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Volumn 690 693, Issue , 2013, Pages 1327-1330

Emulsifying and foaming properties of wheat gluten influenced by high pressure microfluidization

Author keywords

Emulsifying properties; Foaming properties; Microfluidization; Wheat gluten

Indexed keywords

DYNAMIC HIGH PRESSURE MICROFLUIDIZATION (DHPM); EMULSIFYING PROPERTY; FOAMING CAPACITIES; FOAMING PROPERTIES; FOOD PROCESSING INDUSTRY; HIGH PRESSURE MICROFLUIDIZATION; MICROFLUIDIZATION; WHEAT GLUTEN;

EID: 84878662728     PISSN: 10226680     EISSN: None     Source Type: Book Series    
DOI: 10.4028/www.scientific.net/AMR.690-693.1327     Document Type: Conference Paper
Times cited : (4)

References (9)
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    • Liao, L.1    Liu, T.2    Zhao, M.3    Cui, C.4    Yuan, B.5    Tang, S.6    Yang, F.7
  • 2
    • 33744521246 scopus 로고    scopus 로고
    • Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration
    • Wang, J., Zhao, M., Yang, X., & Jiang, Y. Improvement on functional properties of wheat gluten by enzymatic hydrolysis and ultrafiltration. Journal of Cereal Science, 44, 93-100. (2006)
    • (2006) Journal of Cereal Science , vol.44 , pp. 93-100
    • Wang, J.1    Zhao, M.2    Yang, X.3    Jiang, Y.4
  • 3
    • 65249156463 scopus 로고    scopus 로고
    • Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing
    • Dissanayake, M., & Vasiljevic, T. Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. Journal of Dairy Science, 92, 1387-1397. (2009)
    • (2009) Journal of Dairy Science , vol.92 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 4
    • 80051713269 scopus 로고    scopus 로고
    • Effects of microfluidization treatment and transglutatminase cross-linking on physiochemical, functional, and conformational properties of peanut protein isolate
    • Hu, X., Zhao, M., Sun, W., Zhao, G., & Ren, J. Effects of microfluidization treatment and transglutatminase cross-linking on physiochemical, functional, and conformational properties of peanut protein isolate. Journal of Agricultural and Food Chemistry, 59, 8886-8894. (2011)
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , pp. 8886-8894
    • Hu, X.1    Zhao, M.2    Sun, W.3    Zhao, G.4    Ren, J.5
  • 5
    • 34547791761 scopus 로고    scopus 로고
    • The influence of changes in gluten complex structure on technological quality of wheat (Triticum aestivum L.)
    • A. Torbica, M. Antov, J. Mastilović, D. Knežević. The influence of changes in gluten complex structure on technological quality of wheat (Triticum aestivum L.).Food Research International, 40,1038-1045. (2007)
    • (2007) Food Research International , vol.40 , pp. 1038-1045
    • Torbica, A.1    Antov, M.2    Mastilović, J.3    Knežević, D.4
  • 7
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce, K. N., & Kinsella, J. E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry, 26, 716-723. (1978)
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 9
    • 85052696733 scopus 로고    scopus 로고
    • Functionality of protein hydrolysates
    • In A. Paraf & S. Damodaran (Eds.), New York: Marcel Dekker
    • Nielsen, P. M. Functionality of protein hydrolysates. In A. Paraf & S. Damodaran (Eds.), Food proteins and their applications (pp. 443-472). New York: Marcel Dekker. (1997)
    • (1997) Food Proteins and Their Applications , pp. 443-472
    • Nielsen, P.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.