[1]

Code of Federal Regulations (CFR). 2023. Part 133 - Cheeses and related cheese products. pp 199. www.ecfr.gov/current/title-21/chapter-I/subchapter-B/part-133

[2]

Chandan RC, Kapoor R. 2011. Manufacturing outlines and applications of selected cheese varieties. In Dairy Ingredients for Food Processing, eds. Chandan RC, Kilara A. Iowa, USA: Wiley-Blackwell. pp. 267−316. https://doi.org/10.1002/9780470959169.ch11

[3]

Garimella Purna SK, Pollard A, Metzger LE. 2006. Effect of formulation and manufacturing parameters on process cheese food functionality—I. Trisodium Citrate. Journal of Dairy Science 89:2386−96

doi: 10.3168/jds.S0022-0302(06)72311-6
[4]

Kapoor R, Metzger LE. 2008. Process cheese: Scientific and technological aspects – A review. Comprehensive Reviews in Food Science and Food Safety 7:194−214

doi: 10.1111/j.1541-4337.2008.00040.x
[5]

Dularia C, Meena GS, Hossain S, Khetra Y, Arora S. 2023. Effect of emulsifying salts on functional, textural and rheological properties of milk protein concentrate 80 (MPC80) based processed cheese product. Food Hydrocolloids 142:108842

doi: 10.1016/j.foodhyd.2023.108842
[6]

de Kruif CG, Huppertz T, Urban VS, Petukhov AV. 2012. Casein micelles and their internal structure. Advances in Colloid Interface Science 171–172:36−52

doi: 10.1016/j.cis.2012.01.002
[7]

de Kruif CG. 1999. Casein micelle interactions. International Dairy Journal 9:183−88

doi: 10.1016/S0958-6946(99)00058-8
[8]

Dalgleish DG, Corredig M. 2012. The structure of the casein micelle of milk and its changes during processing. Annual Review of Food Science and Technology 3:449−67

doi: 10.1146/annurev-food-022811-101214
[9]

Dickinson E, McClements DJ. 1995. Molecular basis of protein functionality. In Advances in food colloids. Glasgow, UK: Blackie Academic and Professional. pp. 27−80.

[10]

Salunke P, Marella C, Metzger LE. 2021. Microfiltration and Ultrafiltration process to produce Micellar Casein and Milk Protein Concentrates with 80% Crude Protein Content: Partitioning of various protein fractions and constituents. Dairy 2:367−84

doi: 10.3390/dairy2030029
[11]

Pouliot M, Pouliot Y, Britten M. 1996. On the conventional cross-flow microfiltration of skim milk for the production of native phosphocaseinate. International Dairy Journal 6:105−11

doi: 10.1016/0958-6946(94)00046-8
[12]

Nelson BK, Barbano DM. 2005. A microfiltration process to maximize removal of serum proteins from skim milk before cheese making. Journal of Dairy Science 88:1891−900

doi: 10.3168/jds.S0022-0302(05)72865-4
[13]

Salunke P, Metzger LE. 2022. Impact of transglutaminase treatment given to the skim milk before or after microfiltration on the functionality of micellar casein concentrate used in process cheese product and comparison with rennet casein. International Dairy Journal 128:105317

doi: 10.1016/j.idairyj.2022.105317
[14]

Salunke P, Marella C, Amamcharla JK, Muthukumarappan K, Metzger LE. 2022. Use of micellar casein concentrate and milk protein concentrate treated with transglutaminase in imitation cheese products – unmelted texture. Journal of Dairy Science 105:7891−903

doi: 10.3168/jds.2022-21852
[15]

Salunke P, Marella C, Amamcharla JK, Muthukumarappan K, Metzger LE. 2022. Use of Micellar Casein Concentrate and Milk Protein Concentrate Treated with Transglutaminase in Imitation cheese products – Melt and Stretch properties. Journal of Dairy Science 105:7904−916

doi: 10.3168/jds.2022-22253
[16]

Salunke P, Metzger LE. 2023. Functional properties of milk protein concentrate and micellar casein concentrate as affected by transglutaminase treatment. Food Hydrocolloids 137:108367

doi: 10.1016/j.foodhyd.2022.108367
[17]

Salunke P, Biswas AC, Metzger LE. 2023. Manufacture of loaf-type processed cheese products using transglutaminase crosslinked micellar casein concentrate and milk protein concentrate. International Journal of Dairy Technology 76:727−36

doi: 10.1111/1471-0307.12977
[18]

Feeney RE, Whitaker JR. 1988. Importance of cross-linking reactions in proteins. In Advances in Cereal Science and Technology, ed. Pomeranz Y. Vol. IX. St Paul, USA: American Association of Cereal Chemists. pp 21−46.

[19]

Singh H. 1991. Modification of food proteins by covalent crosslinking. Trends in Food Science and Technology 2:196−200

doi: 10.1016/0924-2244(91)90683-A
[20]

Gerrard JA. 2002. Protein-protein crosslinking in food: methods, consequences, applications. Trends in Food Science and Technology 13:391−99

doi: 10.1016/S0924-2244(02)00257-1
[21]

Dickinson E. 1997. Enzymic crosslinking as a tool for food colloid rheology control and interfacial stabilization. Trends in Food Science & Technology 8:334−39

doi: 10.1016/S0924-2244(97)01067-4
[22]

Motoki M, Seguro K. 1998. Transglutaminase and its use for food processing. Trends in Food Science and Technology 9:204−10

doi: 10.1016/S0924-2244(98)00038-7
[23]

Kuraishi C, Yamazaki K, Susa Y. 2001. Transglutaminase: its utilization in the food industry. Food Reviews International 17:221−46

doi: 10.1081/FRI-100001258
[24]

Griffin M, Casadio R, Bergamini CM. 2002. Transglutaminases: Nature's Biological glues. The Biochemical Journal 368:377−96

doi: 10.1042/bj20021234
[25]

DeJong GAH, Koppelman SJ. 2002. Transglutaminase catalyzed reactions: Impact on food applications. Journal of Food Science 67:2798−806

doi: 10.1111/j.1365-2621.2002.tb08819.x
[26]

Jaros D, Partschefeld C, Henle T, Rohm H. 2006. Transglutaminase in dairy products: Chemistry, physics, applications. Journal of Texture Studies 37:113−55

doi: 10.1111/j.1745-4603.2006.00042.x
[27]

Buchert J, Ercili Cura D, Ma H, Gasparetti C, Monogioudi E, et al. 2010. Crosslinking food proteins for improved functionality. Annual Review of Food Science and Technology 1:113−138

doi: 10.1146/annurev.food.080708.100841
[28]

Velazquez-Dominguez A, Hiolle M, Abdallah M, Delaplace G, Peixoto PPS. 2023. Transglutaminase cross-linking on dairy proteins: Functionalities, patents, and commercial uses. International Dairy Journal 143:105688

doi: 10.1016/j.idairyj.2023.105688
[29]

Folk JE, Finlayson JS. 1977. The ɛ-(γ-glutamyl) lysine crosslink and the catalytic role of TGases. Advances in Protein Chemistry 31:1−133

doi: 10.1016/s0065-3233(08)60217-x
[30]

Association of Manufacturers and Formulators of Enzyme Products (AMFEP). 2004. AMFEP fact sheet on transglutaminase. AMFEP/04/19. Roodebeeklaan, Brussels: AMFEP. www.amfep.org. 3 pp.

[31]

Nonaka M, Tanaka H, Okiyama A, Motoki M, Ando H, et al. 1989. Polymerization of several proteins by Ca2+− independent transglutaminase derived from microorganisms. Agricultural and Biological Chemistry 53:2619−23

doi: 10.1080/00021369.1989.10869736
[32]

Traore F, Meunier JC. 1991. Cross-linking of caseins by human placental factor XIIIa. Journal of Agricultural and Food Chemistry 39:1892−96

doi: 10.1021/jf00010a042
[33]

Moon JH, Hong YH, Huppertz T, Fox PF, Kelly AL. 2009. Properties of casein micelles cross-linked by Transglutaminase. International Journal of Dairy Technology 62:27−32

doi: 10.1111/j.1471-0307.2008.00442.x
[34]

Sharma R, Lorenzen PC, Qvist KB. 2001. Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl) lysine and the susceptibility of individual proteins towards crosslinking. International Dairy Journal 11:785−93

doi: 10.1016/S0958-6946(01)00096-6
[35]

Tang C, Yang XQ, Chen Z, Wu H, Peng ZY. 2005. Physicochemical and structural characteristics of sodium caseinate biopolymers induced by microbial transglutaminase. Journal of Food Biochemistry 29:402−21

doi: 10.1111/j.1745-4514.2005.00038.x
[36]

Motoki M, Seguro K, Nio N, Takinami K. 1986. Glutamine specific deamidation of αs1-casein by transglutaminase. Agricultural and Biological Chemistry 50:3025−30

doi: 10.1271/bbb1961.50.3025
[37]

Stamnaes J, Fleckenstein B, Sollid LM. 2008. The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 1784:1804−11

doi: 10.1016/j.bbapap.2008.08.011
[38]

Mycek MJ, Waelsch H. 1960. The enzymatic deamidation of proteins. The Journal of Biological Chemistry 235:3513−17

doi: 10.1016/S0021-9258(18)64499-0
[39]

Lorenzen P. 2000. Techno-functional properties of transglutaminase-treated milk proteins. Milchwissenshaft 55:667−70

[40]

O'Sullivan MM, Kelly AL, Fox PF. 2002. Effect of transglutaminase on the heat stability of milk: A possible mechanism. Journal of Dairy Science 85:1−7

doi: 10.3168/jds.S0022-0302(02)74045-9
[41]

O'Sullivan MM, Lorenzen PC, O'Connell JE, Kelly AL, Schlimme E, et al. 2001. Short communication: Influence of transglutaminase on the heat stability of milk. Journal of Dairy Science 84:1331−34

doi: 10.3168/jds.S0022-0302(01)70162-2
[42]

Mounsey JS, O'Kennedy BT, Kelly PM. 2005. Influence of transglutaminase treatment on properties of micellar casein and products made therefrom. Le Lait 85:405−18

doi: 10.1051/lait:2005028
[43]

Huppertz T, de Kruif CG. 2007. Ethanol stability of casein micelles cross-linked with transglutaminase. International Dairy Journal 17:436−41

doi: 10.1016/j.idairyj.2006.05.005
[44]

Smiddy MA, Martin JEGH, Kelly AL, de Kruif CG, Huppertz T. 2006. Stability of casein micelles cross-linked by transglutaminase. Journal of Dairy Science 89:1906−14

doi: 10.3168/jds.S0022-0302(06)72258-5
[45]

Partschefeld C, Schwarzenbolz U, Richter S, Henle T. 2007. Crosslinking of casein by microbial transglutaminase and its resulting influence on the stability of micelle structure. Biotechnology Journal 2:456−61

doi: 10.1002/biot.200600232
[46]

Hiller B, Lorenzen PC. 2009. Effect of phosphatase/transglutaminase treatment on molar mass distribution and techno-functional properties of sodium caseinate. LWT - Food Science and Technology 42:87−92

doi: 10.1016/j.lwt.2008.06.003
[47]

Liu M, Damodaran S. 1999. Effect of Transglutaminase-Catalyzed Polymerization of β-Casein on Its Emulsifying Properties. Journal of Agricultural and Food Chemistry 47:1514−19

doi: 10.1021/jf981030c
[48]

Færgemand M, Otte J, Qvist KB. 1998. Emulsifying Properties of Milk Proteins Cross-linked with Microbial Transglutaminase. International Dairy Journal 8:715−23

doi: 10.1016/S0958-6946(98)00111-3
[49]

Færgemand M, Qvist KB. 1997. Transglutaminase: effect on rheological properties, microstructure and permeability of set style acid skim milk gel. Food Hydrocolloids 11:287−92

doi: 10.1016/S0268-005X(97)80058-6
[50]

Schorsch C, Carrie H, Clark AH, Norton IT. 2000. Cross-linking casein micelles by a microbial transglutaminase conditions for formation of transglutaminase-induced gels. International Dairy Journal 10:519−28

doi: 10.1016/S0958-6946(00)00052-2
[51]

Bönisch MP, Huss M, Weitl K, Kulozik U. 2007. Transglutaminase cross-linking of milk proteins and impact on yoghurt gel properties. International Dairy Journal 17:1360−71

doi: 10.1016/j.idairyj.2007.01.019
[52]

Jaros D, Heidig C, Rohm H. 2007. Enzymatic modification through microbial Transglutaminase enhances the viscosity of Stirred yogurt. Journal of Texture Studies 38:179−98

doi: 10.1111/j.1745-4603.2007.00093.x
[53]

Myllärinen P, Buchert J, Autio K. 2007. Effect of transglutaminase on rheological properties and microstructure of chemically acidified sodium caseinate gels. International Dairy Journal 17:800−7

doi: 10.1016/j.idairyj.2005.10.031
[54]

Yüksel Z, Erdem YK. 2010. The influence of transglutaminase treatment on functional properties of set yoghurt. International Journal of Dairy Technology 63:86−97

doi: 10.1111/j.1471-0307.2009.00539.x
[55]

Guyot C, Kulozik U. 2011. Effect of transglutaminase-treated milk powders on the properties of skim milk yoghurt. International Dairy Journal 21:628−35

doi: 10.1016/j.idairyj.2010.10.010
[56]

Pham TH, Pham KC, Huynh AT, Thi NUL, Trinh KS. 2021. Effect of transglutaminase on quality properties of fresh cheese. International Journal of Advanced and Applied Sciences 8:44−53

doi: 10.21833/ijaas.2021.04.006
[57]

Hebishy E, Nagarajah J, Thompson LS, Shennan S, Best L, et al. 2022. Impact of microbial transglutaminase and cooking time on functional properties of mozzarella cheese analogues. International Journal of Dairy Technology 75:201−21

doi: 10.1111/1471-0307.12831
[58]

Hooi R, Barbano DM, Bradley RL, Budde D, Bulthaus M, et al. 2004. Chemical and Physical Methods. In Standard Methods for the examination of dairy products, eds. Wehr HM, Frank JF. 17th Edition. Washington DC, USA: American Public Health Association. pp. 480−510. https://doi.org/10.2105/9780875530024ch15

[59]

Lee SK, Buwalda RJ, Euston SR, Foegeding EA, McKenna AB. 2003. Changes in the rheology and microstructure of process cheese during cooking. LWT - Food Science and Technology 36:339−45

doi: 10.1016/S0023-6438(03)00012-4
[60]

Guinee TP, Carić M, Kaláb M. 2004. Pasteurized processed cheese and substitute/imitation cheese products. In Cheese: chemistry, physics and microbiology, eds. Fox PF, McSweeney PLH, Cogan TM, Guinee TP. Volume 2: Major cheese groups. London, U.K.: Elsevier Applied Science. pp. 349–94. https://doi.org/10.1016/s1874-558x(04)80052-6

[61]

Brickley CA, Auty MAE, Piraino P, . McSweeney PLH. 2007. The effect of natural cheddar cheese ripening on the functional and textural properties of the processed cheese manufactured therefrom. Journal of Food Science 72:C483−C490

doi: 10.1111/j.1750-3841.2007.00539.x
[62]

Salunke P, Metzger LE. 2022. Functional characteristics of process cheese product as affected by milk protein concentrate and micellar casein concentrate at different usage levels. International Dairy Journal 128:105324

doi: 10.1016/j.idairyj.2022.105324
[63]

Lucey JA, Johnson ME, Horne DS. 2003. Invited review: Perspectives on the basis of the rheology and texture properties of cheese. Journal of Dairy Science 86:2725−43

doi: 10.3168/jds.S0022-0302(03)73869-7
[64]

Wong DWS, Camirand WM, Pavlath AE. 1996. Structures and functionalities of milk proteins. Critical Reviews in Food Science and Nutrition 36:807−44

doi: 10.1080/10408399609527751
[65]

Gupta VK, Reuter H. 1993. Firmness and melting quality of processed cheese foods with added whey protein concentrates. Le Lait 73:381−88

doi: 10.1051/lait:1993435
[66]

Savello PA, Ernstrom CA, Kalab M. 1989. Microstructure and meltability of model process cheese made with rennet and acid casein. Journal of Dairy Science 72:1−11

doi: 10.3168/jds.S0022-0302(89)79073-1
[67]

Park J, Rosenau JR. 1984. Melting characteristics of cheese. Korean Journal of Food Science and Technology 16:153−58