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Volumn 101, Issue 6, 2018, Pages 4869-4878

Effect of temperature and pH on the properties of skim milk gels made from a tamarillo (Cyphomandra betacea) coagulant and rennet

Author keywords

gelation temperature and pH; microstructure; rennet; rheology; tamarillo crude extract

Indexed keywords

CHYMOSIN; PEPTIDE HYDROLASE; PLANT PROTEIN; RENNET;

EID: 85044313518     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2017-14050     Document Type: Article
Times cited : (9)

References (51)
  • 2
    • 33646068371 scopus 로고    scopus 로고
    • Purification and characterization of a serine protease from Cucumis trigonus Roxburghi
    • 16603211
    • Asif-Ullah, M., Kim, K.S., Yu, Y.G., Purification and characterization of a serine protease from Cucumis trigonus Roxburghi. Phytochemistry 67 (2006), 870–875 16603211.
    • (2006) Phytochemistry , vol.67 , pp. 870-875
    • Asif-Ullah, M.1    Kim, K.S.2    Yu, Y.G.3
  • 3
    • 84921056684 scopus 로고    scopus 로고
    • Biochemical, kinetic, and in silico characterization of DING protein purified from probiotic lactic acid bacteria Pediococcus acidilactici NCDC 252
    • 25367285
    • Attri, P., Khaket, T.P., Jodha, D., Singh, J., Dhanda, S., Biochemical, kinetic, and in silico characterization of DING protein purified from probiotic lactic acid bacteria Pediococcus acidilactici NCDC 252. Appl. Biochem. Biotechnol. 175 (2015), 1092–1110 25367285.
    • (2015) Appl. Biochem. Biotechnol. , vol.175 , pp. 1092-1110
    • Attri, P.1    Khaket, T.P.2    Jodha, D.3    Singh, J.4    Dhanda, S.5
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding
    • 942051
    • Bradford, M.M., A rapid and sensitive method for the quantitation of micrograms quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976), 248–254 942051.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 85047128209 scopus 로고    scopus 로고
    • Effects of different concentrations of fresh and dried Calotropis procera (Sodom apple) extract on cow milk coagulating time, cheese yield and organoleptic properties of West African soft cheese (WAGA SHIE)
    • Chikpah, S.K., Teye, G.A., Teye, M., Mawuli, F.F., Effects of different concentrations of fresh and dried Calotropis procera (Sodom apple) extract on cow milk coagulating time, cheese yield and organoleptic properties of West African soft cheese (WAGA SHIE). Eur. Sci. J. 10 (2014), 317–326.
    • (2014) Eur. Sci. J. , vol.10 , pp. 317-326
    • Chikpah, S.K.1    Teye, G.A.2    Teye, M.3    Mawuli, F.F.4
  • 6
    • 0032054231 scopus 로고    scopus 로고
    • Chymosin and aspartic proteinases
    • Chitpinityol, S., Crabbe, M.J.C., Chymosin and aspartic proteinases. Food Chem. 61 (1998), 395–418.
    • (1998) Food Chem. , vol.61 , pp. 395-418
    • Chitpinityol, S.1    Crabbe, M.J.C.2
  • 8
    • 0032839313 scopus 로고    scopus 로고
    • Casein micelle interactions
    • De Kruif, C.G., Casein micelle interactions. Int. Dairy J. 9 (1999), 183–188.
    • (1999) Int. Dairy J. , vol.9 , pp. 183-188
    • De Kruif, C.G.1
  • 9
    • 0001041028 scopus 로고    scopus 로고
    • Identification of peptides released from casein micelles by limited trypsinolysis
    • Diaz, O., Gouldsworthy, A.M., Leaver, J., Identification of peptides released from casein micelles by limited trypsinolysis. J. Agric. Food Chem. 44 (1996), 2517–2522.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 2517-2522
    • Diaz, O.1    Gouldsworthy, A.M.2    Leaver, J.3
  • 10
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • DuBois, M., Gilles, K., Hamilton, J., Rebers, P., Smith, F., Colorimetric method for determination of sugars and related substances. Anal. Chem. 28 (1956), 350–356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • DuBois, M.1    Gilles, K.2    Hamilton, J.3    Rebers, P.4    Smith, F.5
  • 11
    • 34047107397 scopus 로고    scopus 로고
    • Milk-clotting activity of enzyme extracts from sunflower and albizia seeds and specific hydrolysis of bovine κ-casein
    • Egito, A.S., Girardet, J.-M., Laguna, L.E., Poirson, C., Mollé, D., Miclo, L., Humbert, G., Gaillard, J.-L., Milk-clotting activity of enzyme extracts from sunflower and albizia seeds and specific hydrolysis of bovine κ-casein. Int. Dairy J. 17 (2007), 816–825.
    • (2007) Int. Dairy J. , vol.17 , pp. 816-825
    • Egito, A.S.1    Girardet, J.-M.2    Laguna, L.E.3    Poirson, C.4    Mollé, D.5    Miclo, L.6    Humbert, G.7    Gaillard, J.-L.8
  • 12
    • 0036098599 scopus 로고    scopus 로고
    • Rheological properties of milk gels made with coagulants of plant origin and chymosin
    • Esteves, C.L., Lucey, J.A., Pires, E.M., Rheological properties of milk gels made with coagulants of plant origin and chymosin. Int. Dairy J. 12 (2002), 427–434.
    • (2002) Int. Dairy J. , vol.12 , pp. 427-434
    • Esteves, C.L.1    Lucey, J.A.2    Pires, E.M.3
  • 13
    • 0142198452 scopus 로고    scopus 로고
    • Effect of gelation temperature on the properties of skim milk gels made from plant coagulants and chymosin
    • Esteves, C.L.C., Lucey, J.A., Hyslop, D.B., Pires, E.M.V., Effect of gelation temperature on the properties of skim milk gels made from plant coagulants and chymosin. Int. Dairy J. 13 (2003), 877–885.
    • (2003) Int. Dairy J. , vol.13 , pp. 877-885
    • Esteves, C.L.C.1    Lucey, J.A.2    Hyslop, D.B.3    Pires, E.M.V.4
  • 14
    • 2142691155 scopus 로고    scopus 로고
    • Effect of pH on the gelation properties of skim milk gels made from plant coagulants and chymosin
    • 12939079
    • Esteves, C.L.C., Lucey, J.A., Wang, T., Pires, E.M.V., Effect of pH on the gelation properties of skim milk gels made from plant coagulants and chymosin. J. Dairy Sci. 86 (2003), 2558–2567 12939079.
    • (2003) J. Dairy Sci. , vol.86 , pp. 2558-2567
    • Esteves, C.L.C.1    Lucey, J.A.2    Wang, T.3    Pires, E.M.V.4
  • 15
    • 21844492142 scopus 로고
    • Rennet: Current trends and future research
    • Garg, S.K., Johri, B.N., Rennet: Current trends and future research. Food Rev. Int. 10 (1994), 313–355.
    • (1994) Food Rev. Int. , vol.10 , pp. 313-355
    • Garg, S.K.1    Johri, B.N.2
  • 16
    • 0041502793 scopus 로고
    • Efficiency of chicken pepsin as a milk clotting enzyme
    • Gordin, S., Rosenthal, I., Efficiency of chicken pepsin as a milk clotting enzyme. J. Food Prot. 41 (1978), 684–688.
    • (1978) J. Food Prot. , vol.41 , pp. 684-688
    • Gordin, S.1    Rosenthal, I.2
  • 17
    • 85017119353 scopus 로고    scopus 로고
    • Optimization of milk-clotting enzyme production by Bacillus amyloliquefaciens SP1 isolated from apple rhizosphere
    • Guleria, S., Walia, A., Chauhan, A., Shirkot, C.K., Optimization of milk-clotting enzyme production by Bacillus amyloliquefaciens SP1 isolated from apple rhizosphere. Bioresour. Bioprocess., 3, 2016, 30.
    • (2016) Bioresour. Bioprocess. , vol.3 , pp. 30
    • Guleria, S.1    Walia, A.2    Chauhan, A.3    Shirkot, C.K.4
  • 18
    • 85000420335 scopus 로고    scopus 로고
    • High milk-clotting activity expressed by the newly isolated Paenibacillus spp. strain BD3526
    • 26771589
    • Hang, F., Liu, P., Wang, Q., Han, J., Wu, Z., Gao, C., Liu, Z., Zhang, H., Chen, W., High milk-clotting activity expressed by the newly isolated Paenibacillus spp. strain BD3526. Molecules, 21, 2016, 73 26771589.
    • (2016) Molecules , vol.21 , pp. 73
    • Hang, F.1    Liu, P.2    Wang, Q.3    Han, J.4    Wu, Z.5    Gao, C.6    Liu, Z.7    Zhang, H.8    Chen, W.9
  • 19
    • 1542715667 scopus 로고    scopus 로고
    • Determination of early stages of rennet-induced aggregation of casein micelles by diffusing wave spectroscopy and rheological measurements
    • Hemar, Y., Singh, H., Horne, D.S., Determination of early stages of rennet-induced aggregation of casein micelles by diffusing wave spectroscopy and rheological measurements. Curr. Appl. Phys. 4 (2004), 362–365.
    • (2004) Curr. Appl. Phys. , vol.4 , pp. 362-365
    • Hemar, Y.1    Singh, H.2    Horne, D.S.3
  • 20
    • 0001871181 scopus 로고    scopus 로고
    • The hairy casein micelle: Evolution of the concept and its implications for dairy technology
    • Holt, C., Horne, D.S., The hairy casein micelle: Evolution of the concept and its implications for dairy technology. Neth. Milk Dairy J. 50 (1996), 85–111.
    • (1996) Neth. Milk Dairy J. , vol.50 , pp. 85-111
    • Holt, C.1    Horne, D.S.2
  • 21
    • 79955090158 scopus 로고    scopus 로고
    • Purification, characterization, and milk coagulation properties of ginger proteases
    • 21524515
    • Huang, X.W., Chen, L.J., Luo, Y.B., Guo, H.Y., Ren, F.Z., Purification, characterization, and milk coagulation properties of ginger proteases. J. Dairy Sci. 94 (2011), 2259–2269 21524515.
    • (2011) J. Dairy Sci. , vol.94 , pp. 2259-2269
    • Huang, X.W.1    Chen, L.J.2    Luo, Y.B.3    Guo, H.Y.4    Ren, F.Z.5
  • 22
    • 0012289658 scopus 로고
    • Optimum pH for the limited specific proteolysis of kappa-casein by rennin (primary phase of milk clotting)
    • Humme, H.E., Optimum pH for the limited specific proteolysis of kappa-casein by rennin (primary phase of milk clotting). Ned. Melk Zui. 26 (1972), 180–185.
    • (1972) Ned. Melk Zui. , vol.26 , pp. 180-185
    • Humme, H.E.1
  • 23
    • 78751632114 scopus 로고    scopus 로고
    • Recent advances in milk clotting enzymes
    • Jacob, M., Jaros, D., Rohm, H., Recent advances in milk clotting enzymes. Int. J. Dairy Technol. 64 (2011), 14–33.
    • (2011) Int. J. Dairy Technol. , vol.64 , pp. 14-33
    • Jacob, M.1    Jaros, D.2    Rohm, H.3
  • 24
    • 84886062421 scopus 로고    scopus 로고
    • The formation of cheese curd
    • B.A. Law A.Y. Tamime 2nd ed. Blackwell Ames, IA
    • Janhøj, T., Qvist, K.B., The formation of cheese curd. Law, B.A., Tamime, A.Y., (eds.) Technology of Cheesemaking, 2nd ed., 2010, Blackwell, Ames, IA, 130–165.
    • (2010) Technology of Cheesemaking , pp. 130-165
    • Janhøj, T.1    Qvist, K.B.2
  • 25
    • 0029797121 scopus 로고    scopus 로고
    • SDS-PAGE of protein in goat milk cheeses ripened under different conditions
    • Jin, Y.K., Park, Y.W., SDS-PAGE of protein in goat milk cheeses ripened under different conditions. J. Food Sci. 61 (1996), 490–495.
    • (1996) J. Food Sci. , vol.61 , pp. 490-495
    • Jin, Y.K.1    Park, Y.W.2
  • 26
    • 73049092943 scopus 로고    scopus 로고
    • Production of novel dairy products using actindin and high pressure as enzyme activity regulator
    • Katsaros, G.I., Tavantzis, G., Taoukis, P.S., Production of novel dairy products using actindin and high pressure as enzyme activity regulator. Innov. Food Sci. Emerg. 11 (2010), 47–51.
    • (2010) Innov. Food Sci. Emerg. , vol.11 , pp. 47-51
    • Katsaros, G.I.1    Tavantzis, G.2    Taoukis, P.S.3
  • 27
    • 84871972794 scopus 로고    scopus 로고
    • Textbook of Pharmaceutical Biotechnology
    • Elsevier Haryana, India
    • Kokate, C., Hurakadle, P.J., Jalalpure, S.S., Textbook of Pharmaceutical Biotechnology. 2011, Elsevier, Haryana, India.
    • (2011)
    • Kokate, C.1    Hurakadle, P.J.2    Jalalpure, S.S.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063
    • Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970), 680–685 5432063.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0000592021 scopus 로고
    • The relationship between cheese flavour and texture
    • Lawrence, R.C., Gilles, J., Creamer, L.K., The relationship between cheese flavour and texture. N. Z. J. Dairy Sci. 70 (1983), 1748–1760.
    • (1983) N. Z. J. Dairy Sci. , vol.70 , pp. 1748-1760
    • Lawrence, R.C.1    Gilles, J.2    Creamer, L.K.3
  • 31
    • 84901024868 scopus 로고    scopus 로고
    • Rheological and structural properties of differently acidified and renneted milk gels
    • 24731639
    • Liu, X.T., Zhang, H., Wang, F., Luo, J., Guo, H.Y., Ren, F.Z., Rheological and structural properties of differently acidified and renneted milk gels. J. Dairy Sci. 97 (2014), 3292–3299 24731639.
    • (2014) J. Dairy Sci. , vol.97 , pp. 3292-3299
    • Liu, X.T.1    Zhang, H.2    Wang, F.3    Luo, J.4    Guo, H.Y.5    Ren, F.Z.6
  • 32
    • 0037051526 scopus 로고    scopus 로고
    • Characterization of “lettucine,” a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting
    • 11929310
    • Lo Piero, A.R., Puglisi, I., Petrone, G., Characterization of “lettucine,” a serine-like protease from Lactuca sativa leaves, as a novel enzyme for milk clotting. J. Agric. Food Chem. 50 (2002), 2439–2443 11929310.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 2439-2443
    • Lo Piero, A.R.1    Puglisi, I.2    Petrone, G.3
  • 34
    • 2442667390 scopus 로고    scopus 로고
    • Acid coagulation of milk
    • P.F. Fox P.L.H. McSweeney Springer New York, NY
    • Lucey, J.A., Singh, H., Acid coagulation of milk. Fox, P.F., McSweeney, P.L.H., (eds.) Advanced Dairy Chemistry, Vol. 1, 2003, Springer, New York, NY, 1001–1025.
    • (2003) Advanced Dairy Chemistry , vol.1 , pp. 1001-1025
    • Lucey, J.A.1    Singh, H.2
  • 35
    • 0031752754 scopus 로고    scopus 로고
    • Effect of interactions between denatured whey proteins and casein micelles on the formation and rheological properties of acid skim milk gel
    • Lucey, J.A., Tamehana, M., Singh, H., Munro, P.A., Effect of interactions between denatured whey proteins and casein micelles on the formation and rheological properties of acid skim milk gel. J. Dairy Res. 65 (1998), 555–567.
    • (1998) J. Dairy Res. , vol.65 , pp. 555-567
    • Lucey, J.A.1    Tamehana, M.2    Singh, H.3    Munro, P.A.4
  • 37
    • 0014807078 scopus 로고
    • Anionic proteinase from Actinidia chinensis. Preparation and properties of the crystalline enzyme
    • 5506167
    • McDowall, M.A., Anionic proteinase from Actinidia chinensis. Preparation and properties of the crystalline enzyme. Eur. J. Biochem. 14 (1970), 214–221 5506167.
    • (1970) Eur. J. Biochem. , vol.14 , pp. 214-221
    • McDowall, M.A.1
  • 38
    • 0037177375 scopus 로고    scopus 로고
    • Effects of structural rearrangements on the rheology of rennet-induced casein particle gels
    • 12061711
    • Mellema, M., Walstra, P., Van Opheusden, J.H.J., Van Vliet, T., Effects of structural rearrangements on the rheology of rennet-induced casein particle gels. Adv. Colloid Interface Sci. 98 (2002), 25–50 12061711.
    • (2002) Adv. Colloid Interface Sci. , vol.98 , pp. 25-50
    • Mellema, M.1    Walstra, P.2    Van Opheusden, J.H.J.3    Van Vliet, T.4
  • 39
    • 62549122479 scopus 로고    scopus 로고
    • Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen
    • 19268997
    • Mohamed Ahmed, I.A., Morishima, I., Babiker, E.E., Mori, N., Dubiumin, a chymotrypsin-like serine protease from the seeds of Solanum dubium Fresen. Phytochemistry 70 (2009), 483–491 19268997.
    • (2009) Phytochemistry , vol.70 , pp. 483-491
    • Mohamed Ahmed, I.A.1    Morishima, I.2    Babiker, E.E.3    Mori, N.4
  • 40
    • 84859977458 scopus 로고    scopus 로고
    • Influence of Withania coagulans protease as a vegetable rennet on proteolysis of Iranian UF white cheese
    • Pezeshki, A., Hesari, J., Zonoz, A.A., Ghambarzadeh, B., Influence of Withania coagulans protease as a vegetable rennet on proteolysis of Iranian UF white cheese. J. Agric. Sci. Technol. 13 (2011), 567–576.
    • (2011) J. Agric. Sci. Technol. , vol.13 , pp. 567-576
    • Pezeshki, A.1    Hesari, J.2    Zonoz, A.A.3    Ghambarzadeh, B.4
  • 42
    • 0033852286 scopus 로고    scopus 로고
    • Effect of temperature of milk acidification on rennet gel properties
    • Renault, C., Gastaldi, E., Cuq, J.L., La Fuente, D., Tarodo, B., Effect of temperature of milk acidification on rennet gel properties. J. Food Sci. 65 (2000), 630–634.
    • (2000) J. Food Sci. , vol.65 , pp. 630-634
    • Renault, C.1    Gastaldi, E.2    Cuq, J.L.3    La Fuente, D.4    Tarodo, B.5
  • 43
    • 0032725188 scopus 로고    scopus 로고
    • Residual clotting activity and ripening properties of vegetable rennet from Cynara cardunculus in La Serena cheese
    • Roa, I., López, M.B., Mendiola, F.J., Residual clotting activity and ripening properties of vegetable rennet from Cynara cardunculus in La Serena cheese. Food Res. Int. 32 (1999), 413–419.
    • (1999) Food Res. Int. , vol.32 , pp. 413-419
    • Roa, I.1    López, M.B.2    Mendiola, F.J.3
  • 44
    • 0038274072 scopus 로고    scopus 로고
    • Cheese making with vegetable coagulants; the use of Cynara L. for the production of ovine milk cheeses
    • Roseiro, L.B., Barbosa, M.M., Ames, J., Wilbey, R., Cheese making with vegetable coagulants; the use of Cynara L. for the production of ovine milk cheeses. Int. J. Dairy Technol. 56 (2003), 76–85.
    • (2003) Int. J. Dairy Technol. , vol.56 , pp. 76-85
    • Roseiro, L.B.1    Barbosa, M.M.2    Ames, J.3    Wilbey, R.4
  • 45
    • 80051795627 scopus 로고    scopus 로고
    • Protease: Introduction
    • A.B. Salleh R.N.Z.R.A. Rahman M. Basri Nova Science New York, NY
    • Salleh, A.B., Razak, C.N.A., Rahman, R.N.Z.R.A., Basri, M., Protease: Introduction. Salleh, A.B., Rahman, R.N.Z.R.A., Basri, M., (eds.) New Lipases and Proteases, 2006, Nova Science, New York, NY, 23–39.
    • (2006) New Lipases and Proteases , pp. 23-39
    • Salleh, A.B.1    Razak, C.N.A.2    Rahman, R.N.Z.R.A.3    Basri, M.4
  • 46
    • 70349910022 scopus 로고    scopus 로고
    • Extraction and measurement of total lipids
    • R.E. Wrolstad T.E. Acree H. An E.A. Decker R.H. Penner D.S. Reid S.J. Schwartz C.R. Shoemaker P. Sporns Wiley New York, NY
    • Shahidi, F., Extraction and measurement of total lipids. Wrolstad, R.E., Acree, T.E., An, H., Decker, E.A., Penner, R.H., Reid, D.S., Schwartz, S.J., Shoemaker, C.R., Sporns, P., (eds.) Current Protocols in Food Analytical Chemistry, Vol. 1, 2001, Wiley, New York, NY, D1.1–D1.11.
    • (2001) Current Protocols in Food Analytical Chemistry , vol.1 , pp. D1.1-D1.11
    • Shahidi, F.1
  • 47
    • 26444515972 scopus 로고    scopus 로고
    • Partial identification of water-soluble peptides released at early stages of proteolysis in sterilized ovine cheese-like systems: Influence of type of coagulant and starter
    • 15905424
    • Silva, S.V., Malcata, F.X., Partial identification of water-soluble peptides released at early stages of proteolysis in sterilized ovine cheese-like systems: Influence of type of coagulant and starter. J. Dairy Sci. 88 (2005), 1947–1954 15905424.
    • (2005) J. Dairy Sci. , vol.88 , pp. 1947-1954
    • Silva, S.V.1    Malcata, F.X.2
  • 48
    • 85019259695 scopus 로고    scopus 로고
    • Industrial applications and production sources of serine alkaline proteases: A review
    • Sundus, H., Mukhtar, H., Nawaz, A., Industrial applications and production sources of serine alkaline proteases: A review. J. Bacteriol. Mycol., 3, 2016, 00051.
    • (2016) J. Bacteriol. Mycol. , vol.3 , pp. 00051
    • Sundus, H.1    Mukhtar, H.2    Nawaz, A.3
  • 49
    • 0001558145 scopus 로고
    • pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 1. Effect of acidification on physico-chemical properties
    • Van Hooydonk, A.C.M., pH-induced physico-chemical changes of casein micelles in milk and their effect on renneting. 1. Effect of acidification on physico-chemical properties. Neth. Milk Dairy J. 40 (1986), 281–296.
    • (1986) Neth. Milk Dairy J. , vol.40 , pp. 281-296
    • Van Hooydonk, A.C.M.1
  • 50
    • 76849095321 scopus 로고    scopus 로고
    • Production and characterization of a milk-clotting enzyme from Aspergillus oryzae MTCC 5341
    • 19727708
    • Vishwanatha, K.S., Appu Rao, A.G., Singh, S.A., Production and characterization of a milk-clotting enzyme from Aspergillus oryzae MTCC 5341. Appl. Microbiol. Biotechnol. 85 (2010), 1849–1859 19727708.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1849-1859
    • Vishwanatha, K.S.1    Appu Rao, A.G.2    Singh, S.A.3
  • 51
    • 79953153292 scopus 로고
    • Properties of the milk clotting activity of ficin
    • Whitaker, J.R., Properties of the milk clotting activity of ficin. J. Food Technol. 13 (1959), 86–91.
    • (1959) J. Food Technol. , vol.13 , pp. 86-91
    • Whitaker, J.R.1


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