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3/4/2013

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The Surprising Versatility of Leucine

The role of leucine in metabolism, disease prevention, and sports performance.

Jenna A. Bell, PhD, RDSponsored by Daisy Brand Cottage Cheese

Objective of Presentation:

• Define Leucine

• Define leucine’s role in diet

• Recommended intake of Leucine

• Sources of Leucine in diet

• Leucine’s beneficial effects on:

– Protein synthesis, fat loss, hydration, metabolic syndrome markers, insulin sensitivity, and glucose management.

– The effects of sarcopenia and cachetic diseases

• Leucine’s role in exercise performance

• Leucine-rich recipes

What is Leucine?

What is Leucine?

• Leucine is an essential branched-chain amino

acid (BCAA) that cannot be produced in the

body, it must be obtained through the diet.

• It is abundant in all protein sources.

• It impacts several processes associated with

metabolism, including insulin signaling in

muscle, liver and fat.

Zhang, Guo, LeBlanc, Loh, Schwartz, and Yu 2007

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What is Leucine?, cont.

• The most profound effects of dietary leucine appear when combined with a High Fat Diet (HFD).

• Studies show that when combined with a HFD, doubling the intake of dietary leucine reduces: – Adipose tissue inflammation

– Insulin intolerance

– Glucose intolerance

– Hepatic steatosis (accumulation of fats in the liver)

– Hepatic lipid deposition

• And it improves multiple aspects of the metabolic profile.

Macotela, Emanuelli, Bang, Espinoza, Boucher, Beebe, Gall and Kahn 2011.

Leucine’s Effect on Diet

Leucine’s Effect on Overall Diet

• During caloric restriction, leucine has shown

to result in more fat loss and improved protein

synthesis in liver and muscle.

• Leucine acts as an activator of protein

synthesis and a suppressor of protein

breakdown.

• It also inhibits insulin signaling and decreases

glucose utilization in skeletal muscles.

Layman and Walker, 2006Freudenberg et al 2011

Leucine and High Protein Diets

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Leucine’s Role in High Protein Diets

• Studies suggest that a higher protein diet can be beneficial during weight loss and that the effects are largely derived from leucine.

• Leucine is suggested to influence energy balance and lipid metabolism.

• It also plays a key role in muscle protein turnover and skeletal muscle metabolism.

• Higher protein intake (and increased leucine) has shown to promote weight loss without reducing skeletal muscle, increase energy expenditure and fat oxidation, and reduce hepatic steatosis and plasma lipid levels.

Freudenberg et al 2011


• Diets with total protein intake >1.5 g/kg/d and carbohydrate intake <150 g/d showed:– increased weight loss

– increased loss of body fat

– attenuated loss of lean tissue

– improved glycemic control

– reduced serum triacylglyceride levels

– reduced blood pressure.

– These diets show efficacy in catabolic conditions, such as weight loss, resulting in these clinical outcomes. The spectrum of metabolic changes seen with weight loss also have specificity for the condition known as the Metabolic Syndrome.

Layman and Walker, 2006


• Freudenberg et al. studied whether leucine supplementation was able to mimic the benefits of high-protein diets on metabolic syndrome parameters in mice fed high-fat diets.

• Results show that leucine is able to mimic several effects, such as the reduced BW gain, increased skeletal muscle protein synthesis and the prevention of liver steatosis and improvement of insulin sensitivity.

• The study showed that there was a strong down-regulation of liver lipogenesis genes by high protein diets and leucine supplementation, suggesting that this is the primary mechanism limiting liver and body fat accretion.

Freudenberg, Petzke, and Klaus 2011

Leucine Dosage Recommendations

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How Much Leucine is Necessary?

• Vegetarians may have higher dietary supplementation protein needs than omnivores

• Protein intakes up to 2.0 g/kg/day are generally safe for healthy adults

• Few convincing data show that >2g/kg/day is helpful and may actually increase risk of adverse effects

• A particular protein intake goal is difficult to establish, but is influenced by energy intake and factors such as adaptation and desire to increase lean body mass versus maintenance.

• The idea of a “leucine threshold” has been proposed; that a lower dosage of leucine (5g whey protein) is required of young subjects versus a higher dosage (20 g whey protein) for elderly. This threshold must be surpassed in order for MPS to be stimulated.

Protein And Amino Acids In Sports Nutrition- Advanced Level PPT

Intake Recommendations for Athletes

• After exercise, 2.5g of leucine will stimulate muscle protein synthesis which will aid in recovery.

• Daily recommended intake is 0.8g/kg/day– ~65 g/day for a 180lb individual

– ~47 g/day for a 130lb individual

• American College of Sports Medicine– Endurance athletes: 1.2-1.4 g/kg/day

• Increased protein oxidation during endurance exercise

– Strength athletes: 1.2-1.7 g/kg/day• Essential AAs are needed to support muscle growth, particularly during early

phase of training when most significant gains in muscle occur and protein utilization is less efficient.

– Despite increased recommendations, ACSM does not state that protein supplementation has a positive impact on athletic performance.


Intake Recommendations for Athletes

• The dose of protein in younger men that maximally stimulated muscle protein synthesis (MPS) was found to be approximately 20g, which corresponds to approximately 8.5g essential amino acids (EAA) or 1.5g leucine.

• The addition of carbohydrate does not appear to enhance MPS further than the protein itself (AW Staples and SM Phillips, unpublished results), consistent with the concept that insulin is a permissive hormone for protein synthesis and not stimulatory.

• Optimal stimulation of MPS post-exercise would include:

• At least 25g high-quality protein containing at least 10g EAA, higher leucine content would appear to be advantageous, delivered as soon as possible post-exercise.

Phillips 2010

What are the Sources for Leucine

in Diet?

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Leucine Content in Various Proteins

• A recent animal study has shown that the leucinecontent of a meal determines its capacity to maximally stimulate the muscle protein synthesis.

– Whey protein (higher leucine) activates protein synthesis more than wheat protein (lower leucine).

• Human studies have shown that leucine-rich protein sources such as whey are better at stimulating muscle growth than sources with less leucine, such as soy.

• For example, compared with soy protein, whey promoted more muscle protein synthesis

– By 18% at rest (P=.067)

– By 31% following resistance exercise (P<.05)


Sources of Leucine in the Diet

• 1 cup of low fat cottage cheese (2%) has 31 g

protein

• This translates to 31,000 mg of amino acids

• The branched-chain amino acid content of the

cottage cheese (leucine + isoleucine + valine)

is 6,942 mg (6.9 g)


Leucine Content of Selected Protein

Sources


Protein Content of Various Foods


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Leucine Sources: Whey vs. Casein

• Whey protein shows greater effects in increasing plasma amino acids and muscle protein synthesis in the first 3.5 hours after a meal versus casein.

• However, the casein treatment promotes more sustained plasma amino acid levels and higher protein synthesis 3.5 to 6 hr after the meal.

– Both proteins result in comparable amounts of protein synthesis by the end of a 6-h study. Thus, it appears that whey and casein complement each other well for promoting muscle protein synthesis.

Reitelseder S, Agergaard J, Doessing S, Helmark IC, Lund P, Kristensen NB, Frystyk J, Flyvbjerg A, Schjerling P, van Hall G, Kjaer M, & Holm L. Am. J. 2011.

Leucine and Dairy Products

• There is some evidence that low fat milk products like cottage cheese, milk, and yogurt, in combination with restricted energy intake and increased exercise, can help maintain muscle while losing fat mass.

• In a study of premenopausal women, while engaging in a diet and exercise program, consuming a high protein, high dairy diet (low fat dairy, specifically) was more effective at retaining lean muscle mass.

– From this experiment, also, it is hypothesized that the higher intakes of calcium led to a greater reduction of inflammatory biomarkers as well as aiding in fat loss.

Josse AR, Atkinson SA, Tarnopolsky MA, & Phillips SM, 2011.

Dairy Products and Leucine

Leucine, Dairy, and Metabolic

Syndrome• Dairy foods and dietary calcium are potential regulators of body

weight and insulin sensitivity.

• In the majority of intervention studies examining the impact of dairy foods and calcium (Ca) on metabolic outcomes, Ca consumed with dairy foods exerted a greater effect than equal amounts of Caconsumed as a supplement.

• It has been shown that a complete dairy diet containing high or low amounts of Ca attenuated weight gain in diet-induced obese rats better than casein or whey alone. – This supports the findings that some component of dairy food acts in

concert with Ca to enhance these positive effects.

• In a study involving obese rats, Eller et al. found that both leucineand complete dairy reduced body weight, and leucine alone was associated with a robust insulin-sensitizing effect.

Eller, Saha, Shearer, and Reimer, 2012

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Syndrome, cont.• Dairy foods, such as cottage cheese, yogurt and milk, are a rich

source of both essential amino acids and branched chain amino acids, particularly leucine. – Both leucine and antagonism of cellular Ca have been shown to

decrease energy storage in adipocytes and increase fatty acid oxidation in muscle.

– Leucine is the likely mediator of these beneficial effects via an increase in mitochondrial mass, whose biogenesis is regulated by leucine.

• In a study by Eller et al., it was found that protein and Ca, effected final body weight, weight gain and fat mass.

• Rats fed a complete dairy (powdered skim milk) and leucine diets had significantly lower final body weight than those fed casein.

• High dietary Ca also reduced final body weight, weight gain and fat mass compared to low dietary Ca. It also showed significant improvements in bone mineral density.



Syndrome, cont.• Eller et al. found that a complete dairy diet altered genes associated

with fatty acid metabolism in hepatic tissue.

• Consumption of leucine improved whole-body insulin sensitivity, reduced fat mass, and alterations in gene expressions in insulin signaling and related metabolic pathways.

• Collectively, leucine regulated glucose homeostasis and may be one important bioactive component found in dairy foods.

– Certain genes that are known regulators of insulin sensitivity, glucose uptake, food intake, and energy expenditure were effected positively with leucine treatment.

– The Zhang et al. study showed a reduction in adiposity due to an increased resting energy expenditure in mice after doubling the leucine supplementation in drinking water.

Eller, Saha, Shearer, and Reimer, 2012Zhang, Guo, LeBlanc, Loh, Schwartz, and Yu

2007

Possible Mechanisms for Benefits of

Dairy’s Role in Metabolic Syndrome

– The changes in energy metabolism mediated through calcitriol and parathyroid hormone in response to dietary Ca supplementation.

• By forming insoluble soaps in the intestine, dietary Camay increase fecal fat excretion.

– Complete dairy diets effect the nutrient utilization pathways and fatty acid metabolism in both skeletal muscle and liver.

• Changes to regulation of beta-oxidation in the liver may reflect a change in nutrient partitioning and a possible alteration in metabolic rate and substrate utilization.


Leucine’s Effect on Hydration

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Leucine’s Effect on Hydration

• In a study of healthy men, an energy density-

matched rehydration beverage that contained

milk protein in addition to carbohydrate was

retained better than a rehydration beverage

that contained only carbohydrate.

• Post-exercise, rehydrating with a protein, or

milk-based drink will be more effective than a

solely carbohydrate-based drink.

James LJ, Clayton D, & Evans GH. 2011.

Leucine and Insulin

Leucine and Its Effects on Insulin

• In a study by Macotela et al., leucine was

found to have a profound impact on the risk of

diabetes.

• By doubling dietary leucine intake in mice on a

HFD, many metabolite abnormalities were

reversed and a marked improvement in

glucose tolerance and insulin signaling were

recorded.

Macotela, Emanuelli, Bang, Espinoza, Boucher, Beebe, Gall and Kahn. 2011.

Leucine and Its Effects on Insulin, cont.

• The Macotela et al. study showed:– A decrease in subcutaneous fat and in inflammation and

fat content of liver

– Improved glucose tolerance and insulin signaling

– Reduced inflammation of adipose tissue

– Improved leucine metabolism

– Improved glucose and energy metabolism

– Reductions in fatty acids and serum levels in long chain free fatty acids

– Reductions in perigonadal fat content

– Near-normalization of elevated cholesterol levels resulting from HFDs.


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Leucine, Metabolic Syndrome and

Insulin


Leucine and Glucose Management

Leucine’s Role in Glucose Management

• Leucine is known to interact with the insulin signaling pathway to stimulate downstream signal control of protein synthesis, resulting in maintenance of muscle protein during periods of restricted energy intake.

• Leucine also appears to modulate insulin signaling and glucose use by skeletal muscle. Whereas total protein is important in providing substrates for gluconeogenesis, leucine appears to regulate oxidative use of glucose by skeletal muscle through stimulation of glucose recycling via the glucose alanine cycle.– These mechanisms produce protein sparing and provide a

stable glucose environment with low insulin responses during energy-restricted periods.



• High-protein, low-carbohydrate diets achieve glycemic control by shifting regulation from insulin-mediated peripheral glucose disposal to hepatic regulation of glucose appearance. – Diets with reduced levels of carbohydrates minimize postprandial glucose and

insulin responses and minimize the role of liver glycogen in maintaining fasting blood glucose.

– Increased dietary protein contributes amino acids to de novo synthesis of glucose via gluconeogenesis, and BCAAs increase recycling of glucose carbon via the glucose-alanine cycle.

• When intracellular levels of leucine are elevated, muscles use glucose derived from either the blood or glycogen stores as a glycolytic fuel. These mechanisms appear to be particularly important during periods of low energy intake or endurance exercise when BCAAs are increased in muscle, insulin is low, and sparing of blood glucose is important.


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• In clinical studies, persons with type 2 diabetes reduce postprandial glucose and insulin levels, reduce glycosylated hemoglobin, and increase insulin sensitivity when using isoenergetic meals that replace dietary protein for carbohydrates. – Likewise, obese subjects reduce glucose and insulin response after

such meals and specifically decrease Phase II insulin release.

• While total protein is important in providing substrates for gluconeogenesis, leucine appears to regulate oxidative use of glucose by skeletal muscle through stimulation of glucose recycling via the glucose-alanine cycle. – These mechanisms appear to provide a stable glucose environment

with low insulin responses during energy-restricted periods.


Leucine and Cholesterol

Leucine and Cholesterol

• Zhang et al. found that plasma levels of total and LDL cholesterol were decreased by 27% (P<0.001) and 53% (P<0.001), respectively, in leucinesupplemented HFD-fed mice compared with the control mice fed the same diet.

• Increases in dietary leucine intake substantially decrease diet-induced obesity, hyperglycemia, and hypercholesterolemia in mice with ad libitum consumption of HFD likely via multiple mechanisms.

Zhang et al 2007

Leucine Supplementation in Mice on

HFDs

Zhang et al 2007

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Leucine and Muscle Growth


• Philips’ 2010 study examines how the post-

exercise intake of protein, especially whey

protein for its high leucine content and rapid

digestibility, appears to more efficiently

stimulate muscle protein synthesis and should

lead to greater hypertrophy with continued

ingestion after workouts.

Phillips 2010


• The two processes of muscle protein breakdown (MPB) and muscle protein synthesis (MPS) are simultaneous and ongoing.

• Hypertrophy (a net gain of muscle) and atrophy (a net loss of muscle) result when the balance of the two processes is compromised.

• Activities such as weightlifting and resistance exercise result in hypertrophy, while aging will naturally result in some atrophy due to sarcopenic muscle loss.

• Leucine plays a key role in the stimulation and “switching on” of MPS, which is important in the elderly and also following resistance exercise.

• High quality, rapidly digested, leucine-rich proteins such as whey protein (liquid dairy) would be ideal candidates for stimulating MPS and promotion of hypertrophy.

Phillips 2010

Leucine and Exercise

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Leucine and Exercise

• Leucine and exercise:

– Adequate protein intake is critical for athletic performance and good health

– There is increasing agreement that immediate post-exercise ingestion of protein, specifically leucine, in combination with carbohydrate, has beneficial effects on:

• Muscle glycogen replenishment (carbohydrate)

• Muscle protein synthesis (leucine)

– Protein intake helps promote muscle recovery and eventual hypertrophy

Amino Acids and Sports Nutrition Module II

Timing of Protein Ingestion After

Exercise– When protein is consumed after resistance exercise,

the net effects of resistance and the accompanying hyperaminoacidemia on muscle protein synthesis are synergistic and an even greater accumulation of muscle protein is thought to sum over time to yield muscle hypertrophy.

– Studies of post-exercise protein consumption (within three hours) are unequivocal in their finding of an enhanced rate of MPS after exercise.

– The rise in MPS occurs rapidly following a maximally stimulatory bolus dose of protein being apparent within the first hour after resistance exercise and peaking at 3 hours post-exercise.

Phillips 2010

Types of Protein For Post-Exercise

Ingestion

• A number of studies have shown that different proteins elicit different anabolic (building up) responses when consumed at both a whole-body and skeletal muscle level.

• The rate of digestion and level of amino acid content will dictate the amplitude and rise of EAA and particularly leucine, which will affect the degree to which Muscle Protein Synthesis is stimulated.

• High-quality proteins (high leucine content and rapid digestibility) are beneficial for the stimulation of MPS and rehydration.

Phillips 2010


Ingestion• In trials, greater muscle protein synthesis and gain were observed

when the test subjects ingested milk over a matched soya protein. • The study lasted 12 weeks and also resulted in greater whole-body lean mass.

• Results indicated that liquid dairy proteins (specifically, milk) were superior in eliciting acute rises in MPS than soya protein.

– Aminoacidemia is slower in milk than the soya-based drink. • Milk is 80% casein and 20% whey, the casein is digested slowly, the whey

rapidly.

– The appearance of leucine in the systemic circulation was markedly different and actually more rapid in the milk condition

• Leucinemia is greater and more prolonged with milk consumption than soya, presumably reflecting the contribution of the digestion of whey proteins within the milk, which are higher in leucine than both casein and soya.

Phillips 2010

3/4/2013

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Ingestion

• Phillips observed that whey, as a hydrolyzed protein, resulted in a pronounced and rapid hyperaminoacidemia and leucinemia compared to both isonitrogenous quantities of soya and casein.

• Whey and soya promote the greatest increases in resting MPS and whey alone shows the greatest results in MPS for increments in post-resistance exercise.

• Phillips reviewed the evidence for the efficacy of whey as an exercise supplement in supporting resistance training-induced gains in lean mass and found that milk proteins and particularly whey were more effective than carbohydrate or soya supplements.

Phillips 2010

Leucine and Exercise Performance

• Deldicque and Francaux examined whether functional foods or specific dietary components could provide health benefits beyond basic nutrition and the already agreed-upon sports nutritional benefits.

• Findings for leucine included a diminished muscle soreness after exercise, enhanced endurance performance, and improved muscle strength with a dosage of 0.3-0.5 g/kg before or immediately after exercise.

• Leucine undergoes oxidation during prolonged endurance exercise; supplementation is helpful during and after such exercise possibly by limiting the increase in the ratio-free tryptophan/BCAAs, thereby reducing central fatigue.

Deldicque and Francaux, 2008

Mechanisms of BCAA on Muscle

Hypertrophy

– Branched Chain Amino Acids both reduce muscle

protein breakdown and stimulate protein

synthesis in rats, but has not been confirmed in

humans.

• The improvement in humans seems to stem from a

decrease in protein degradation primarily.

• It is possible that to promote protein synthesis in

human skeletal muscle, BCAAs must be coupled with

resistance exercise in order for signaling events leading

to protein synthesis to be activated.

Deldicque and Francaux, 2008

Leucine and Exercise regarding

Cachetic Diseases and Sarcopenia

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Leucine and Cachexia

• Breen et al.’s review is based upon the use of exercise and nutrient interventions to combat the effects of cachetic diseases (where muscle protein breakdown outpaces muscle protein synthesis).– Rapidly digested, leucine-rich protein sources may stimulate

greater post-exercise rates of MPS than other protein sources, as leucine acts as a key anabolic signal for mRNA translation.

– In conjunction with resistance exercise, leucine-rich proteins will optimize muscle growth and long-term exercise adaptation.

– Cachetic populations tend to respond positively to larger doses (40g) of amino acids following exercise than do healthy, young adults, whose response plateaus after moderate doses (20g).

Breen and Phillips 2012


• Patients respond more positively to one bolus dose of 25g of whey protein post-exercise than they do to a pulse dose of 10x2.5g over 3hours. – Greater MPS rates were still apparent 3-5 hours post-exercise with the single

bolus dose.

• Milk protein, with relatively slow aminoacidemia but potent leucinemia, is superior in potentiating resistance exercise-induced rates of MPS than soya protein.– This potency can be attributed to the digestion of whey proteins within milk,

which are higher in leucine than both casein and soya.

– These data support the use of rapidly digested leucine-rich proteins, such as whey, in conjunction with resistance exercise to promote hypertrophy.




Leucine and Sarcopenia

• Age-related muscle wasting (particularly of type II muscle fibers), sarcopenia, is due to:– Elevated basal-fasted rates of muscle protein breakdown

– Reduction in basal muscle protein synthesis• Sensitivity to amino acid dosages can be reduced with age, showing that

higher quantities of protein may be necessary to stimulate equivalent muscle protein synthesis above rest and to accrue muscle proteins.

• Leucine is thought to play a central role in mediating mRNA translation for MPS, and the elderly should ensure sufficient leucine is provided with dietary protein intake.

• Sarcopenia causes a predisposition in the elderly to illness, fractures, and other chronic metabolic conditions such as obesity and type 2 diabetes, which ultimately increases mortality.

• The elderly must ingest 20-30g of high quality, leucine-rich, rapidly digestible protein at each meal in order to elicit a robust acute muscle protein synthetic response that will aid in the accretion of muscle protein over time.

Breen and Phillips 2011.

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Leucine and Sarcopenia

Pasiakos, 2012.

Bottom Line for the Benefits of

Leucine

• Leucine is abundant in all protein food sources but is especially usable through dairy products like milk and cottage cheese.

• Supplementation of Branched Chain Amino Acids, especially leucine, during caloric restriction has shown to result in more fat loss and improved protein synthesis in liver and muscle.

• It regulates insulin signaling and impacts several metabolic processes.– The most profound effects of dietary leucine are visible in the context of a

HFD, where doubling dietary leucine reduces:• HFD-induced insulin resistance

• Inflammatory changes in adipose tissue

• Glucose intolerance

• Hepatic steatosis and lipid deposition

– And it improves:• Insulin signaling in muscle, liver and fat

• Multiple aspects of the metabolic profile

• High dietary calcium reduces body weight, weight gain and fat mass compared to low dietary calcium. It also shows significant improvements in bone mineral density.

• There is evidence that low fat milk products like cottage cheese, milk, and yogurt, in combination with restricted energy intake and increased exercise, can help maintain muscle while losing fat mass.

Leucine-Rich Recipes

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Caramelized Onion and Fig Pizza16 ounces whole grain bakery pizza dough4 teaspoons extra virgin olive oil3/4 teaspoon minced garlic1 cup Daisy Low Fat Cottage Cheese1 large sweet onion, thinly sliced1 teaspoon kosher salt2 tablespoons balsamic vinegar + extra for drizzle1/2 Bosc pear, cored and thinly sliced5 dried figs, stem removed and thinly sliced1/3 cup Gorgonzola cheese1/2 cup baby arugula

Directions: Preheat oven to 400 degrees. Heat 2 teaspoons oil in skillet over medium-high heat. Add onions and sprinkle of salt. Stir frequently until onion softens. Reduce heat to medium-low and partially cover with lid. Cook for 20 minutes, stirring occasionally. Prepare pizza dough by rolling out to 16 inch pie. Dust pan or baking stone with corn meal or spray with cooking spray to prevent sticking. Add flattened dough. In small bowl, combine garlic with 2 teaspoons olive oil. Spread olive oil mixture evenly onto pizza. Spread cottage cheese onto pizza. Top with caramelized onions. Layer with pears, figs, and Gorgonzola cheese. Bake for 20-25 minutes until crust is golden brown. Move to cutting board. Before slicing, garnish with arugula and balsamic drizzle. Cut into 8 slices.

www.daisybrandhealth.com

Crispy Kale with Creamy Herb Dip

8 ounces fresh kale

1 tablespoon olive oil

1/2 cup Daisy Brand Cottage Cheese

2 tablespoons skim milk

1 tablespoon garlic & herb salad dressing mix

(from a .75 ounce packet)

1 tablespoon fresh lemon juice

Directions: Heat the oven to 350 degrees. Cut out the tough stems from the kale; tear

into bite-sized pieces. Wash the kale; place in salad spinner and spin all the water out;

repeat spinning to ensure the kale is completely dry. Place the kale in a large bowl.

Drizzle with the oil tossing to coat the leaves in oil. Arrange kale in a single layer on a

baking sheet. Bake the kale for 10-15 minutes or just until the leaves are crisp.

Meanwhile, blend the cottage cheese, milk, salad dressing mix and lemon juice in a

blender or food processor until almost smooth. Serve with Kale Chips.

www.daisybrandhealth.com

Apple, Banana, Cinnamon Smoothie1 cup Daisy Brand Cottage Cheese

1 cup apple sauce

1/2 cup milk

1 cup cracked ice

1 medium banana, cut in chunks

1 teaspoon ground cinnamon

2 tablespoons brown sugar Directions: Place all of the ingredients in a blender container and cover. Blend on High for 30 to 45 seconds or until smooth.

www.daisybrand.com www.daisybrand.com

Apple-Walnut Breakfast


1/2 cup unsweetened applesauce

1/4 teaspoon cinnamon

1/4 teaspoon nutmeg

1 tablespoon chopped walnuts

4 sliced grapes

1 tablespoon quick oatmeal

Directions: Layer the cottage cheese and the applesauce in a dish. Sprinkle with

cinnamon and nutmeg. Garnish with cut grapes, walnuts, and oats.

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Cottage Cheese, Egg and Ham Muffins:

3/4 cup all purpose flour

3/4 cup whole wheat flour

3 teaspoons baking powder

1/4 teaspoon salt


2 eggs, lightly beaten

1/3 cup vegetable oil

1/4 cup milk

1/2 cup ham, finely chopped

1/2 cup Cheddar cheese, shredded

1/4 cup green onions, sliced

Directions: Mix the flours, baking powder and salt in large bowl and set aside. Mix the cottage cheese, eggs, oil and milk in another large bowl. Fold the ham, Cheddar cheese and green onions into the cottage cheese mixture. Stir the wet mixture into the dry mixture until moistened. Spray 12 nonstick muffin cups very well with nonstick spray. Fill each muffin cup 2/3 full with batter. Bake in a preheated 375 degree oven 20 to 25 minutes or until the muffins are golden brown on top and toothpick inserted in center comes out clean. *The muffins can be made ahead and reheated.

www.daisybrand.com

Questions?

Email:

[email protected]

Reference List

Anne Freudenberg, Klaus J. Petzke, and Susanne Klaus. Journal of Nutritional Biochemistry. Vol 23: 1524-1530. October 2011

Anne Freudenberg, Klaus J. Petzke, and Susanne Klaus. The Forum for Amino Acid, Peptide, and Protein Research. 201210.1007/s00726-012-1363-2. July 31, 2012.

Donald K. Layman and Denise A. Walker. The Journal of Nutrition. Vol. 136: 319S–323S. 2006.

EAS Fitness ppts for Protein and Amino Acids in Sports Nutrition, Advance Level, Modules I & II, and Rookie Edition.

James LJ, Clayton D, & Evans GH. Br. J. Nutr. 105, 393-399. 2011Josse AR, Atkinson SA, Tarnopolsky MA, & Phillips SM. J. Nutr. 141, 1626-1634. 2011.

Leigh Breen and Stuart M. Phillips. Clinical Nutrition and Metabolic Care. Vol 15:3: 226-232. May 2012.

Leigh Breen and Stuart M. Phillips. Nutrition & Metabolism. Vol 8:68: 1-11. 2011.

Lindsay K. Eller, Doan C. Saha, Jane Shearer, and Raylene A. Reimer. Journal of

Nutritional Biochemistry. P1-10. 2013.

Louise Deldicque and Marc Francaux. Clinical Nutrition and Metabolic Care.

11:774-781. 2008.

Reitelseder S, Agergaard J, Doessing S, Helmark IC, Lund P, Kristensen NB,

Frystyk J, Flyvbjerg A, Schjerling P, van Hall G, Kjaer M, & Holm L. Am. J.

Physiol. Endocrinol. Metab. 300, E231-242. 2011.

Stefan M. Pasiakos. Nutrients. 4, 740-758. 2012.

Stuart M. Phillips. Proceedings of the Nutrition Society. 70, 100-103. 2011.

Yazmin Macotela, Brice Emanuelli, Anneli M. Bang, Daniel O. Espinoza,

Jeremie Boucher, Kirk Beebe, Walter, Gall, and C. Ronald Kahn. PLoS ONE

6(6):e21187: 1-13. June 2011.

Yiying Zhang, Kaiying Guo, Robert E. LeBlanc, Daniella Loh, Gary J. Schwartz,

and Yi-Hao Yu. Diabetes. Vol. 56: 1647-1654. June 2007.

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