메뉴 건너뛰기




Volumn 170, Issue , 2015, Pages 33-40

Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate

Author keywords

Disulfide bond; Emulsifying properties; Flexibility; Peanut protein isolate; Secondary structure; Surface hydrophobicity

Indexed keywords

COVALENT BONDS; DRYING; FLEXIBLE STRUCTURES; FOOD PROCESSING; FOURIER TRANSFORM INFRARED SPECTROSCOPY; HYDROGEN BONDS; HYDROPHOBICITY; OILSEEDS; PHASE INTERFACES; PROTEINS; SPRAY DRYING; STRUCTURAL PROPERTIES;

EID: 84952863030     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2015.09.011     Document Type: Article
Times cited : (143)

References (36)
  • 1
    • 0036722336 scopus 로고    scopus 로고
    • Application of a simplified method based on regular regime approach to determine the effective moisture dilusivity of mixture of low molecular weight sugars and maltodextrin
    • B. Adhikari, T. Howes, B.R. Bhandari, S. Yamamoto, and V. Troung Application of a simplified method based on regular regime approach to determine the effective moisture dilusivity of mixture of low molecular weight sugars and maltodextrin J. Food Eng. 54 2002 157 165
    • (2002) J. Food Eng. , vol.54 , pp. 157-165
    • Adhikari, B.1    Howes, T.2    Bhandari, B.R.3    Yamamoto, S.4    Troung, V.5
  • 2
    • 0142106520 scopus 로고    scopus 로고
    • Effect of addition of maltodextrin on drying kinetics and stickiness of sugar and acid-rich foods during convective drying: Experiments and modeling
    • B. Adhikari, T. Howes, B.R. Bhandari, and V. Troung Effect of addition of maltodextrin on drying kinetics and stickiness of sugar and acid-rich foods during convective drying: experiments and modeling J. Food Eng. 62 2004 53 68
    • (2004) J. Food Eng. , vol.62 , pp. 53-68
    • Adhikari, B.1    Howes, T.2    Bhandari, B.R.3    Troung, V.4
  • 3
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • A. Barth Infrared spectroscopy of proteins Biochim. Biophys. Acta 1767 2007 1073 1101
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 4
    • 0012067672 scopus 로고
    • Functional and electrophoretic characteristics of succinylated peanut flour proteins
    • L.R. Beuchat Functional and electrophoretic characteristics of succinylated peanut flour proteins J. Agric. Food Chem. 25 2 1977 258 261
    • (1977) J. Agric. Food Chem. , vol.25 , Issue.2 , pp. 258-261
    • Beuchat, L.R.1
  • 5
    • 85032119438 scopus 로고
    • Determination of SH- and SS- groups in some food proteins using Ellman's reagent
    • T. Beveridge, S.J. Toma, and S.D. Nakai Determination of SH- and SS- groups in some food proteins using Ellman's reagent J. Food Sci. 39 1974 49 51
    • (1974) J. Food Sci. , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.J.2    Nakai, S.D.3
  • 6
    • 75149150222 scopus 로고    scopus 로고
    • Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques
    • J.I. Boye, S. Aksay, S. Roufik, S. Ribéreau, M. Mondor, E. Farnworth, and S.H. Rajamohamed Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques Food Res. Int. 43 2010 537 546
    • (2010) Food Res. Int. , vol.43 , pp. 537-546
    • Boye, J.I.1    Aksay, S.2    Roufik, S.3    Ribéreau, S.4    Mondor, M.5    Farnworth, E.6    Rajamohamed, S.H.7
  • 7
    • 0344561302 scopus 로고
    • Particle structure of spray dried caseinate and spray-dried lactose as observed by a scanning electron microscope
    • T.J. Buma, and S. Henstra Particle structure of spray dried caseinate and spray-dried lactose as observed by a scanning electron microscope Neith Milk Dairy J. 25 1971 278 284
    • (1971) Neith Milk Dairy J. , vol.25 , pp. 278-284
    • Buma, T.J.1    Henstra, S.2
  • 8
    • 0010431656 scopus 로고
    • Quantitative studies of protein structure by FT-IR spectral deconvolution and curve fitting
    • D.M. Byler, J.N. Brouillette, and H. Susi Quantitative studies of protein structure by FT-IR spectral deconvolution and curve fitting Spectroscopy 1 3 1986 19 32
    • (1986) Spectroscopy , vol.1 , Issue.3 , pp. 19-32
    • Byler, D.M.1    Brouillette, J.N.2    Susi, H.3
  • 9
    • 84858149133 scopus 로고    scopus 로고
    • Effect of drying methods on the physical properties and microstructures of mango (Philippine 'Carabao' var.) powder
    • O.A. Caparino, J. Tang, C.I. Nindo, S.S. Sablani, J.R. Powers, and J.K. Fellman Effect of drying methods on the physical properties and microstructures of mango (Philippine 'Carabao' var.) powder J. Food Eng. 111 2012 135 148
    • (2012) J. Food Eng. , vol.111 , pp. 135-148
    • Caparino, O.A.1    Tang, J.2    Nindo, C.I.3    Sablani, S.S.4    Powers, J.R.5    Fellman, J.K.6
  • 11
    • 0035146503 scopus 로고    scopus 로고
    • Milk protein interfacial layers and the relationship to emulsion stability and rheology, Colloid
    • E. Dickinson Milk protein interfacial layers and the relationship to emulsion stability and rheology, Colloid Surface B, 20 2001 197 210
    • (2001) Surface B , vol.20 , pp. 197-210
    • Dickinson, E.1
  • 12
    • 84857974517 scopus 로고    scopus 로고
    • Nutritional and functional characterization of defatted seed cake flour of two sudanese groundnut (Arachis hypogaea) cultivars
    • A.M. Fekria, A.M.A. Isam, O.A. Suha, and E.B. Elfadil Nutritional and functional characterization of defatted seed cake flour of two sudanese groundnut (Arachis hypogaea) cultivars Int. Food Res. J. 19 2012 629 637
    • (2012) Int. Food Res. J. , vol.19 , pp. 629-637
    • Fekria, A.M.1    Isam, A.M.A.2    Suha, O.A.3    Elfadil, E.B.4
  • 13
    • 84896137310 scopus 로고    scopus 로고
    • Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions
    • X.L. Feng, H.Z. Liu, A.M. Shi, L. Liu, Q. Wang, and B. Adhikari Effects of transglutaminase catalyzed crosslinking on physicochemical characteristics of arachin and conarachin-rich peanut protein fractions Food Res. Int. 62 2014 84 90
    • (2014) Food Res. Int. , vol.62 , pp. 84-90
    • Feng, X.L.1    Liu, H.Z.2    Shi, A.M.3    Liu, L.4    Wang, Q.5    Adhikari, B.6
  • 14
    • 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, and B. Adihikari Drying and denaturation kinetics of whey protein isolate (WPI) during convective air drying process Dry. Technol. 31 2013 1532 1544
    • (2013) Dry. Technol. , vol.31 , pp. 1532-1544
    • Haque, M.A.1    Putranto, A.2    Aldred, P.3    Chen, J.4    Adihikari, B.5
  • 15
    • 84885724866 scopus 로고    scopus 로고
    • Effects of high pressure on the physicochemical and functional properties of peanut protein isolates
    • X.H. He, H.Z. Liu, L. Liu, G.L. Zhao, Q. Wang, and Q.L. Chen Effects of high pressure on the physicochemical and functional properties of peanut protein isolates Food Hydrocoll. 36 2014 123 129
    • (2014) Food Hydrocoll. , vol.36 , pp. 123-129
    • He, X.H.1    Liu, H.Z.2    Liu, L.3    Zhao, G.L.4    Wang, Q.5    Chen, Q.L.6
  • 16
    • 77957806506 scopus 로고    scopus 로고
    • Effects of partial hydrolysis and plasticizer content on the properties of film from cuttle sh (Sepia pharaonis) skin gelatin
    • M.S. Hoque, S. Benjakul, and T. Prodpran Effects of partial hydrolysis and plasticizer content on the properties of film from cuttle sh (Sepia pharaonis) skin gelatin Food Hydrocoll. 25 2011 82 90
    • (2011) Food Hydrocoll. , vol.25 , pp. 82-90
    • Hoque, M.S.1    Benjakul, S.2    Prodpran, T.3
  • 17
    • 77954751565 scopus 로고    scopus 로고
    • Effects of drying method on physicochemical and functional properties of soy protein isolates
    • X.Z. Hu, Y.Q. Cheng, J.F. Fan, Z.H. Lui, K. Yamaki, and L.T. Li Effects of drying method on physicochemical and functional properties of soy protein isolates J. Food Process. Preserv. 34 2010 520 540
    • (2010) J. Food Process. Preserv. , vol.34 , pp. 520-540
    • Hu, X.Z.1    Cheng, Y.Q.2    Fan, J.F.3    Lui, Z.H.4    Yamaki, K.5    Li, L.T.6
  • 18
    • 84899823421 scopus 로고    scopus 로고
    • Emulsifying properties of cross-linking between proteins extracted from cold/hot pressed peanut meal and hydrolysed fish (Decapterus maruadsi) proteins
    • X. Hu, M.M. Zhao, L.H. Li, B. Yang, X.Q. Yang, H.Y. Wang, and J.Y. Ren Emulsifying properties of cross-linking between proteins extracted from cold/hot pressed peanut meal and hydrolysed fish (Decapterus maruadsi) proteins Int. J. Food Prop. 17 2014 1750 1762
    • (2014) Int. J. Food Prop. , vol.17 , pp. 1750-1762
    • Hu, X.1    Zhao, M.M.2    Li, L.H.3    Yang, B.4    Yang, X.Q.5    Wang, H.Y.6    Ren, J.Y.7
  • 19
    • 75749122983 scopus 로고    scopus 로고
    • Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate
    • S. Jamdar, V. Rajalakshmi, M. Pednekar, F. Juan, V. Yardi, and A. Sharma Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate Food Chem. 121 2010 178 184
    • (2010) Food Chem. , vol.121 , pp. 178-184
    • Jamdar, S.1    Rajalakshmi, V.2    Pednekar, M.3    Juan, F.4    Yardi, V.5    Sharma, A.6
  • 20
    • 0007496851 scopus 로고    scopus 로고
    • Interpretive spectroscopy for near infrared
    • J. Jerome, and J.R. Workman Interpretive spectroscopy for near infrared Appl. Spectrosc. Rev. 31 3 1996 251 320
    • (1996) Appl. Spectrosc. Rev. , vol.31 , Issue.3 , pp. 251-320
    • Jerome, J.1    Workman, J.R.2
  • 21
    • 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, and S. Kasapis Physicochemical and functional properties of lentil protein isolates prepared by different drying methods Food Chem. 129 2011 1513 1522
    • (2011) Food Chem. , vol.129 , pp. 1513-1522
    • Joshi, M.1    Adhikari, B.2    Aldred, P.3    Panozzo, J.F.4    Kasapis, S.5
  • 23
    • 77953152739 scopus 로고    scopus 로고
    • Physico-functional properties of peanut meal flour as affected by processing methods
    • R.J. Kain, and Z.X. Chen Physico-functional properties of peanut meal flour as affected by processing methods J. Food Biochem. 34 2010 229 243
    • (2010) J. Food Biochem. , vol.34 , pp. 229-243
    • Kain, R.J.1    Chen, Z.X.2
  • 24
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a f1uorescence probe method and its conelation with surface properties of proteins
    • A. Kato, and S. Nakai Hydrophobicity determined by a f1uorescence probe method and its conelation with surface properties of proteins Biochim. Biophys. Acta 624 1980 13 20
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 25
    • 84901291145 scopus 로고    scopus 로고
    • Physicochemical properties of peanut protein isolate-glucomannan conjugates prepared by ultrasonic treatment
    • C. Li, X.J. Huang, Q. Peng, Y.Y. Shan, and F. Xue Physicochemical properties of peanut protein isolate-glucomannan conjugates prepared by ultrasonic treatment Ultrason. Sonochem. 21 2014 1722 1727
    • (2014) Ultrason. Sonochem. , vol.21 , pp. 1722-1727
    • Li, C.1    Huang, X.J.2    Peng, Q.3    Shan, Y.Y.4    Xue, F.5
  • 26
    • 84866407057 scopus 로고    scopus 로고
    • Functional, conformational and topographical changes of succinic acid deamidated wheat gluten upon freeze- and spray-drying: A comparative study
    • L. Liao, Q. Wang, and M.M. Zhao Functional, conformational and topographical changes of succinic acid deamidated wheat gluten upon freeze- and spray-drying: a comparative study LWT Food Sci. Technol. 50 2013 177 184
    • (2013) LWT Food Sci. Technol. , vol.50 , pp. 177-184
    • Liao, L.1    Wang, Q.2    Zhao, M.M.3
  • 27
    • 79960083927 scopus 로고    scopus 로고
    • Effect of denaturation during extraction on the conformational and functional properties of peanut protein isolate
    • Y. Liu, G.L. Zhao, J.Y. Ren, M.M. Zhao, and B. Yang Effect of denaturation during extraction on the conformational and functional properties of peanut protein isolate Innov. Food Sci. Emerg. Technol. 12 2011 375 380
    • (2011) Innov. Food Sci. Emerg. Technol. , vol.12 , pp. 375-380
    • Liu, Y.1    Zhao, G.L.2    Ren, J.Y.3    Zhao, M.M.4    Yang, B.5
  • 28
    • 84901759829 scopus 로고    scopus 로고
    • Evidence of conformational changes in oil molecules with protein aggregation and conformational changes at oil-'protein solution' interface
    • P. Patra, and P. Somasundaran Evidence of conformational changes in oil molecules with protein aggregation and conformational changes at oil-'protein solution' interface Coll. Surf. B Biointerfaces 120 2014 132 141
    • (2014) Coll. Surf. B Biointerfaces , vol.120 , pp. 132-141
    • Patra, P.1    Somasundaran, P.2
  • 29
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of turbidimentric technique
    • K.N. Pearce, and J.E. Kinsella Emulsifying properties of proteins: evaluation of turbidimentric technique J. Agric. Food Chem. 26 3 1978 716 723
    • (1978) J. Agric. Food Chem. , vol.26 , Issue.3 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 30
    • 77955944455 scopus 로고    scopus 로고
    • The influence of additives and drying methods on quality attributes of fish protein powder made from saithe (Pollachius virens)
    • G.R. Shaviklo, G. Thorkelsson, and S. Arason The influence of additives and drying methods on quality attributes of fish protein powder made from saithe (Pollachius virens) J. Sci. Food Agric. 90 2010 2133 2143
    • (2010) J. Sci. Food Agric. , vol.90 , pp. 2133-2143
    • Shaviklo, G.R.1    Thorkelsson, G.2    Arason, S.3
  • 31
    • 84892595882 scopus 로고    scopus 로고
    • Studies on the functional properties of protein concentrate of Kappaphycus alvarezii (Doty) Doty-An edible seaweed
    • K. Suresh Kumar, K. Ganesan, Kandasami Selvaraj, and P.V. Subba Rao Studies on the functional properties of protein concentrate of Kappaphycus alvarezii (Doty) Doty-An edible seaweed Food Chem. 153 2014 353 360
    • (2014) Food Chem. , vol.153 , pp. 353-360
    • Suresh Kumar, K.1    Ganesan, K.2    Selvaraj, K.3    Subba Rao, P.V.4
  • 32
    • 84867080873 scopus 로고    scopus 로고
    • Effect of disulfide bond and mercapto-group on structure and function of protein and analytical method
    • Y. Tian, and J.B. Du Effect of disulfide bond and mercapto-group on structure and function of protein and analytical method J. Appl. Clin. Pediatr. 19 2007 1499 1501
    • (2007) J. Appl. Clin. Pediatr. , vol.19 , pp. 1499-1501
    • Tian, Y.1    Du, J.B.2
  • 33
    • 33847174684 scopus 로고    scopus 로고
    • Peanut protein concentrate: Production and functional properties as affected by processing
    • J.M. Yu, M. Ahmedna, and I. Goktepe Peanut protein concentrate: production and functional properties as affected by processing Food Chem. 103 2007 121 129
    • (2007) Food Chem. , vol.103 , pp. 121-129
    • Yu, J.M.1    Ahmedna, M.2    Goktepe, I.3
  • 36
    • 0000310777 scopus 로고
    • Secondary structure of globulins from plant seeds: A re-evaluation from circular dichroism measurements
    • D. Zirwer, K. Gast, H. Welfle, and K.D. Schwenke Secondary structure of globulins from plant seeds: a re-evaluation from circular dichroism measurements Int. J. Biol. Macromol. 7 1985 105 108
    • (1985) Int. J. Biol. Macromol. , vol.7 , pp. 105-108
    • Zirwer, D.1    Gast, K.2    Welfle, H.3    Schwenke, K.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.