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Volumn 186, Issue , 2016, Pages 69-76

Reduction of particle size based on superfine grinding: Effects on structure, rheological and gelling properties of whey protein concentrate

Author keywords

Gelling properties; Rheological; Structure; Superfine grinding

Indexed keywords

GELS; GRINDING (MACHINING); PARTICLE SIZE; PARTICLE SIZE ANALYSIS; POWDERS; PROTEINS; STRUCTURE (COMPOSITION);

EID: 84992307242     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2016.03.002     Document Type: Article
Times cited : (55)

References (42)
  • 1
    • 39649116430 scopus 로고    scopus 로고
    • Particle size distribution and compositional effects on textural properties and appearance of dark chocolates
    • E.O. Afoakwa, A. Paterson, M. Fowler, and J. Vieira Particle size distribution and compositional effects on textural properties and appearance of dark chocolates J. Food Eng. 87 2 2008 181 190
    • (2008) J. Food Eng. , vol.87 , Issue.2 , pp. 181-190
    • Afoakwa, E.O.1    Paterson, A.2    Fowler, M.3    Vieira, J.4
  • 2
    • 80054951068 scopus 로고    scopus 로고
    • Comparative study of high intensity ultrasound effects on food proteins functionality
    • C. Arzeni, K. Martínez, P. Zema, A. Arias, O.E. Pérez, and A.M.R. Pilosof Comparative study of high intensity ultrasound effects on food proteins functionality J. Food Eng. 108 3 2012 463 472
    • (2012) J. Food Eng. , vol.108 , Issue.3 , pp. 463-472
    • Arzeni, C.1    Martínez, K.2    Zema, P.3    Arias, A.4    Pérez, O.E.5    Pilosof, A.M.R.6
  • 4
    • 79956344900 scopus 로고    scopus 로고
    • Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate
    • J. Chandrapala, B. Zisu, M. Palmer, S. Kentish, and M. Ashokkumar Effects of ultrasound on the thermal and structural characteristics of proteins in reconstituted whey protein concentrate Ultrason. Sonochem. 18 5 2011 951 957
    • (2011) Ultrason. Sonochem. , vol.18 , Issue.5 , pp. 951-957
    • Chandrapala, J.1    Zisu, B.2    Palmer, M.3    Kentish, S.4    Ashokkumar, M.5
  • 5
    • 0036328703 scopus 로고    scopus 로고
    • Influence of NaCl on optical properties, large-strain rheology and water holding capacity of heat-induced whey protein isolate gels
    • W. Chantrapornchai, and D.J. McClements Influence of NaCl on optical properties, large-strain rheology and water holding capacity of heat-induced whey protein isolate gels Food Hydrocoll. 16 5 2002 467 476
    • (2002) Food Hydrocoll. , vol.16 , Issue.5 , pp. 467-476
    • Chantrapornchai, W.1    McClements, D.J.2
  • 6
    • 34547843061 scopus 로고    scopus 로고
    • Sensory properties of meal replacement bars and beverages made from whey and soy proteins
    • J. Childs, M. Yates, and M. Drake Sensory properties of meal replacement bars and beverages made from whey and soy proteins J. food Sci. 72 6 2007 S425 S434
    • (2007) J. Food Sci. , vol.72 , Issue.6 , pp. S425-S434
    • Childs, J.1    Yates, M.2    Drake, M.3
  • 7
    • 27144501099 scopus 로고    scopus 로고
    • Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry
    • S.-M. Choi, and C.-Y. Ma Conformational study of globulin from common buckwheat (Fagopyrum esculentum Moench) by Fourier transform infrared spectroscopy and differential scanning calorimetry J. Agric. Food Chem. 53 20 2005 8046 8053
    • (2005) J. Agric. Food Chem. , vol.53 , Issue.20 , pp. 8046-8053
    • Choi, S.-M.1    Ma, C.-Y.2
  • 8
    • 84866164096 scopus 로고    scopus 로고
    • Hydrostatic pressure effects on the structural properties of condensed whey protein/lactose systems
    • M. Dissanayake, S. Kasapis, P. George, B. Adhikari, M. Palmer, and B. Meurer Hydrostatic pressure effects on the structural properties of condensed whey protein/lactose systems Food Hydrocoll. 30 2 2013 632 640
    • (2013) Food Hydrocoll. , vol.30 , Issue.2 , pp. 632-640
    • Dissanayake, M.1    Kasapis, S.2    George, P.3    Adhikari, B.4    Palmer, M.5    Meurer, B.6
  • 9
    • 85001229637 scopus 로고    scopus 로고
    • Effects of superfine grinding on physical-chemical characteristics and processing properties of glutinous rice
    • M.-r. Fu, Q.-m. Chen, F. Liu, Q.-s. Wang, and X. Wang Effects of superfine grinding on physical-chemical characteristics and processing properties of glutinous rice Food Nutr. China 6 2011 011
    • (2011) Food Nutr. China , vol.6 , pp. 011
    • Fu, M.-R.1    Chen, Q.-M.2    Liu, F.3    Wang, Q.-S.4    Wang, X.5
  • 10
    • 79958175070 scopus 로고    scopus 로고
    • Influence of pH on the dry heat-induced denaturation/aggregation of whey proteins
    • M. Gulzar, S. Bouhallab, R. Jeantet, P. Schuck, and T. Croguennec Influence of pH on the dry heat-induced denaturation/aggregation of whey proteins Food Chem. 129 1 2011 110 116
    • (2011) Food Chem. , vol.129 , Issue.1 , pp. 110-116
    • Gulzar, M.1    Bouhallab, S.2    Jeantet, R.3    Schuck, P.4    Croguennec, T.5
  • 11
    • 0000685269 scopus 로고
    • Microparticulation by jet mill grinding of protein powders and effects on hydrophobicity
    • I. Hayakawa, Y. Yamada, and Y. Fujio Microparticulation by jet mill grinding of protein powders and effects on hydrophobicity J. Food Sci. 58 5 1993 1026 1029
    • (1993) J. Food Sci. , vol.58 , Issue.5 , pp. 1026-1029
    • Hayakawa, I.1    Yamada, Y.2    Fujio, Y.3
  • 12
    • 84867744049 scopus 로고    scopus 로고
    • Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments
    • H. Hu, X. Fan, Z. Zhou, X. Xu, G. Fan, L. Wang, X. Huang, S. Pan, and L. Zhu Acid-induced gelation behavior of soybean protein isolate with high intensity ultrasonic pre-treatments Ultrason. Sonochem. 20 1 2013 187 195
    • (2013) Ultrason. Sonochem. , vol.20 , Issue.1 , pp. 187-195
    • Hu, H.1    Fan, X.2    Zhou, Z.3    Xu, X.4    Fan, G.5    Wang, L.6    Huang, X.7    Pan, S.8    Zhu, L.9
  • 13
    • 84874416406 scopus 로고    scopus 로고
    • The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate
    • H. Hu, E.C.Y. Li-Chan, L. Wan, M. Tian, and S. Pan The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate Food Hydrocoll. 32 2 2013 303 311
    • (2013) Food Hydrocoll. , vol.32 , Issue.2 , pp. 303-311
    • Hu, H.1    Li-Chan, E.C.Y.2    Wan, L.3    Tian, M.4    Pan, S.5
  • 14
    • 80052961953 scopus 로고    scopus 로고
    • Effect of superfine grinding on quality and antioxidant property of fine green tea powders
    • J. Hu, Y. Chen, and D. Ni Effect of superfine grinding on quality and antioxidant property of fine green tea powders LWT Food Sci. Technol. 45 1 2012 8 12
    • (2012) LWT Food Sci. Technol. , vol.45 , Issue.1 , pp. 8-12
    • Hu, J.1    Chen, Y.2    Ni, D.3
  • 15
    • 84919882827 scopus 로고    scopus 로고
    • Enhancement of the gelation properties of hairtail (Trichiurus haumela) muscle protein with curdlan and transglutaminase
    • Y. Hu, W. Liu, C. Yuan, K. Morioka, S. Chen, D. Liu, and X. Ye Enhancement of the gelation properties of hairtail (Trichiurus haumela) muscle protein with curdlan and transglutaminase Food Chem. 176 0 2015 115 122
    • (2015) Food Chem. , vol.176 , pp. 115-122
    • Hu, Y.1    Liu, W.2    Yuan, C.3    Morioka, K.4    Chen, S.5    Liu, D.6    Ye, X.7
  • 16
    • 34247501186 scopus 로고    scopus 로고
    • Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting
    • J.-S. Hwang, K.-M. Lai, and K.-C. Hsu Changes in textural and rheological properties of gels from tilapia muscle proteins induced by high pressure and setting Food Chem. 104 2 2007 746 753
    • (2007) Food Chem. , vol.104 , Issue.2 , pp. 746-753
    • Hwang, J.-S.1    Lai, K.-M.2    Hsu, K.-C.3
  • 17
    • 0040915889 scopus 로고    scopus 로고
    • Effects of lecithin on thermally induced whey protein isolate gels
    • S. Ikeda, and E. Foegeding Effects of lecithin on thermally induced whey protein isolate gels Food Hydrocoll. 13 3 1999 239 244
    • (1999) Food Hydrocoll. , vol.13 , Issue.3 , pp. 239-244
    • Ikeda, S.1    Foegeding, E.2
  • 18
    • 77955049778 scopus 로고    scopus 로고
    • Impact of phase separation of whey proteins/hydroxypropylmethylcellulose mixtures on gelation dynamics and gels properties
    • F. Jara, O.E. Pérez, and A.M.R. Pilosof Impact of phase separation of whey proteins/hydroxypropylmethylcellulose mixtures on gelation dynamics and gels properties Food Hydrocoll. 24 6-7 2010 641 651
    • (2010) Food Hydrocoll. , vol.24 , Issue.6-7 , pp. 641-651
    • Jara, F.1    Pérez, O.E.2    Pilosof, A.M.R.3
  • 19
    • 84870558602 scopus 로고    scopus 로고
    • Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase
    • J. Jiang, and Y.L. Xiong Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase Meat Sci. 93 3 2013 469 476
    • (2013) Meat Sci. , vol.93 , Issue.3 , pp. 469-476
    • Jiang, J.1    Xiong, Y.L.2
  • 20
    • 39549116952 scopus 로고    scopus 로고
    • Influence of novel food processing technologies on the rheological and thermophysical properties of whey proteins
    • G. Krešić, V. Lelas, A.R. Jambrak, Z. Herceg, and S.R. Brnčić Influence of novel food processing technologies on the rheological and thermophysical properties of whey proteins J. Food Eng. 87 1 2008 64 73
    • (2008) J. Food Eng. , vol.87 , Issue.1 , pp. 64-73
    • Krešić, G.1    Lelas, V.2    Jambrak, A.R.3    Herceg, Z.4    Brnčić, S.R.5
  • 21
    • 47749093534 scopus 로고    scopus 로고
    • Particle size distribution of distillers dried grains with solubles (DDGS) and relationships to compositional and color properties
    • K. Liu Particle size distribution of distillers dried grains with solubles (DDGS) and relationships to compositional and color properties Bioresour. Technol. 99 17 2008 8421 8428
    • (2008) Bioresour. Technol. , vol.99 , Issue.17 , pp. 8421-8428
    • Liu, K.1
  • 22
    • 50249126674 scopus 로고    scopus 로고
    • Role of secondary structures in the gelation of porcine myosin at different pH values
    • R. Liu, S.m. Zhao, S.b Xiong, B.j Xie, and L.h. Qin Role of secondary structures in the gelation of porcine myosin at different pH values Meat Sci. 80 3 2008 632 639
    • (2008) Meat Sci. , vol.80 , Issue.3 , pp. 632-639
    • Liu, R.1    Zhao, S.M.2    Xiong, S.B.3    Xie, B.J.4    Qin, L.H.5
  • 23
    • 0035117850 scopus 로고    scopus 로고
    • Functional improvement of whey protein concentrate on interaction with pectin
    • S. Mishra, B. Mann, and V.K. Joshi Functional improvement of whey protein concentrate on interaction with pectin Food Hydrocoll. 15 1 2001 9 15
    • (2001) Food Hydrocoll. , vol.15 , Issue.1 , pp. 9-15
    • Mishra, S.1    Mann, B.2    Joshi, V.K.3
  • 24
    • 0027347215 scopus 로고
    • Whey protein concentrates and isolates: Processing and functional properties
    • C. Morr, and E. Ha Whey protein concentrates and isolates: processing and functional properties Crit. Rev. Food Sci. Nutr. 33 6 1993 431 476
    • (1993) Crit. Rev. Food Sci. Nutr. , vol.33 , Issue.6 , pp. 431-476
    • Morr, C.1    Ha, E.2
  • 25
    • 84877792443 scopus 로고    scopus 로고
    • Viscosity of high concentration protein formulations of monoclonal antibodies of the IgG1 and IgG4 subclass - Prediction of viscosity through protein-protein interaction measurements
    • M.S. Neergaard, D.S. Kalonia, H. Parshad, A.D. Nielsen, E.H. Møller, and M. van de Weert Viscosity of high concentration protein formulations of monoclonal antibodies of the IgG1 and IgG4 subclass - prediction of viscosity through protein-protein interaction measurements Eur. J. Pharm. Sci. 49 3 2013 400 410
    • (2013) Eur. J. Pharm. Sci. , vol.49 , Issue.3 , pp. 400-410
    • Neergaard, M.S.1    Kalonia, D.S.2    Parshad, H.3    Nielsen, A.D.4    Møller, E.H.5    Van De Weert, M.6
  • 26
    • 19944370818 scopus 로고    scopus 로고
    • A comparative study of heat and high pressure induced gels of whey and egg albumen proteins and their binary mixtures
    • S. Ngarize, A. Adams, and N. Howell A comparative study of heat and high pressure induced gels of whey and egg albumen proteins and their binary mixtures Food Hydrocoll. 19 6 2005 984 996
    • (2005) Food Hydrocoll. , vol.19 , Issue.6 , pp. 984-996
    • Ngarize, S.1    Adams, A.2    Howell, N.3
  • 27
    • 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, and 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 J. Agric. Food Chem. 52 21 2004 6470 6477
    • (2004) J. Agric. Food Chem. , vol.52 , Issue.21 , pp. 6470-6477
    • Ngarize, S.1    Herman, H.2    Adams, A.3    Howell, N.4
  • 28
    • 79961167329 scopus 로고    scopus 로고
    • Reducing the stiffness of concentrated whey protein isolate (WPI) gels by using WPI microparticles
    • N. Purwanti, A. Moerkens, A.J. Van der Goot, and R. Boom Reducing the stiffness of concentrated whey protein isolate (WPI) gels by using WPI microparticles Food Hydrocoll. 26 1 2012 240 248
    • (2012) Food Hydrocoll. , vol.26 , Issue.1 , pp. 240-248
    • Purwanti, N.1    Moerkens, A.2    Van Der Goot, A.J.3    Boom, R.4
  • 30
    • 84919439060 scopus 로고    scopus 로고
    • Properties of heat-induced gels of caprine whey protein concentrates obtained from clarified cheese whey
    • B. Sanmartín, O. Díaz, L. Rodríguez-Turienzo, and Á. Cobos Properties of heat-induced gels of caprine whey protein concentrates obtained from clarified cheese whey Small Rumin. Res. 123 1 2015 142 148
    • (2015) Small Rumin. Res. , vol.123 , Issue.1 , pp. 142-148
    • Sanmartín, B.1    Díaz, O.2    Rodríguez-Turienzo, L.3    Cobos, Á.4
  • 31
    • 80054686062 scopus 로고    scopus 로고
    • Evaluation of structural changes in raw and heated meat batters prepared with different lipids using Raman spectroscopy
    • J.-H. Shao, Y.-F. Zou, X.-L. Xu, J.-Q. Wu, and G.-H. Zhou Evaluation of structural changes in raw and heated meat batters prepared with different lipids using Raman spectroscopy Food Res. Int. 44 9 2011 2955 2961
    • (2011) Food Res. Int. , vol.44 , Issue.9 , pp. 2955-2961
    • Shao, J.-H.1    Zou, Y.-F.2    Xu, X.-L.3    Wu, J.-Q.4    Zhou, G.-H.5
  • 32
    • 0000326329 scopus 로고
    • Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate
    • K. Shimada, and J.C. Cheftel Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate J. Agric. Food Chem. 37 1 1989 161 168
    • (1989) J. Agric. Food Chem. , vol.37 , Issue.1 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 33
    • 24744444064 scopus 로고    scopus 로고
    • Probe into characteristics of Taraxacum mongolicum ultramicro-power
    • Zhongguo Zhong yao za zhi= Zhongguo zhongyao zazhi
    • L.-L. Song, B.-Y. Fan, S.-Z. Jiang, and D.-L. Zhang Probe into characteristics of Taraxacum mongolicum ultramicro-power China J. Chin. Materia Medica Zhongguo Zhong yao za zhi= Zhongguo zhongyao zazhi 27 1 2002 12 15
    • (2002) China J. Chin. Materia Medica , vol.27 , Issue.1 , pp. 12-15
    • Song, L.-L.1    Fan, B.-Y.2    Jiang, S.-Z.3    Zhang, D.-L.4
  • 34
    • 79959625364 scopus 로고    scopus 로고
    • Secondary structure of chorion proteins of the Lepidoptera Pericallia ricini and Ariadne merione by ATR FT-IR and micro-Raman spectroscopy
    • A. Srivastava, V. Iconomidou, G. Chryssikos, V. Gionis, K. Kumar, and S. Hamodrakas Secondary structure of chorion proteins of the Lepidoptera Pericallia ricini and Ariadne merione by ATR FT-IR and micro-Raman spectroscopy Int. J. Biol. Macromol. 49 3 2011 317 322
    • (2011) Int. J. Biol. Macromol. , vol.49 , Issue.3 , pp. 317-322
    • Srivastava, A.1    Iconomidou, V.2    Chryssikos, G.3    Gionis, V.4    Kumar, K.5    Hamodrakas, S.6
  • 35
    • 85001210778 scopus 로고    scopus 로고
    • Combined superfine grinding and heat-shearing treatment for the microparticulation of whey proteins
    • C. Sun, R. Liu, T. Wu, B. Liang, C. Shi, X. Cong, T. Hou, and M. Zhang Combined superfine grinding and heat-shearing treatment for the microparticulation of whey proteins Food Bioprocess Technol. 2015 1 9
    • (2015) Food Bioprocess Technol. , pp. 1-9
    • Sun, C.1    Liu, R.2    Wu, T.3    Liang, B.4    Shi, C.5    Cong, X.6    Hou, T.7    Zhang, M.8
  • 36
    • 84942774890 scopus 로고    scopus 로고
    • Effect of superfine grinding on the structural and physicochemical properties of whey protein and applications for microparticulated proteins
    • C. Sun, R. Liu, T. Wu, B. Liang, C. Shi, and M. Zhang Effect of superfine grinding on the structural and physicochemical properties of whey protein and applications for microparticulated proteins Food Sci. Biotechnol. 24 5 2015 1637 1643
    • (2015) Food Sci. Biotechnol. , vol.24 , Issue.5 , pp. 1637-1643
    • Sun, C.1    Liu, R.2    Wu, T.3    Liang, B.4    Shi, C.5    Zhang, M.6
  • 37
    • 84933523078 scopus 로고    scopus 로고
    • Effects of superfine grinding and microparticulation on the surface hydrophobicity of whey protein concentrate and its relation to emulsions stability
    • C. Sun, T. Wu, R. Liu, B. Liang, Z. Tian, E. Zhang, and M. Zhang Effects of superfine grinding and microparticulation on the surface hydrophobicity of whey protein concentrate and its relation to emulsions stability Food Hydrocoll. 51 2015 512 518
    • (2015) Food Hydrocoll. , vol.51 , pp. 512-518
    • Sun, C.1    Wu, T.2    Liu, R.3    Liang, B.4    Tian, Z.5    Zhang, E.6    Zhang, M.7
  • 38
    • 84938789978 scopus 로고    scopus 로고
    • Rheology and microstructure of heat-induced fluid gels from Antarctic krill (Euphausia superba) protein: Effect of pH
    • Y. Wang, Y. Chang, Y. Xue, Z. Li, Y. Wang, and C. Xue Rheology and microstructure of heat-induced fluid gels from Antarctic krill (Euphausia superba) protein: effect of pH Food Hydrocoll. 52 2016 510 519
    • (2016) Food Hydrocoll. , vol.52 , pp. 510-519
    • Wang, Y.1    Chang, Y.2    Xue, Y.3    Li, Z.4    Wang, Y.5    Xue, C.6
  • 39
    • 84929468063 scopus 로고    scopus 로고
    • Preparation and thermo-reversible gelling properties of protein isolate from defatted Antarctic krill (Euphausia superba) byproducts
    • Y. Wang, R. Wang, Y. Chang, Y. Gao, Z. Li, and C. Xue Preparation and thermo-reversible gelling properties of protein isolate from defatted Antarctic krill (Euphausia superba) byproducts Food Chem. 188 2015 170 176
    • (2015) Food Chem. , vol.188 , pp. 170-176
    • Wang, Y.1    Wang, R.2    Chang, Y.3    Gao, Y.4    Li, Z.5    Xue, C.6
  • 40
    • 84894091182 scopus 로고    scopus 로고
    • Effect of pre-emulsification of plant lipid treated by pulsed ultrasound on the functional properties of chicken breast myofibrillar protein composite gel
    • Y.-Y. Zhao, P. Wang, Y.-F. Zou, K. Li, Z.-L. Kang, X.-L. Xu, and G.-H. Zhou Effect of pre-emulsification of plant lipid treated by pulsed ultrasound on the functional properties of chicken breast myofibrillar protein composite gel Food Res. Int. 58 2014 98 104
    • (2014) Food Res. Int. , vol.58 , pp. 98-104
    • Zhao, Y.-Y.1    Wang, P.2    Zou, Y.-F.3    Li, K.4    Kang, Z.-L.5    Xu, X.-L.6    Zhou, G.-H.7
  • 41
    • 84936931538 scopus 로고    scopus 로고
    • Influence of pH and ionic strength on heat-induced formation and rheological properties of cottonseed protein gels
    • J.-z. Zhou, H. Zhang, L. Gao, L. Wang, and H.-F. Qian Influence of pH and ionic strength on heat-induced formation and rheological properties of cottonseed protein gels Food Bioprod. Process. 96 2015 27 34
    • (2015) Food Bioprod. Process. , vol.96 , pp. 27-34
    • Zhou, J.-Z.1    Zhang, H.2    Gao, L.3    Wang, L.4    Qian, H.-F.5
  • 42
    • 84942589106 scopus 로고    scopus 로고
    • Superfine grinding improves functional properties and antioxidant capacities of bran dietary fibre from Qingke (hull-less barley) grown in Qinghai-Tibet Plateau, China
    • F. Zhu, B. Du, and B. Xu Superfine grinding improves functional properties and antioxidant capacities of bran dietary fibre from Qingke (hull-less barley) grown in Qinghai-Tibet Plateau, China J. Cereal Sci. 65 2015 43 47
    • (2015) J. Cereal Sci. , vol.65 , pp. 43-47
    • Zhu, F.1    Du, B.2    Xu, B.3


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