• Digestible amino acids should be used to calculate protein digestibility as opposed to digestible protein;
• When evaluating lysine, available or reactive lysine should be used;
• Ileal amino acid digestibility should be used; and
• Determinations for each indispensable amino acid should preferably be determined using humans. If this is not possible, pigs or rats should be used.
Different scoring patterns were also included in these recommendations. The recommendations included those for infants, young and older children, plus considerations for regulatory applications.
The Expert Consultation group recommended that the Digestible Indispensable Amino Acid Score, or DIAAS, be adopted to replace PDCAAS. Percent DIAAS may be
defined as follows. DIAAS % = 100 x [(mg of digestible dietary IAA in 1g of the dietary protein)/(mg of the same dietary IAA in 1g of the reference protein)].
The values are calculated for each indispensable amino acid (IAA) and the lowest value is designated as the DIAAS.
There are, however, challenges that must be addressed with DIAAS. One of these is the method to determine true ileal digestibility and the current dearth of data on this all-important factor. In the interim, options include utilizing protein digestibility as an equivalent for amino acid digestibility; and if true ileal protein digestibility values are unavailable, utilizing true fecal protein digestibility as a substitute; and using protein digestibility to calculate digestible individual amino acids.
There are many challenges that must be met to enhance the overall food supply and, specifically, to enhance overall protein quality. Boye concluded by listing suggestions to
help move forward in reaching these goals. The suggestions were that more data is needed on the true ileal amino acid digestibility of human foods (i.e., using human and animal models) and the need for inter-species (human, pig, rat) true ileal amino acid digestibility comparisons. Also, there is a need for data on the impact of processing, anti-nutritional factors, matrix effects, etc., on protein quality and clear recommendations on practical applications of DIAAS and implications on food supply (e.g., CODEX applications).
Joyce Boye, Ph.D., Agriculture & Agri-Food Canada, firstname.lastname@example.org, http://ow.ly/wVIoD
Protein in Support of Skeletal Muscle Health: The Science Behind Recommendations for Athletes and “Mere” MortalsPosted on:
October 22, 2014, Global Food Forums — The following is an excerpt from the Arla Foods’-sponsored “2014 Protein Trends & Technology Seminar Report: Formulating with Proteins”
Muscle loss with aging (sarcopenia) is an important issue. Studies show that maintenance of muscle mass and strength can reduce risk for chronic health problems and is accomplished by the elderly through protein consumption and exercise.
“If strength is a function of skeletal muscle mass, then the data suggests two things. The greater strength/muscle mass means reduced risk for death, all-cause or cancer-related, especially for those over 60 years of age. And, aging people need to practice strategies to retain muscle, such as
physical activity and adequate (spaced and timed) high-quality protein,” explained Stuart M. Phillips, Ph.D., at McMaster University.
Data suggest that there is an advantage to consuming more protein than the RDA suggests, especially for older persons. However, aging is associated with reduced food intake, predisposing the elderly to energy-protein under-nutrition. One study showed that nitrogen excretion, muscle area and strength decreased in older subjects fed an isocaloric diet containing protein at the RDA. Phillips speculated that there would be greater benefit seen with higher intakes, yet many older adults are not consuming these intakes.
Athletes are another story. They do things that most others do not—such as losing 26lbs in 10 days to make weight to quality for an athletic event—but strength and endurance must be preserved at all costs. They may want to gain 15lbs of muscle in a 16-week off-season training program to make the team, but not lose speed. Or, they may need to get down to 4-5% body fat prior to the Olympic Games, for the springboard competition, but maintain muscle mass/strength/power.
Phillips went on to state that variations in protein synthesis affect muscle mass and are affected by protein ingestion and loading. After exercise, studies show that, in young men, the optimal amount of protein intake for a maximal rate of muscle protein synthesis is ~0.25g protein/kg per meal. This maximally stimulates muscle protein synthesis after resistance exercise.
In elderly men, ~0.38g protein/kg per meal is shown to maximally stimulate muscle protein synthesis after resistance exercise. Phillips presented a theoretical calculation showing that younger persons who wished to optimize muscle protein synthesis at each meal feeding should be eating, at most, four times daily (4 times 0.25) plus a larger pre-sleep meal, to counteract overnight loss of muscle mass, as to promote optimal repair/recovery of muscle protein (0.5), for a daily protein intake of at least 1.5g protein per kg, per day.
Phillips stressed that this was a minimal estimate, based on studies from isolated proteins. In addition, there is an upper limit of ~2.2g protein per kg per day beyond which protein can be consumed—but is not likely contributing to gains in muscle mass.
Protein source is also important. Post-exercise consumption of milk promoted greater net protein balance than soy. Milk proteins are more effective in promoting protein accretion following resistance exercise than soy proteins, Phillips concluded. After 12 weeks of resistance training with milk consumption, significantly greater lean mass gains were shown in young men than those consuming soy or control. Milk is so effective, due to its combination of “fast” (whey) and “slow” (casein) proteins. When whey is consumed, the rise in the blood levels of amino acids is more rapid than with casein or soy consumption.
Whey promotes a greater increase in both rested and exercised muscle protein synthesis and is more effective than soy or casein in promoting anabolism following exercise. Whey is shown to promote a greater rise in muscle protein synthesis than casein, at rest or with resistance exercise in
older men. Whey protein is more effective than soy, and 40g is better than 20g in stimulating muscle protein synthesis. Data suggest high levels of the amino acid leucine in whey are acting as an effective trigger for muscle protein synthesis.
Finally, Phillips said we need to dispel the myth that too much protein causes kidney and liver problems. This is categorically incorrect, as there is no data linking higher-protein diets to renal disease, as agreed upon by the IOM and the WHO/FAO reports.
Stuart M. Phillips, Ph.D., Exercise and Metabolism Research Group, McMaster University, email@example.com, www.science.mcmaster.ca/kinesiology/emrg/
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- Flavorings: Clean and Friendly on
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