UNJURY Chocolate Whey Splendor Protein Powder - Container

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UNJURY Chocolate Whey Splendor Protein Powder - Container

This product is similar to UNJURY Chocolate Classic. The difference is that in UNJURY Chocolate Splendor, one of the sweeteners is a small amount of sucralose, the sweetener in Splenda®. In UNJURY Chocolate Classic, we use a small amount of aspartame, the sweetener in Equal, instead of sucralose.

Create a great tasting protein shake, a fresh cold protein smoothie or add quality protein to your own protein recipes.

Control Hunger and Give Your Body the Protein It Needs!

Clinical research indicates that diets higher in protein create greater satisfaction, less hunger, and weight loss success. Developed by a clinical dietitian, UNJURY works to satisfy your hunger -- and greater satisfaction helps you lose weight. You don't have to watch calories. Instead, UNJURY lessens hunger by providing a vital nutrient to your diet -- protein!

Your Body Needs Quality Protein.

Sufficient protein is essential for a healthy immune system and good energy levels. In an effort to avoid fat and cholesterol, dieters often avoid foods such as meat and cheese. Unfortunately, these foods are good sources of protein. Reducing protein intake can negatively effect on both weight loss and overall health. It appears that when we don't get enough high-quality protein -- your satiety decreases and a sense of feeling hungry can increase. UNJURY helps your body get the quality protein it needs.

UNJURY Means Trusted Taste and Quality

UNJURY is Medical Quality Protein™ trusted and highly recommended by doctors, dietitians and nurses -- and their patients. Our reputation is built upon an unwavering commitment to taste, tolerability and quality. UNJURY uses only Whey Protein Isolate -- and receives the highest score (100) on the protein quality scoring system recommended by the Institute of Medicine at the National Academy of Sciences. UNJURY is protein you can trust..../ UNJURY Chocolate Whey Splendor Protein Powder - Container / whey protein


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  • Designed by a Registered Dietitian, and Recommended by Leading Hospitals, Doctors, Dietitians and Nurses nationwide.
  • UNJURY uses only the highest quality whey protein isolate.
  • UNJURY tastes great in milk, recipes and shakes! 100% Satisfaction Gaurantee.
  • One scoop of Unjury provides 20 grams of protein, as much as 3 eggs, without the fat and cholesterol.
  • UNJURY Chocolate Splendor Protein container has 17 scoops.
.../ UNJURY Chocolate Whey Splendor Protein Powder - Container / whey protein


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UNJURY Chocolate Whey Splendor Protein Powder - Container

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UNJURY Chocolate Whey Splendor Protein Powder - Container


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Protein-Based Films and Coatings

Protein-Based Films and Coatings

This volume presents the most up-to-date and detailed information available on protein-based biopolymer films and coatings. It provides a comprehensive overview of the design, technology, properties, functionality, and applications of biopolymer films and coatings (edible and inedible) from plant and animal proteins. Both widely commercialized and envisioned applications of protein films are discussed, including hard and soft gelatin capsules, microcapsules, collagen casings, and meat and produce coatings. Expert contributors provide thorough reviews of related interdisciplinary research and extensive lists of references.

About the Editor:

Aristippos Gennadios, Ph.D. is Senior Manager, Materials Science and Clinical Supplies, Product Development: US and Canada, Banner Pharmacaps Inc. (a Sobel NV Company) in High Point, North Carolina. He received his B.S. in Chemical Engineering from the National Technical University in Athens, Greece, his M.S. in Agricultural Engineering from Clemson University, and his Ph.D. in Agricultural and Biological Systems Engineering from the University of Nebraska in Lincoln. Dr. Gennadios is also Adjunct Associate Professor in the Department of Biological Systems Engineering at the University of Nebraska in Lincoln. He has authored or co-authored over 40 refereed publications and has been granted 2 U.S. patents. ...Read more

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Protein-Based Films and Coatings



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Protein-Based Films and Coatings

Protein-Based Films and Coatings

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Green tea and grape seed extracts to control Listeria monocytogenes, Escherichia coli O157: H7 and Salmonella Typhimurium in whey protein edible film ... monocytogenes and Escherichia coli O157:H7.

IMAGE OF Green tea and grape seed extracts to control Listeria monocytogenes, Escherichia coli O157: H7 and Salmonella Typhimurium in whey protein edible film ... monocytogenes and Escherichia coli O157:H7.

Green tea and grape seed extracts to control Listeria monocytogenes, Escherichia coli O157: H7 and Salmonella Typhimurium in whey protein edible film ... monocytogenes and Escherichia coli O157:H7.

Green tea and grape seed extracts to control Listeria monocytogenes, Escherichia coli O157: H7 and Salmonella Typhimurium in whey protein edible film ... monocytogenes and Escherichia coli O157:H7.




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Green tea and grape seed extracts to control Listeria monocytogenes, Escherichia coli O157: H7 and Salmonella Typhimurium in whey protein edible film ... monocytogenes and Escherichia coli O157:H7.

Green tea and grape seed extracts to control Listeria monocytogenes, Escherichia coli O157: H7 and Salmonella Typhimurium in whey protein edible film ... monocytogenes and Escherichia coli O157:H7.Foodborne diseases caused by Listeria monocytogenes, E. coli O157:H7 and Salmonella Typhimurium have been associated with the consumption of a range of food products including ready-to-eat poultry and meat products. There is an increasing interest in natural therapies and consumer demand for effective, safe, natural products. Hence, it is important to investigate antimicrobial activities of plant extracts as potential sources of novel antimicrobials. Combinations of natural antimicrobials can serve as potential intervention strategies for controlling foodborne pathogens. Also, understanding mode of action of grape seed extract (GSE) and green tea extract (GTE) is important if they are to find commercial application as natural preservatives. Therefore, the objectives of this study were to evaluate the inhibitory effect of GSE and GTE combined with nisin (N) and malic acid (MA) in whey protein edible films against the three major pathogens in the turkey frankfurter system and to investigate the mode of action of GTE and GSE in inhibiting the pathogens. GSE and GTE had synergistic effects when combined with N and MA and lowered the Listeria monocytogenes population by 4.6 log cycles after 28 days in turkey frankfurters stored at 4 °C. No such synergistic effects between the extracts and N and MA were observed in Salmonella Typhimurium and E. coli O157:H7. MA alone lowered the Salmonella Typhimurium population by 3.3 log cycles compared to the control, while the combination of N, MA, GSE and EDTA lowered the counts by 2.0 log cycles only compared to the control. The E. coli O157:H7 population was lowered by 4.6 log cycles compared to the control, while combination of N, MA, GSE and EDTA lowered the counts by 3.4 log cycles. GSE and GTE had bactericidal effects on Listeria monocytogenes and E. coli O157:H7 at concentrations of more than 4 and 6 mg/ml, respectively. At bactericidal concentrations GSE and GTE resulted in a high percentage (90%) of cells with propidium iodide uptake in Listeria monocytogenes and E. coli O157:H7, respectively. Cell killing was accompanied by depletion in the ATP pools of the cells due to cellular cytoplasmic leakage, indicating that the bactericidal activity of GSE and GTE results from damage to the cytoplasmic membrane. Both GSE and GTE inhibited the membrane bound ATPase activity significantly at concentrations of more than 2 and 6 mg/ml in Listeria monocytogenes and E. coli O157:H7, respectively.


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Heat Induced Interactions between Casein, Whey Proteins and Lecithins: Study of Heat Induced Interactions and Aggregation of Casein Micelles with Whey Proteins, and Effect of Lecithins

IMAGE OF Heat Induced Interactions between Casein, Whey Proteins and Lecithins: Study of Heat Induced Interactions and Aggregation of Casein Micelles with Whey Proteins, and  Effect of Lecithins

Heat Induced Interactions between Casein, Whey Proteins and Lecithins: Study of Heat Induced Interactions and Aggregation of Casein Micelles with Whey Proteins, and  Effect of Lecithins

Heat Induced Interactions between Casein, Whey Proteins and Lecithins: Study of Heat Induced Interactions and Aggregation of Casein Micelles with Whey Proteins, and Effect of Lecithins




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Heat Induced Interactions between Casein, Whey Proteins and Lecithins: Study of Heat Induced Interactions and Aggregation of Casein Micelles with Whey Proteins, and  Effect of Lecithins

Heat Induced Interactions between Casein, Whey Proteins and Lecithins: Study of Heat Induced Interactions and Aggregation of Casein Micelles with Whey Proteins, and  Effect of LecithinsMilk proteins consist of casein micelles and whey proteins. Heat treatments cause denaturation of whey proteins. The denatured whey proteins may either form whey protein aggregates or may provoke whey protein coating of the casein micelles. This research focused on the effect of heat on the properties of milk proteins and their heat-induced interactions. This effect was studied in different concentrations of whey proteins and different types and concentrations of lecithins, by using three techniques; Photon Correlation Spectroscopy (PCS), Centrifugal Photosedimentometry or Centrifugal Particle Size Analyser and Differential Scanning Calorimetry (DSC). From the overall results obtained, it was concluded that the heat-induced interaction between casein micelles and whey proteins could be reduced by addition of hydrophilic lecithins, which could be due to the fact that the latter stabilises the unfolded state of the denatured whey proteins and hence minimises its aggregation and interaction with other proteins.


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Characterization of heat cured and transglutaminase cross-linked whey protein-based edible films.

Characterization of heat cured and transglutaminase cross-linked whey protein-based edible films.

Edible whey protein films were produced using whey protein isolate (WPI), glycerol and candelilla wax. Films were also produced with the addition of microbial transglutaminase (TG) to the film forming solution after heating. Both sets of films were vacuum heat cured for 0, 12 and 24h at 90°C. The effect of heat curing and transglutaminase treatments on mechanical properties [tensile strength (TS), elongation at break (%E) and toughness], the free suflhydryl, disulfide, and lysine contents and degree of cross-linking of WPI films were assessed. Heat curing increased the TS of WPI and WPI/TG films compared to uncured films. Heat curing films for 24h had increased %E compared to other films. Heat curing increased the toughness of WPI films. Heat curing decreased the free sulfhydryl content of WPI and WPI/TG films. The disulfide bond content of WPI films heat cured for 12h was higher than for films heat cured at 0 and 24h. The disulfide content of WPI/TG films heat cured for 12 and 24h was higher than for films at 0 and 48h. Heat cured WPI films had lower lysine content compared to uncured films. WPI/TG films heat cured for 24h had lower lysine content compared to films heat cured at 0 and 12h. SDS-PAGE was used to confirm heat curing and TG treatment resulted in the formation of covalent cross-links, between whey protein fractions. The water vapor permeability (WVP) of WPI and WPI/TG films heat cured for 0 and 24h was determined at 37.8°C and 85% RH as well as the oxygen permeability at 23°C and 0% RH. Moisture sorption isotherms (MSI) of films were determined at 23°C and 5°C using the Guggenheim-Anderson-de Boer equation (GAB). Heat curing WPI/TG films reduced the WVP compared to uncured WPI, WPI/TG and cured WPI films. The addition of TG reduced the oxygen permeability (O2P) compared to films without TG. Heat curing reduced the O2P of films compared to uncured films. Heat curing of WPI/TG films produced the greatest reduction in O2P of films tested. The moisture sorption isotherm of WPI and WPI/TG films heat cured for 0 and 24h at 90°C were found to closely follow the GAB mode) at 5 and 23°C. The films MSI, at 5°C were higher than the MSI of films at 23°C. The ultraviolet and visible light transmission and the color characteristics of WPI and WPI/TG films heat cured for 0 and 24h were assessed. Heat curing increased the yellowness of films. All films had low transmission of ultraviolet light. The effect of heat curing and transglutaminase treatments on the thermal properties (melting onset temperature, peak melting temperature and enthalpy of fusion) of whey protein isolate films with and without transglutaminase, and heat cured at 90°C for 0, 12 and 24h was assessed. The peak melting temperatures for films increased with heat curing and time. ...Read more

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Characterization of heat cured and transglutaminase cross-linked whey protein-based edible films.



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Characterization of heat cured and transglutaminase cross-linked whey protein-based edible films.

Characterization of heat cured and transglutaminase cross-linked whey protein-based edible films.

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