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Figure 4. The protein neural network (co-occurrence chart) based on 20000 patents and NPL of the selected field. (Prtn&x) (x =mlk, why, vgtbl respectively milk, whey, vegetable), (food ingredients = Fd&ngrdnt).

Figure 4 The protein neural network (co-occurrence chart) based on 20000 patents and NPL of the selected field. (Prtn&x) (x =mlk, why, vgtbl respectively milk, whey, vegetable), (food ingredients = Fd&ngrdnt).

Related Figures (20)

Illustration 1. The “SWHPM”, interpreted by artist BS, is a disruptive prophetic concept of the author making use of Sun, Wind, Hydraulic, Photosynthesis, Gravitational, Geographical Gradients to power a mill- like generator of various energy streams.
Illustration 1. The “SWHPM”, interpreted by artist BS, is a disruptive prophetic concept of the author making use of Sun, Wind, Hydraulic, Photosynthesis, Gravitational, Geographical Gradients to power a mill- like generator of various energy streams.
Illustration 2. The Multiplying Dimensions of the Innovator, at large technical, science and business, now amount to 4C2 2Cx2C © as per Re- bouillat et al. [1]-[5].
Illustration 2. The Multiplying Dimensions of the Innovator, at large technical, science and business, now amount to 4C2 2Cx2C © as per Re- bouillat et al. [1]-[5].
Figure 1. Citations per year (Occurrence) in the field of interest using about 100 listed references used in the current review.
Figure 1. Citations per year (Occurrence) in the field of interest using about 100 listed references used in the current review.
Figure 2. The relative importance of the matters of interest in the current review using about 100 listed ref- erences used in the current review.
Figure 2. The relative importance of the matters of interest in the current review using about 100 listed ref- erences used in the current review.
Figure 3. The patent repartition per region per year in the field of interest using a sample of 5000 patents (from a standard state of the art semantic analysis using title, keywords, introduction and conclusion of the present review— selected relevance level 80%).
Figure 3. The patent repartition per region per year in the field of interest using a sample of 5000 patents (from a standard state of the art semantic analysis using title, keywords, introduction and conclusion of the present review— selected relevance level 80%).
gure 5. Relative milk component sizes in comparison with membrane pore size ranges [ 10]
gure 5. Relative milk component sizes in comparison with membrane pore size ranges [ 10]
Figure 6. Membralox GP® membrane cross section and membrane module (left). Isoflux® membrane cros section (right) from advertisement brochures. The excellent surface-active and colloid- stabilizing characteristics of milk proteins make them highly valued food ingredients, both in soluble and dispersed form [28]. Some of their main functional characteristics are solu- bility, water binding, gelling, foaming, emulsification and heat stability. Their hydrophilic and hydrophobic
Figure 6. Membralox GP® membrane cross section and membrane module (left). Isoflux® membrane cros section (right) from advertisement brochures. The excellent surface-active and colloid- stabilizing characteristics of milk proteins make them highly valued food ingredients, both in soluble and dispersed form [28]. Some of their main functional characteristics are solu- bility, water binding, gelling, foaming, emulsification and heat stability. Their hydrophilic and hydrophobic
polar nature makes them desirable emulsifiers used as fat replacers and to improve texture and increase shelf-life in diverse products such as breads, meats and frozen desserts. Thanks to their foaming properties, milk proteins can also be used in whipped products, function that has traditionally relied on eggs. MPCs are currently used as ingredients for manufacturing products including: cheese and yogurt, ice cream, dietetic formulations, cereal and energy bars, infant formulae, desserts, baked goods, toppings, low-fat spreads, sports beverages/foods and geria- tric nutritional products.
polar nature makes them desirable emulsifiers used as fat replacers and to improve texture and increase shelf-life in diverse products such as breads, meats and frozen desserts. Thanks to their foaming properties, milk proteins can also be used in whipped products, function that has traditionally relied on eggs. MPCs are currently used as ingredients for manufacturing products including: cheese and yogurt, ice cream, dietetic formulations, cereal and energy bars, infant formulae, desserts, baked goods, toppings, low-fat spreads, sports beverages/foods and geria- tric nutritional products.
Figure 8. Schematic representation of casein submicelles and casein micelle composed of submicelles held together by cal- cium phosphate. A bar chart with the amount of the different caseins that comprise the casein fraction is showed (Cn stands for Casein).
Figure 8. Schematic representation of casein submicelles and casein micelle composed of submicelles held together by cal- cium phosphate. A bar chart with the amount of the different caseins that comprise the casein fraction is showed (Cn stands for Casein).
contribute to their high surface activity, which gives them good foaming and emulsifying properties. Casein functional properties are significantly affected by changes in pH, method of preparation, ionic strength and na- ture of the salt ion [37].
contribute to their high surface activity, which gives them good foaming and emulsifying properties. Casein functional properties are significantly affected by changes in pH, method of preparation, ionic strength and na- ture of the salt ion [37].
Figure 10. Protein structure of the main whey proteins [34]. Whey protein products are produced for food, cosmetic and pharmaceutical sectors. There are diverse types of whey protein products (Figure 11): whey protein concentrate (WPC) (which contains 25% - 80% protein), whey protein isolates (WPI) (containing =90% protein), whey protein hydrolysate (which will be commented in the following section), #lactoglobulin, a-lactalbumin and protein-peptone fraction [39] [40].
Figure 10. Protein structure of the main whey proteins [34]. Whey protein products are produced for food, cosmetic and pharmaceutical sectors. There are diverse types of whey protein products (Figure 11): whey protein concentrate (WPC) (which contains 25% - 80% protein), whey protein isolates (WPI) (containing =90% protein), whey protein hydrolysate (which will be commented in the following section), #lactoglobulin, a-lactalbumin and protein-peptone fraction [39] [40].
Figure 11. General composition of WPCs.
Figure 11. General composition of WPCs.
Figure 12. Different processes of manufacture of whey products (UF, MF Ultra and Micro Filtration). ———— OD ee ae ee ee eS WPC containing 34% - 35% protein (WPC35) is also rich in lactose and minerals. It has good emulsification properties, is highly soluble and has a mild dairy flavor. This product is used in the manufacture of yogurt, processed cheese, infant formulae, and in various bakery applications. WPC is also marketed for use in stews and sauces because of their thickening properties as well as nutritional benefit. WPC with ~80% protein (WPC80) has lower carbohydrate content and is characterized by good gelation, emulsification and foaming properties. WPC80 is an excellent ingredient for sports nutrition and weight management products as well as for meat products, thanks to its high gel strength and good water- binding properties [40].
Figure 12. Different processes of manufacture of whey products (UF, MF Ultra and Micro Filtration). ———— OD ee ae ee ee eS WPC containing 34% - 35% protein (WPC35) is also rich in lactose and minerals. It has good emulsification properties, is highly soluble and has a mild dairy flavor. This product is used in the manufacture of yogurt, processed cheese, infant formulae, and in various bakery applications. WPC is also marketed for use in stews and sauces because of their thickening properties as well as nutritional benefit. WPC with ~80% protein (WPC80) has lower carbohydrate content and is characterized by good gelation, emulsification and foaming properties. WPC80 is an excellent ingredient for sports nutrition and weight management products as well as for meat products, thanks to its high gel strength and good water- binding properties [40].
Figure 13. Appearance of WPC from different sources, powdered and in solution.
Figure 13. Appearance of WPC from different sources, powdered and in solution.
Table 2. Comparisons of quality of different proteins.
Table 2. Comparisons of quality of different proteins.
Figure 14. Transglutaminase- catalyzed protein cross-linking. AEE SSE Me aS A: NE SA EO: SE MA ee eee: SSR, Sa A A Se A eh ee ST Ne Semen eee, It has been reported that properties of emulsions containing cross-linked a-lactalbumin were influenced by the sequence of cross-linking and emulsification. While cross-linking before emulsification decreased the stability of the emulsion, due to a lower rate of protein adsorption and restricted ability of protein to unfold at the oil- water interface, this stability was improved when cross-linking was carried out after emulsification [70]. In ad. dition, due to the partial unfolding of globular proteins when adsorbed at the oil-water interface, cross-linkinc after emulsification is easier and a higher increase in surface viscosity is reached [71]. In sodium-caseinate- sta bilized emulsions, it was found that cross-linking by transglutaminase before emulsification significantly im- proved the emulsion stability. In contrast, cross-linking after emulsification produced a great loss of long-tern stability due to droplet coalescence [72].
Figure 14. Transglutaminase- catalyzed protein cross-linking. AEE SSE Me aS A: NE SA EO: SE MA ee eee: SSR, Sa A A Se A eh ee ST Ne Semen eee, It has been reported that properties of emulsions containing cross-linked a-lactalbumin were influenced by the sequence of cross-linking and emulsification. While cross-linking before emulsification decreased the stability of the emulsion, due to a lower rate of protein adsorption and restricted ability of protein to unfold at the oil- water interface, this stability was improved when cross-linking was carried out after emulsification [70]. In ad. dition, due to the partial unfolding of globular proteins when adsorbed at the oil-water interface, cross-linkinc after emulsification is easier and a higher increase in surface viscosity is reached [71]. In sodium-caseinate- sta bilized emulsions, it was found that cross-linking by transglutaminase before emulsification significantly im- proved the emulsion stability. In contrast, cross-linking after emulsification produced a great loss of long-tern stability due to droplet coalescence [72].
Figure 15. Chemical structure of a bioactive peptide; casoxin Aderived from «casein, fragment (35-41), with opioid anta- gonist activity. Aminoacid sequence: Tyr-Pro-Ser-Tyr-Gly-Leu-A sn [84]. Major milk proteins (caseins, a-lactalbumin, Z-lactoglobulin) constitute an important source for bioactive peptides with a wide range of physiological properties. Milk-derived bioactive peptides were shown to have an- tihypertensive, antithrombotic, antimicrobial, antioxidant, immunomodulatory, antipyretic, opioid, mineral- binding properties and anticarcinogenic activities (Figure 15). Numerous fragments of caseins and whey pro- teins have been identified as bioactive peptides and categorized according to their particular health beneficial potentials [79] [81]-[83]. Phelan et al. published a comprehensive review regarding biological effects of case- in-derived bioactive peptides, their application in industry and safety aspects and regulations [78].
Figure 15. Chemical structure of a bioactive peptide; casoxin Aderived from «casein, fragment (35-41), with opioid anta- gonist activity. Aminoacid sequence: Tyr-Pro-Ser-Tyr-Gly-Leu-A sn [84]. Major milk proteins (caseins, a-lactalbumin, Z-lactoglobulin) constitute an important source for bioactive peptides with a wide range of physiological properties. Milk-derived bioactive peptides were shown to have an- tihypertensive, antithrombotic, antimicrobial, antioxidant, immunomodulatory, antipyretic, opioid, mineral- binding properties and anticarcinogenic activities (Figure 15). Numerous fragments of caseins and whey pro- teins have been identified as bioactive peptides and categorized according to their particular health beneficial potentials [79] [81]-[83]. Phelan et al. published a comprehensive review regarding biological effects of case- in-derived bioactive peptides, their application in industry and safety aspects and regulations [78].
Figure 18. Indication of the sites of hydrolysis of phospholipids by phospholipases type A,, Az, C, and D (left). Productior of lysophospholipid by action of phospholipase A 2 (right).
Figure 18. Indication of the sites of hydrolysis of phospholipids by phospholipases type A,, Az, C, and D (left). Productior of lysophospholipid by action of phospholipase A 2 (right).
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Bioactive PeptidesWhey Proteins
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