[1]

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
[2]

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
[3]

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
[4]

Marella C, Muthukumarappan K, Metzger LE. 2013. Application of membrane separation technology for developing novel dairy food ingredients. Journal of Food Processing & Technology 4:9

doi: 10.4172/2157-7110.1000269
[5]

Gavazzi-April C, Benoit S, Doyen A, Britten M, Pouliot Y. 2018. Preparation of milk protein concentrates by ultrafiltration and continuous diafiltration: Effect of process design on overall efficiency. Journal of Dairy Science 101:9670−79

doi: 10.3168/jds.2018-14430
[6]

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
[7]

Patel H, Patel S, Agarwal S. 2014. Milk protein concentrates: manufacturing and applications. Technical report. US Dairy Export Council, USA.

[8]

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

doi: 10.1016/j.cis.2012.01.002
[9]

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
[10]

Dickinson E, McClements DJ. 1996. Advances in food colloids. New York: Springer. https://link.springer.com/book/9780751402032

[11]

Hamouda MEA, Salunke P. 2024. Changes in milk protein functionality at low temperatures and rennet concentrations. Foods 13:447

doi: 10.3390/foods13030447
[12]

Gruppi A, Dermiki M, Spigno G, FitzGerald RJ. 2022. Impact of enzymatic hydrolysis and heat inactivation on the physicochemical properties of milk protein hydrolysates. Foods 11:516

doi: 10.3390/foods11040516
[13]

Cui Q, Sun Y, Zhou Z, Cheng J, Guo M. 2021. Effects of enzymatic hydrolysis on physicochemical properties and solubility and bitterness of milk protein hydrolysates. Foods 10:2462

doi: 10.3390/foods10102462
[14]

Ahmadifard N, Murueta JHC, Abedian-Kenari A, Motamedzadegan A, Jamali H. 2016. Comparison the effect of three commercial enzymes for enzymatic hydrolysis of two substrates (rice bran protein concentrate and soy-been protein) with SDS-PAGE. Journal of Food Science and Technology 53:1279−84

doi: 10.1007/s13197-015-2087-6
[15]

Tacias-Pascacio VG, Morellon-Sterling R, Siar EH, Tavano O, Berenguer-Murcia Á, et al. 2020. Use of Alcalase in the production of bioactive peptides: a review. International Journal of Biological Macromolecules 165:2143−96

doi: 10.1016/j.ijbiomac.2020.10.060
[16]

Severin S, Xia WS. 2006. Enzymatic hydrolysis of whey proteins by two different proteases and their effect on the functional properties of resulting protein hydrolysates. Journal of Food Biochemistry 30:77−97

doi: 10.1111/j.1745-4514.2005.00048.x
[17]

Chanarat S, Benjakul S. 2013. Impact of microbial transglutaminase on gelling properties of Indian mackerel fish protein isolates. Food Chemistry 136:929−37

doi: 10.1016/j.foodchem.2012.09.021
[18]

Folk JE, Chung SI. 1973. Molecular and catalytic properties of transglutaminases. Advances in Enzymology and Related Areas of Molecular Biology 38:109−91

doi: 10.1002/9780470122839.ch3
[19]

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
[20]

Hinz K, Huppertz T, Kulozik U, Kelly AL. 2007. Influence of enzymatic cross-linking on milk fat globules and emulsifying properties of milk proteins. International Dairy Journal 17:289−93

doi: 10.1016/j.idairyj.2006.05.001
[21]

O’Sullivan MM, Kelly AL, Fox PF. 2002. Influence of transglutaminase treatment on some physico-chemical properties of milk. Journal of Dairy Research 69:433−42

doi: 10.1017/S0022029902005617
[22]

Arora DS, Sharma RK. 2010. Ligninolytic fungal laccases and their biotechnological applications. Journal of Agricultural and Food Chemistry 160:1760−88

doi: 10.1007/s12010-009-8676-y
[23]

Steffensen CL, Andersen ML, Degn PE, Nielsen JH. 2008. Cross-linking proteins by laccase-catalyzed oxidation: importance relative to other modifications. Journal of Agricultural and Food Chemistry 56:12002−10

doi: 10.1021/jf801234v
[24]

Cura DE, Lantto R, Lille M, Andberg M, Kruus K, et al. 2009. Laccase-aided protein modification: effects on the structural properties of acidified sodium caseinate gels. International Dairy Journal 19:737−45

doi: 10.1016/j.idairyj.2009.06.007
[25]

Mattinen ML, Hellman M, Permi P, Autio K, Kalkkinen N, et al. 2006. Effect of protein structure on laccase-catalyzed protein oligomerization. Journal of Agricultural and Food Chemistry 54:8883−90

doi: 10.1021/jf062397h
[26]

Hiller B, Lorenzen PC. 2009. Functional properties of milk proteins as affected by enzymatic oligomerisation. Food Research International 42:899−908

doi: 10.1016/j.foodres.2009.04.022
[27]

Mokoonlall A, Hippich M, Struch M, Berger RG, Weiss J, et al. 2016. Antioxidant activity of milk suppresses laccase induced radicals and the subsequent modification of acidified milk protein gels. International Dairy Journal 60:24−31

doi: 10.1016/j.idairyj.2016.01.014
[28]

Ahmadi Z, Razavi SMA, Varidi M. 2017. Sequential ultrasound and transglutaminase treatments improve functional, rheological, and textural properties of whey protein concentrate. Innovative Food Science & Emerging Technologies 43:207−15

doi: 10.1016/j.ifset.2017.08.013
[29]

Hooi R, Barbano D, Bradley R, 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. Washington DC, USA: American Public Health Association. pp. 480−510. doi: 10.2105/9780875530024ch15

[30]

Olson D, White C, Richter R. 2004. Effect of pressure and fat content on particle sizes in microfluidized milk. Journal of Dairy Science 87:3217−23

doi: 10.3168/jds.S0022-0302(04)73457-8
[31]

Tarapatskyy M, Domagała J, Zaguła G, Saletnik B, Puchalski C. 2019. The effect of transglutaminase on colloidal stability of milk proteins. Journal of Food Measurement and Characterization 13:2339−46

doi: 10.1007/s11694-019-00153-0
[32]

Gani A, Broadway AA, Masoodi FA, Wani AA, Maqsood S, et al. 2015. Enzymatic hydrolysis of whey and casein protein-effect on functional rheological, textural and sensory properties of breads. Journal of Food Science and Technology 52:7697−709

doi: 10.1007/s13197-015-1840-1
[33]

Benvenutti L, Zielinski AAF, Ferreira SRS. 2022. Subcritical water extraction (SWE) modified by deep eutectic solvent (DES) for pectin recovery from a Brazilian berry by-product. The Journal of Supercritical Fluids 189:105729

doi: 10.1016/j.supflu.2022.105729
[34]

Sutariya SG, Salunke P. 2022. Effect of hyaluronic acid on milk properties: rheology protein stability, acid and rennet gelation properties. Food Hydrocolloids 131:107740

doi: 10.1016/j.foodhyd.2022.107740
[35]

Miralles B, Ramos M, Amigo L. 2003. Influence of proteolysis of milk on the whey protein to total protein ratio as determined by capillary electrophoresis. Journal of Dairy Science 86:2813−17

doi: 10.3168/jds.S0022-0302(03)73878-8
[36]

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
[37]

Hsieh JF, Pan PH. 2012. Proteomic profiling of microbial transglutaminase-induced polymerization of milk proteins. Journal of Dairy Science 95:580−89

doi: 10.3168/jds.2011-4773
[38]

Li K, Woo MW, Patel H, Metzger L, Selomulya C. 2018. Improvement of rheological and functional properties of milk protein concentrate by hydrodynamic cavitation. Journal of Food Engineering 221:106−13

doi: 10.1016/j.jfoodeng.2017.10.005
[39]

Zhao Z, Corredig M. 2016. Colloidal properties of casein micelles suspensions as a function of pH during concentration by osmotic stressing. Food Hydrocolloids 60:445−52

doi: 10.1016/j.foodhyd.2016.04.016
[40]

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
[41]

Dumpler J, Huppertz T, Kulozik U. 2020. Invited review: heat stability of milk and concentrated milk: past, present, and future research objectives. Journal of Dairy Science 103:10986−1007

doi: 10.3168/jds.2020-18605
[42]

Lorenzen PC. 2007. Effects of varying time/temperature-conditions of pre-heating and enzymatic cross-linking on techno-functional properties of reconstituted dairy ingredients. Food Research International 40:700−8

doi: 10.1016/j.foodres.2006.12.001
[43]

Zhang L, Xiao Q, Wang Y, Hu J, Xiong H, et al. 2022. Effects of sequential enzymatic hydrolysis and transglutaminase crosslinking on functional, rheological, and structural properties of whey protein isolate. LWT 153:112415

doi: 10.1016/j.lwt.2021.112415
[44]

Flanagan J, Gunning Y, FitzGerald RJ. 2003. Effect of cross-linking with transglutaminase on the heat stability and some functional characteristics of sodium caseinate. Food Research International 36:267−74

doi: 10.1016/S0963-9969(02)00168-0
[45]

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

[46]

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
[47]

Flanagan J, FitzGerald RJ. 2002. Functionality of Bacillus proteinase hydrolysates of sodium caseinate. International Dairy Journal 12:737−48

doi: 10.1016/S0958-6946(02)00067-5
[48]

Zeeb B, McClements DJ, Weiss J. 2017. Enzyme-based strategies for structuring foods for improved functionality. Annual Review of Food Science and Technology 8:21−34

doi: 10.1146/annurev-food-030216-025753
[49]

Wilde P, Clark D. 1996. Foam formation and stability. In Methods of testing protein functionality, ed. Hall GM. Vol. 1. Boston, MA, US: Springer. pp. 110−52. https://ouci.dntb.gov.ua/en/works/98gVj5al/

[50]

Huppertz T. 2010. Foaming properties of milk: a review of the influence of composition and processing. International Journal of Dairy Technology 63:477−88

doi: 10.1111/j.1471-0307.2010.00629.x
[51]

Augustin MA, Udabage P. 2007. Influence of processing on functionality of milk and dairy proteins. Advances in Food and Nutrition Research 53:1−38

doi: 10.1016/S1043-4526(07)53001-9
[52]

Panyam D, Kilara A. 1996. Enhancing the functionality of food proteins by enzymatic modification. Trends in Food Science & Technology 7:120−25

doi: 10.1016/0924-2244(96)10012-1
[53]

Chen SA. 2003. United States. Modification of foaming properties of proteins. Patents No. US-2002012720-A1

[54]

Konrad G, Kleinschmidt T, Rohenkohl H, Reimerdes EH. 2005. Peptic partial hydrolysis of whey protein concentrate for modifying the surface properties of whey protein. II. Effects on the emulsifying and foaming properties. Milchwissenschaft 60:195−98

[55]

Giardina C, Pelizzola V, Avalli A, Iametti S, Cattaneo T. 2004. Functional properties of milk protein hydrolysates obtained by controlled enzymatic hydrolysis. Milchwissenschaft 59:476−79

[56]

Kaur S, Vasiljevic T, Huppertz T. 2023. Influence of actinidin-induced hydrolysis on the functional properties of milk protein and whey protein concentrates. Foods 12:3806

doi: 10.3390/foods12203806
[57]

Li Q, Zhao Z. 2019. Acid and rennet-induced coagulation behavior of casein micelles with modified structure. Food Chemistry 291:231−38

doi: 10.1016/j.foodchem.2019.04.028
[58]

Dickinson E. 1999. Caseins in emulsions: interfacial properties and interactions. International Dairy Journal 9:305−12

doi: 10.1016/S0958-6946(99)00079-5
[59]

Gopirajah R, Singha P, Javad S, Rizvi SSH. 2020. Emulsifying properties of milk protein concentrate functionalized by supercritical fluid extrusion. Journal of Food Processing and Preservation 44:e14754

doi: 10.1111/jfpp.14754
[60]

de Castro RJS, Bagagli MP, Sato HH. 2015. Improving the functional properties of milk proteins: focus on the specificities of proteolytic enzymes. Current Opinion in Food Science 1:64−69

doi: 10.1016/j.cofs.2014.12.004
[61]

Liu XX, Yan YY, Liu HM, Wang XD, Qin GY. 2019. Emulsifying and structural properties of polysaccharides extracted from Chinese yam by an enzyme-assisted method. LWT 111:242−51

doi: 10.1016/j.lwt.2019.05.016
[62]

Abd El-Salam MH, El-Shibiny S. 2017. Preparation properties, and uses of enzymatic milk protein hydrolysates. Critical Reviews in Food Science and Nutrition 57:1119−32

doi: 10.1080/10408398.2014.899200
[63]

Singh AM, Dalgleish DG. 1998. The emulsifying properties of hydrolyzates of whey proteins. Journal of Dairy Science 81:918−24

doi: 10.3168/jds.S0022-0302(98)75651-6
[64]

Euston SR, Finnigan SR, Hirst RL. 2001. Heat-induced destabilization of oil-in-water emulsions formed from hydrolyzed whey protein. Journal of Agricultural and Food Chemistry 49:5576−83

doi: 10.1021/jf0102620
[65]

Ma H, Forssell P, Partanen R, Buchert J, Boer H. 2011. Improving laccase catalyzed cross-linking of whey protein isolate and their application as emulsifiers. Journal of Agricultural and Food Chemistry 59:1406−14

doi: 10.1021/jf103591p
[66]

Zheng H. 2019. Introduction: measuring rheological properties of foods. In Rheology of Semisolid Foods, ed. Joyner HS, Cham: Springer. pp. 3−30. doi: 10.1007/978-3-030-27134-3_1

[67]

Uluko H, Liu L, Lv JP, Zhang SW. 2016. Functional characteristics of milk protein concentrates and their modification. Critical Reviews in Food Science and Nutrition 56:1193−208

doi: 10.1080/10408398.2012.758625
[68]

Lomholt SB, Qvist KB. 1997. Relationship between rheological properties and degree of κ-casein proteolysis during renneting of milk. Journal of Dairy Research 64:541−49

doi: 10.1017/S002202999700246X
[69]

Ganesh S, Ningtyas DW, Prakash S. 2022. Investigating the functionality of enzymatically (transglutaminase and alcalase) treated almond protein isolate. Food Bioscience 49:101914

doi: 10.1016/j.fbio.2022.101914
[70]

Puppo MC, Afñón MC. 1999. Soybean protein dispersions at acid pH. Thermal and rheological properties. Journal of Food Science 64:50−56

doi: 10.1111/j.1365-2621.1999.tb09859.x
[71]

Al-Shamsi KA, Mudgil P, Hassan HM, Maqsood S. 2018. Camel milk protein hydrolysates with improved technofunctional properties and enhanced antioxidant potential in in vitro and in food model systems. Journal of Dairy Science 101:47−60

doi: 10.3168/jds.2017-13194
[72]

Kilara A, Panyam D. 2003. Peptides from milk proteins and their properties. Critical Reviews in Food Science and Nutrition 43:607−33

doi: 10.1080/10408690390251138
[73]

Dermiki M, FitzGerald RJ. 2020. Physicochemical and gelling properties of whey protein hydrolysates generated at 5 and 50 °C using Alcalase® and Neutrase®, effect of total solids and incubation time. International Dairy Journal 110:104792

doi: 10.1016/j.idairyj.2020.104792
[74]

Renzetti S, Dal Bello F, Arendt EK. 2008. Microstructure, fundamental rheology and baking characteristics of batters and breads from different gluten-free flours treated with a microbial transglutaminase. Journal of Cereal Science 48:33−45

doi: 10.1016/j.jcs.2007.07.011
[75]

Sato ACK, Perrechil FA, Costa AAS, Santana RC, Cunha RL. 2015. Cross-linking proteins by laccase: effects on the droplet size and rheology of emulsions stabilized by sodium caseinate. Food Research International 75:244−51

doi: 10.1016/j.foodres.2015.06.010
[76]

Foegeding A, Vardhanabhuti B, Yang X. 2011. Dairy systems. In Practical food rheology: an interpretive approach, eds. Norton IT, Spyropoulos F, Cox P. UK: Blackwell Publishing Ltd. pp. 133−72. doi:10.1002/9781444391060.ch7