메뉴 건너뛰기




Volumn 33, Issue 10, 2015, Pages 1243-1254

Denaturation and Physical Characteristics of Spray-Dried Whey Protein Isolate Powders Produced in the Presence and Absence of Lactose, Trehalose, and Polysorbate-80

Author keywords

Denaturation; Secondary structure; Sugar; Surface morphology; Surfactant; Whey protein isolate

Indexed keywords

AGGLOMERATION; DENATURATION; DRYING; EMULSIONS; PARTICLE SIZE; PROTEINS; SOLUBILITY; SUGARS; SURFACE ACTIVE AGENTS; SURFACE MORPHOLOGY;

EID: 84931748554     PISSN: 07373937     EISSN: 15322300     Source Type: Journal    
DOI: 10.1080/07373937.2015.1023311     Document Type: Article
Times cited : (36)

References (57)
  • 1
    • 34250652436 scopus 로고    scopus 로고
    • Effects of process variables on the denaturation of whey proteins during spray drying
    • C.Anandharamakrishnan, ; C.D.Rielly, ; A.G.F.Stapley, Effects of process variables on the denaturation of whey proteins during spray drying. Drying Technology 2007, 25(5), 799–807.
    • (2007) Drying Technology , vol.25 , Issue.5 , pp. 799-807
    • Anandharamakrishnan, C.1    Rielly, C.D.2    Stapley, A.G.F.3
  • 4
    • 84879050616 scopus 로고    scopus 로고
    • Effect of whey protein agglomeration on spray dried microcapsules containing Saccharomyces boulardii
    • D.Duongthingoc, ; P.George, ; L.Katopo, ; E.Gorczyca, ; S.Kasapis, Effect of whey protein agglomeration on spray dried microcapsules containing Saccharomyces boulardii. Food Chemistry 2013, 141, 1782–1788.
    • (2013) Food Chemistry , vol.141 , pp. 1782-1788
    • Duongthingoc, D.1    George, P.2    Katopo, L.3    Gorczyca, E.4    Kasapis, S.5
  • 6
    • 12344290549 scopus 로고    scopus 로고
    • Kinetics of combined thermal and pressure-induced whey protein denaturation in bovine skim milk
    • J.Hinrichs, ; B.Rademacher, Kinetics of combined thermal and pressure-induced whey protein denaturation in bovine skim milk. International Dairy Journal 2005, 15, 315–323.
    • (2005) International Dairy Journal , vol.15 , pp. 315-323
    • Hinrichs, J.1    Rademacher, B.2
  • 7
    • 0032047305 scopus 로고    scopus 로고
    • Kinetics of denaturation and aggregation of whey protein in skim milk heated in an ultra-high temperature (UHT) pilot plant
    • D.J.Oldfield, ; S.Harjinder, ; W.T.Michael, ; N.P.Kevin, Kinetics of denaturation and aggregation of whey protein in skim milk heated in an ultra-high temperature (UHT) pilot plant. International Dairy Journal 1998, 8, 311–318.
    • (1998) International Dairy Journal , vol.8 , pp. 311-318
    • Oldfield, D.J.1    Harjinder, S.2    Michael, W.T.3    Kevin, N.P.4
  • 8
    • 16244382873 scopus 로고    scopus 로고
    • Effect of preheating and other process parameters on whey proteins reactions during skim milk powder manufacture
    • D.J.Oldfield, ; M.W.Taylor, ; H.Singh, Effect of preheating and other process parameters on whey proteins reactions during skim milk powder manufacture. International Dairy Journal 2005, 15, 501–511.
    • (2005) International Dairy Journal , vol.15 , pp. 501-511
    • Oldfield, D.J.1    Taylor, M.W.2    Singh, H.3
  • 9
    • 0033843271 scopus 로고    scopus 로고
    • Surface composition of spray-dried particles of bovine serum albumin/trehalose/surfactant
    • M.Adler, ; M.Unger, ; G.Lee, Surface composition of spray-dried particles of bovine serum albumin/trehalose/surfactant. Pharmaceutical Research 2000, 17, 863–870.
    • (2000) Pharmaceutical Research , vol.17 , pp. 863-870
    • Adler, M.1    Unger, M.2    Lee, G.3
  • 10
    • 0031914743 scopus 로고    scopus 로고
    • Spray-drying of air–liquid interface sensitive recombinant human growth hormone
    • Y.-F.Maa, ; P.T.Nguyen, ; S.W.Hsu, Spray-drying of air–liquid interface sensitive recombinant human growth hormone. Journal of Pharmaceutical Sciences 1998, 87(2), 152–159.
    • (1998) Journal of Pharmaceutical Sciences , vol.87 , Issue.2 , pp. 152-159
    • Maa, Y.-F.1    Nguyen, P.T.2    Hsu, S.W.3
  • 11
    • 0032962882 scopus 로고    scopus 로고
    • The effect of formulation excipients on protein stability and aerosol performance of spray-dried powders of a recombinant humanized anti-IgE monoclonal antibody
    • J.D.Andya, ; Y.Maa, ; H.R.Costantino, ; P.Nguyen, ; N.Dasovich, ; T.D.Sweeney, ; C.C.Hsu, ; S.J.Shire, The effect of formulation excipients on protein stability and aerosol performance of spray-dried powders of a recombinant humanized anti-IgE monoclonal antibody. Pharmaceutical Research 1999, 16, 350–358.
    • (1999) Pharmaceutical Research , vol.16 , pp. 350-358
    • Andya, J.D.1    Maa, Y.2    Costantino, H.R.3    Nguyen, P.4    Dasovich, N.5    Sweeney, T.D.6    Hsu, C.C.7    Shire, S.J.8
  • 12
    • 80054758768 scopus 로고    scopus 로고
    • Interactions of formulation excipients with proteins in solution and in the dried state
    • S.Ohtake, ; Y.Kita, ; T.Arakawa, Interactions of formulation excipients with proteins in solution and in the dried state. Advanced Drug Delivery Reviews 2011, 63, 1053–1073.
    • (2011) Advanced Drug Delivery Reviews , vol.63 , pp. 1053-1073
    • Ohtake, S.1    Kita, Y.2    Arakawa, T.3
  • 13
    • 0033047323 scopus 로고    scopus 로고
    • Stability and surface activity of lactate dehydrogenase in spray dried trehalose
    • M.Adler, ; G.Lee, Stability and surface activity of lactate dehydrogenase in spray dried trehalose. Journal of Pharmaceutical Sciences 1999, 88, 199–208.
    • (1999) Journal of Pharmaceutical Sciences , vol.88 , pp. 199-208
    • Adler, M.1    Lee, G.2
  • 14
    • 50749134719 scopus 로고
    • Trehalose, a new approach to premium dried foods
    • B.Roser, Trehalose, a new approach to premium dried foods. Trends in Food Science & Technology 1991, 2, 166–169.
    • (1991) Trends in Food Science & Technology , vol.2 , pp. 166-169
    • Roser, B.1
  • 16
    • 0024997351 scopus 로고
    • Trehalose in yeast, stress protectant rather than reserve carbohydrate
    • A.Wiemken, Trehalose in yeast, stress protectant rather than reserve carbohydrate. Antonie van Leeuwenhoek 1990, 58, 209–217.
    • (1990) Antonie van Leeuwenhoek , vol.58 , pp. 209-217
    • Wiemken, A.1
  • 17
    • 0033046866 scopus 로고    scopus 로고
    • Activity–stability considerations of trypsinogen during spray drying: Effect of sucrose
    • S.T.Tzannis, ; S.J.Prestrelski, Activity–stability considerations of trypsinogen during spray drying: Effect of sucrose. Journal of Pharmaceutical Sciences 1999, 88(3), 351–359.
    • (1999) Journal of Pharmaceutical Sciences , vol.88 , Issue.3 , pp. 351-359
    • Tzannis, S.T.1    Prestrelski, S.J.2
  • 18
    • 0033822417 scopus 로고    scopus 로고
    • Protection of bovine serum albumin from aggregation by Tween-80
    • T.Arakawa, ; Y.Kita, Protection of bovine serum albumin from aggregation by Tween-80. Journal of Pharmaceutical Sciences 2000, 89(5), 646–651.
    • (2000) Journal of Pharmaceutical Sciences , vol.89 , Issue.5 , pp. 646-651
    • Arakawa, T.1    Kita, Y.2
  • 19
    • 84974486877 scopus 로고
    • Denaturation, aggregation and heat stability of milk protein during the manufacture of skim powder
    • H.Singh, ; L.K.Creamer, Denaturation, aggregation and heat stability of milk protein during the manufacture of skim powder. Journal of Dairy Research 1991, 58, 269–283.
    • (1991) Journal of Dairy Research , vol.58 , pp. 269-283
    • Singh, H.1    Creamer, L.K.2
  • 20
    • 84858990585 scopus 로고    scopus 로고
    • Functional properties of whey proteins microparticulated at low pH
    • M.Dissanayake, ; S.Liyanaarachchi, ; T.Vasiljevic, Functional properties of whey proteins microparticulated at low pH. Journal of Dairy Science 2012, 95(4), 1667–1679.
    • (2012) Journal of Dairy Science , vol.95 , Issue.4 , pp. 1667-1679
    • Dissanayake, M.1    Liyanaarachchi, S.2    Vasiljevic, T.3
  • 21
    • 0034306719 scopus 로고    scopus 로고
    • The morphology of spray dried particles a qualitative view
    • D.E.Walton, The morphology of spray dried particles a qualitative view. Drying Technolology 2000, 18, 1943–1986.
    • (2000) Drying Technolology , vol.18 , pp. 1943-1986
    • Walton, D.E.1
  • 23
    • 2142837130 scopus 로고    scopus 로고
    • Heat treatment of whey proteins in the presence of anionic surfactants
    • H.J.Giroux, ; M.Britten, Heat treatment of whey proteins in the presence of anionic surfactants. Food Hydrocolloids 2004, 18(4), 685–695.
    • (2004) Food Hydrocolloids , vol.18 , Issue.4 , pp. 685-695
    • Giroux, H.J.1    Britten, M.2
  • 24
    • 0034072201 scopus 로고    scopus 로고
    • Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins
    • A.Kulmyrzaev, ; C.Bryant, ; D.J.McClements, Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins. Journal of Agricultural and Food Chemistry 2000, 48(5), 1593–1597.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.5 , pp. 1593-1597
    • Kulmyrzaev, A.1    Bryant, C.2    McClements, D.J.3
  • 25
    • 84920746992 scopus 로고    scopus 로고
    • Drying and denaturation characteristics of whey protein isolate in the presence of lactose and trehalose
    • M.A.Haque, ; P.Aldred, ; J.Chen, ; B.Adhikari, Drying and denaturation characteristics of whey protein isolate in the presence of lactose and trehalose. Food Chemistry 2015, 177, 8–16.
    • (2015) Food Chemistry , vol.177 , pp. 8-16
    • Haque, M.A.1    Aldred, P.2    Chen, J.3    Adhikari, B.4
  • 26
    • 84878164984 scopus 로고    scopus 로고
    • Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes
    • M.A.Haque, ; P.Aldred, ; J.Chen, ; C.J.Barrow, ; B.Adhikari, Comparative study of denaturation of whey protein isolate (WPI) in convective air drying and isothermal heat treatment processes. Food Chemistry 2013, 141, 702–711.
    • (2013) Food Chemistry , vol.141 , pp. 702-711
    • Haque, M.A.1    Aldred, P.2    Chen, J.3    Barrow, C.J.4    Adhikari, B.5
  • 27
    • 0002348148 scopus 로고
    • A rapid method for the determination of whey protein denaturation
    • N.Parris, ; M.A.Baginski, A rapid method for the determination of whey protein denaturation. Journal of Dairy Science 1991, 74, 58–64.
    • (1991) Journal of Dairy Science , vol.74 , pp. 58-64
    • Parris, N.1    Baginski, M.A.2
  • 28
    • 41849095663 scopus 로고    scopus 로고
    • Whey protein interactions in acidic cold-set gels at different pH values
    • A.L.F.Cavallieria, ; A.P.Costa-Nettob, ; M.Menossib, ; R.L.D.Cunha, Whey protein interactions in acidic cold-set gels at different pH values. Lait 2007, 87, 535–554.
    • (2007) Lait , vol.87 , pp. 535-554
    • Cavallieria, A.L.F.1    Costa-Nettob, A.P.2    Menossib, M.3    Cunha, R.L.D.4
  • 29
    • 1842530304 scopus 로고    scopus 로고
    • Manufacture and use of dairy protein fractions
    • M.R.Etzel, Manufacture and use of dairy protein fractions. The Journal of Nutrition 2004, 134, 996S–1002S.
    • (2004) The Journal of Nutrition , vol.134 , pp. 996S-1002S
    • Etzel, M.R.1
  • 30
    • 65249156463 scopus 로고    scopus 로고
    • Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing
    • M.Dissanayake, ; T.Vasiljevic, Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. Journal of Dairy Science 2009, 92(4), 1387–1397.
    • (2009) Journal of Dairy Science , vol.92 , Issue.4 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 31
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study
    • J.I.Boye, ; I.Alli, Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study. Food Research International 2000, 33, 673–682.
    • (2000) Food Research International , vol.33 , pp. 673-682
    • Boye, J.I.1    Alli, I.2
  • 32
    • 0141619318 scopus 로고    scopus 로고
    • Enthalpy of fusion of indium: A certified reference material for differential scanning calorimetry
    • D.G.Archer, Enthalpy of fusion of indium: A certified reference material for differential scanning calorimetry. Journal of Chemical & Engineering Data 2003, 48, 1157–1163.
    • (2003) Journal of Chemical & Engineering Data , vol.48 , pp. 1157-1163
    • Archer, D.G.1
  • 33
    • 0035887070 scopus 로고    scopus 로고
    • Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors
    • M.van de Weert, ; P.I.Haris, ; W.E.Hennink, ; D.J.A.Crommelin, Fourier transform infrared spectrometric analysis of protein conformation: Effect of sampling method and stress factors. Analytical Biochemistry 2001, 297, 160–169.
    • (2001) Analytical Biochemistry , vol.297 , pp. 160-169
    • van de Weert, M.1    Haris, P.I.2    Hennink, W.E.3    Crommelin, D.J.A.4
  • 34
    • 84901290425 scopus 로고    scopus 로고
    • Drying and denaturation characteristics of α-lactalbumin, β-lactoglobulin and bovine serum albumin in a convective drying process
    • M.A.Haque, ; P.Aldred, ; J.Chen, ; C.Barrow, ; B.Adhikari, Drying and denaturation characteristics of α-lactalbumin, β-lactoglobulin and bovine serum albumin in a convective drying process. Journal of Agricultural and Food Chemistry 2014, 62(20), 4695–4706.
    • (2014) Journal of Agricultural and Food Chemistry , vol.62 , Issue.20 , pp. 4695-4706
    • Haque, M.A.1    Aldred, P.2    Chen, J.3    Barrow, C.4    Adhikari, B.5
  • 35
    • 84866720712 scopus 로고    scopus 로고
    • Comparative study of deteriorative changes in the ageing of milk powder
    • N.Yazdanpanah, ; T.A.G.Langrish, Comparative study of deteriorative changes in the ageing of milk powder. Journal of Food Engineering 2013, 114, 14–21.
    • (2013) Journal of Food Engineering , vol.114 , pp. 14-21
    • Yazdanpanah, N.1    Langrish, T.A.G.2
  • 37
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • J.Kong, ; S.Yu, Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica 2007, 39, 549–559.
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 38
    • 6344277284 scopus 로고    scopus 로고
    • Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution
    • S.Ngarize, ; H.Herman, ; A.Adams, ; N.Howell, Comparison of changes in the secondary structure of unheated, heated, and high-pressure-treated β-lactoglobulin and ovalbumin proteins using Fourier transform Raman spectroscopy and self-deconvolution. Journal of Agricultural and Food Chemistry 2004, 52, 6470–6477.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 6470-6477
    • Ngarize, S.1    Herman, H.2    Adams, A.3    Howell, N.4
  • 39
    • 0024053634 scopus 로고
    • Fourier deconvolution of the amide I Raman band of proteins as related to conformation
    • H.Susi, ; D.M.Byler, Fourier deconvolution of the amide I Raman band of proteins as related to conformation. Applied Spectroscopy 1988, 42, 819–826.
    • (1988) Applied Spectroscopy , vol.42 , pp. 819-826
    • Susi, H.1    Byler, D.M.2
  • 40
    • 34249039632 scopus 로고    scopus 로고
    • Use of whey proteins for encapsulation and controlled delivery applications
    • S.Gunasekaran, ; S.Ko, ; L.Xiao, Use of whey proteins for encapsulation and controlled delivery applications. Journal of Food Engineering 2007, 83, 31–40.
    • (2007) Journal of Food Engineering , vol.83 , pp. 31-40
    • Gunasekaran, S.1    Ko, S.2    Xiao, L.3
  • 41
    • 79958054854 scopus 로고    scopus 로고
    • Surface protein coverage and its implications on spray-drying of model sugar-rich foods: Solubility, powder production and characterisation
    • M.Jayasundera, ; B.Adhikari, ; T.Howes, ; P.Aldred, Surface protein coverage and its implications on spray-drying of model sugar-rich foods: Solubility, powder production and characterisation. Food Chemistry 2011, 128, 1003–1016.
    • (2011) Food Chemistry , vol.128 , pp. 1003-1016
    • Jayasundera, M.1    Adhikari, B.2    Howes, T.3    Aldred, P.4
  • 42
    • 80051784470 scopus 로고    scopus 로고
    • Physicochemical and functional properties of lentil protein isolates prepared by different drying methods
    • M.Joshi, ; B.Adhikari, ; P.Aldred, ; J.F.Panozzo, ; S.Kasapis, Physicochemical and functional properties of lentil protein isolates prepared by different drying methods. Food Chemistry 2011, 129, 1513–1522.
    • (2011) Food Chemistry , vol.129 , pp. 1513-1522
    • Joshi, M.1    Adhikari, B.2    Aldred, P.3    Panozzo, J.F.4    Kasapis, S.5
  • 43
    • 0141720327 scopus 로고    scopus 로고
    • Detection and quantification of bovine, ovine and caprine milk percentages in protected denomination of origin cheeses by reversed-phase high-performance liquid chromatography of beta-lactoglobulins
    • I.M.P.L.V.O.Ferreira, ; H.Caçote, Detection and quantification of bovine, ovine and caprine milk percentages in protected denomination of origin cheeses by reversed-phase high-performance liquid chromatography of beta-lactoglobulins. Journal of Chromatography A 2003, 1015, 111–118.
    • (2003) Journal of Chromatography A , vol.1015 , pp. 111-118
    • Ferreira, I.M.P.L.V.O.1    Caçote, H.2
  • 44
    • 84885150228 scopus 로고    scopus 로고
    • Drying and denaturation kinetics of whey protein isolate (WPI) during convective air drying process
    • M.A.Haque, ; A.Putranto, ; P.Aldred, ; J.Chen, ; B.Adhikari, Drying and denaturation kinetics of whey protein isolate (WPI) during convective air drying process. Drying Technology 2013, 31, 1532–1544.
    • (2013) Drying Technology , vol.31 , pp. 1532-1544
    • Haque, M.A.1    Putranto, A.2    Aldred, P.3    Chen, J.4    Adhikari, B.5
  • 46
    • 33751158541 scopus 로고
    • Heat-induced conformational changes in whey protein isolate and its relation to foaming properties
    • H.Zhu, ; S.Damodaran, Heat-induced conformational changes in whey protein isolate and its relation to foaming properties. Journal of Agricultural and Food Chemistry 1994, 42, 846–855.
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , pp. 846-855
    • Zhu, H.1    Damodaran, S.2
  • 48
    • 0000243469 scopus 로고
    • The beta-turn conformation in wheat gluten proteins: Relationship to gluten elasticity
    • A.S.Tatham, ; B.J.Miflin, ; P.R.Shewry, The beta-turn conformation in wheat gluten proteins: Relationship to gluten elasticity. Cereal Chemistry 1985, 62, 405–412.
    • (1985) Cereal Chemistry , vol.62 , pp. 405-412
    • Tatham, A.S.1    Miflin, B.J.2    Shewry, P.R.3
  • 49
    • 84890338303 scopus 로고    scopus 로고
    • Properties of whey protein–maltodextrin conjugates as impacted by powder acidity during the Maillard reaction
    • W.Wang, ; Q.Zhong, Properties of whey protein–maltodextrin conjugates as impacted by powder acidity during the Maillard reaction. Food Hydrocolloids 2014, 38, 85–94.
    • (2014) Food Hydrocolloids , vol.38 , pp. 85-94
    • Wang, W.1    Zhong, Q.2
  • 52
    • 5544255120 scopus 로고    scopus 로고
    • Effect of vacuum drying on protein–mannitol interactions: The physical state of mannitol and protein structure in the dried state
    • V.K.Sharma, ; D.S.Kalonia, Effect of vacuum drying on protein–mannitol interactions: The physical state of mannitol and protein structure in the dried state. American Association of Pharmaceutical Scientists PharmSciTech 2004, 5, 1–12.
    • (2004) American Association of Pharmaceutical Scientists PharmSciTech , vol.5 , pp. 1-12
    • Sharma, V.K.1    Kalonia, D.S.2
  • 53
    • 84874533085 scopus 로고    scopus 로고
    • Improving process yield by adding WPI to lactose during crystallization and spray drying under high-humidity conditions
    • M.I.Islam, ; M.Edrisi, ; T.Langrish, Improving process yield by adding WPI to lactose during crystallization and spray drying under high-humidity conditions. Drying Technology 2013, 31, 393–404.
    • (2013) Drying Technology , vol.31 , pp. 393-404
    • Islam, M.I.1    Edrisi, M.2    Langrish, T.3
  • 54
    • 84885136661 scopus 로고    scopus 로고
    • Effects of type and concentration of proteins on the recovery of spray-dried sucrose powder
    • Z.Fang, ; R.Wang, ; B.Bhandari, Effects of type and concentration of proteins on the recovery of spray-dried sucrose powder. Drying Technology 2013, 31, 1643–1652.
    • (2013) Drying Technology , vol.31 , pp. 1643-1652
    • Fang, Z.1    Wang, R.2    Bhandari, B.3
  • 55
    • 0027697920 scopus 로고
    • Droplets of materials which gelatinised at high temperature
    • H.M.Hassan, ; C.J.M.O.D.O.S.-F.M.Mumford, C.J. Mechanisms of drying of skin-forming materials.I. Droplets of materials which gelatinised at high temperature. Drying Technology 1993, 11(7), 1713–1750.
    • (1993) Drying Technology , vol.11 , Issue.7 , pp. 1713-1750
    • Hassan, H.M.1
  • 57
    • 0030213636 scopus 로고    scopus 로고
    • Mechanisms of drying of skin-forming materials; the significance of skin formation and comparison between three types of material
    • H.M.Hassan, ; C.J.Mumford, Mechanisms of drying of skin-forming materials; the significance of skin formation and comparison between three types of material. Drying Technology 1996, 14(7&8), 1763–1777.
    • (1996) Drying Technology , vol.14 , Issue.7-8 , pp. 1763-1777
    • Hassan, H.M.1    Mumford, C.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.