메뉴 건너뛰기




Volumn 72, Issue 7, 2007, Pages

The effect of transglutaminase crosslinking on the rheological characteristics of heated peanut flour dispersions

Author keywords

Amidated pectin; Peanut flour; Peanut proteins; Rheology; Transglutaminase

Indexed keywords

CROSS LINKING REAGENT; PECTIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; VEGETABLE PROTEIN;

EID: 34548475555     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1750-3841.2007.00442.x     Document Type: Article
Times cited : (20)

References (35)
  • 2
    • 0000062424 scopus 로고
    • Changes in free amino acids, carbohydrates, and proteins of maturing seeds from various peanut (Arachis-hypogaea L.) cultivars
    • Basha SMM, Cherry JP, Young CT. 1976. Changes in free amino acids, carbohydrates, and proteins of maturing seeds from various peanut (Arachis-hypogaea L.) cultivars. Cereal Chem 53 : 586 97.
    • (1976) Cereal Chem , vol.53 , pp. 586-97
    • Basha, S.M.M.1    Cherry, J.P.2    Young, C.T.3
  • 3
    • 0010476165 scopus 로고
    • Studies on the alcohol-insoluble solids of Chico III and Homestead-24 tomatoes
    • Brown FM, Stein ER. 1977. Studies on the alcohol-insoluble solids of Chico III and Homestead-24 tomatoes. J Agric Food Chem 25 : 790.
    • (1977) J Agric Food Chem , vol.25 , pp. 790
    • Brown, F.M.1    Stein, E.R.2
  • 4
    • 85022241054 scopus 로고
    • Spectrophotometric assay using o-phthaldehyde for determination of proteolysis in milk and isolated milk proteins
    • Church FC, Swaisgood HE, Catignani GL. 1983. Spectrophotometric assay using o-phthaldehyde for determination of proteolysis in milk and isolated milk proteins. J Dairy Sci 66 : 1219 27.
    • (1983) J Dairy Sci , vol.66 , pp. 1219-27
    • Church, F.C.1    Swaisgood, H.E.2    Catignani, G.L.3
  • 5
    • 34047227335 scopus 로고    scopus 로고
    • Transglutaminase polymerization of peanut proteins
    • Clare DA, Gharst G, Sanders TH. 2007. Transglutaminase polymerization of peanut proteins. J Agric Food Chem 55 : 432 8.
    • (2007) J Agric Food Chem , vol.55 , pp. 432-8
    • Clare, D.A.1    Gharst, G.2    Sanders, T.H.3
  • 6
    • 34247377289 scopus 로고    scopus 로고
    • Rheological properties of aqueous peanut flour dispersions
    • Davis JP, Gharst G, Sanders TH. 2007. Rheological properties of aqueous peanut flour dispersions. J Text Stud 38 : 253 72.
    • (2007) J Text Stud , vol.38 , pp. 253-72
    • Davis, J.P.1    Gharst, G.2    Sanders, T.H.3
  • 7
    • 33746215812 scopus 로고    scopus 로고
    • Colloid science of mixed ingredients
    • Dickinson E. 2006. Colloid science of mixed ingredients. Soft Matter 2 : 642 52.
    • (2006) Soft Matter , vol.2 , pp. 642-52
    • Dickinson, E.1
  • 8
    • 32244431731 scopus 로고    scopus 로고
    • Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme
    • Eissa AS, Kahn SA. 2006. Modulation of hydrophobic interactions in denatured whey proteins by transglutaminase enzyme. Food Hydrocolloids 20 : 543 7.
    • (2006) Food Hydrocolloids , vol.20 , pp. 543-7
    • Eissa, A.S.1    Kahn, S.A.2
  • 9
    • 33745609556 scopus 로고    scopus 로고
    • Enzymatic cross-linking of β-lactoglobulin: Conformational properties using FTR spectroscopy
    • Eissa AS, Puhl C, Kadla JF, Khan SA. 2006. Enzymatic cross-linking of β-lactoglobulin: conformational properties using FTR spectroscopy. Biomacromolecules 7 : 1707 13.
    • (2006) Biomacromolecules , vol.7 , pp. 1707-13
    • Eissa, A.S.1    Puhl, C.2    Kadla, J.F.3    Khan, S.A.4
  • 10
    • 84987299986 scopus 로고
    • Viscosity and water absorption characteristics of slurries of sunflower and soybean flours, concentrate and isolates
    • Fleming SA, Sosulski FW, Kilara A, Humbert ES. 1974. Viscosity and water absorption characteristics of slurries of sunflower and soybean flours, concentrate and isolates. J Food Sci 39 : 188 91.
    • (1974) J Food Sci , vol.39 , pp. 188-91
    • Fleming, S.A.1    Sosulski, F.W.2    Kilara, A.3    Humbert, E.S.4
  • 12
    • 0642364573 scopus 로고
    • Peanut composition - Relation to processing and utilization
    • Hoffpauir CL. 1953. Peanut composition - relation to processing and utilization. J Agric Food Chem 1 : 668 71.
    • (1953) J Agric Food Chem , vol.1 , pp. 668-71
    • Hoffpauir, C.L.1
  • 14
    • 0347361429 scopus 로고    scopus 로고
    • Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration
    • Idris WH, Babiker EE, El Tinay AH. 2003. Fractionation, solubility and functional properties of wheat bran proteins as influenced by pH and/or salt concentration. Nahrung/Food 47 (6 425 9.
    • (2003) Nahrung/Food , vol.47 , Issue.6 , pp. 425-9
    • Idris, W.H.1    Babiker, E.E.2    El Tinay, A.H.3
  • 15
    • 84986841252 scopus 로고
    • On the nature of the interaction between some polysaccharides and proteins
    • Imeson AP, Ledward DA, Mitchell JR. 1977. On the nature of the interaction between some polysaccharides and proteins. J Sci Food Agric 28 : 661 8.
    • (1977) J Sci Food Agric , vol.28 , pp. 661-8
    • Imeson, A.P.1    Ledward, D.A.2    Mitchell, J.R.3
  • 16
    • 0022343184 scopus 로고
    • Sugars decrease the thermal denaturation and aggregation of arachin
    • Kella NKD, Poola I. 1985. Sugars decrease the thermal denaturation and aggregation of arachin. J Pept Protein Res 26 : 390 9.
    • (1985) J Pept Protein Res , vol.26 , pp. 390-9
    • Kella, N.K.D.1    Poola, I.2
  • 17
    • 0037671553 scopus 로고    scopus 로고
    • Solubility and functional properties of sesame seed proteins as influenced by pH and/or salt concentration
    • Khalid EK, Babiker EE, El Tinay AH. 2003. Solubility and functional properties of sesame seed proteins as influenced by pH and/or salt concentration. Food Chem 82 : 361 6.
    • (2003) Food Chem , vol.82 , pp. 361-6
    • Khalid, E.K.1    Babiker, E.E.2    El Tinay, A.H.3
  • 18
    • 0035147357 scopus 로고    scopus 로고
    • Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world
    • Koppelman SJ, Vlooswijk RAA, Knipples LMJ, Hessing M, Knoll EF, van Reijsen FC, Bruijnzeel-Koomen CAFM. 2001. Quantification of major peanut allergens Ara h 1 and Ara h 2 in the peanut varieties Runner, Spanish, Virginia, and Valencia, bred in different parts of the world. Allergy 56 : 132 7.
    • (2001) Allergy , vol.56 , pp. 132-7
    • Koppelman, S.J.1    Vlooswijk, R.A.A.2    Knipples, L.M.J.3    Hessing, M.4    Knoll, E.F.5    Van Reijsen, F.C.6    Bruijnzeel-Koomen, C.A.F.M.7
  • 21
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: Its utilization in the food industry
    • Kuraishi C, Yamazaki K, Susa Y. 2001. Transglutaminase: its utilization in the food industry. Food Rev Int 17 (2 221 46.
    • (2001) Food Rev Int , vol.17 , Issue.2 , pp. 221-46
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 22
    • 0028275004 scopus 로고
    • Dietary fiber viscosity and amino acid digestibility, proteolytic digestive enzyme activity and digestive organ weights in growing rats
    • Larsen FM, Wilson MN, Moughan PJ. 1994. Dietary fiber viscosity and amino acid digestibility, proteolytic digestive enzyme activity and digestive organ weights in growing rats. J Food Nutr 124 : 833 41.
    • (1994) J Food Nutr , vol.124 , pp. 833-41
    • Larsen, F.M.1    Wilson, M.N.2    Moughan, P.J.3
  • 23
    • 0037464436 scopus 로고    scopus 로고
    • Preparation and mechanical properties of edible pectin-soy flour films obtained in the absence or presence of transglutaminase
    • Mariniello L, Di Pierro P, Esposito C, Sorrentino A, Masi P, Porta R. 2003. Preparation and mechanical properties of edible pectin-soy flour films obtained in the absence or presence of transglutaminase. J Biotechnol 102 : 191 8.
    • (2003) J Biotechnol , vol.102 , pp. 191-8
    • Mariniello, L.1    Di Pierro, P.2    Esposito, C.3    Sorrentino, A.4    Masi, P.5    Porta, R.6
  • 24
    • 3142537430 scopus 로고    scopus 로고
    • Effects of gum arabic, low-methoxy pectin and xylan on in vitro digestibility of peanut protein
    • Mouecoucou J, Villaume C, Sanchez C, Mejean L. 2004. Effects of gum arabic, low-methoxy pectin and xylan on in vitro digestibility of peanut protein. Food Res Int 37 : 777 83.
    • (2004) Food Res Int , vol.37 , pp. 777-83
    • Mouecoucou, J.1    Villaume, C.2    Sanchez, C.3    Mejean, L.4
  • 25
    • 0142186148 scopus 로고    scopus 로고
    • Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration
    • Ragab DM, Babiker EE, El Tinay AH. 2004. Fractionation, solubility and functional properties of cowpea (Vigna unguiculata) proteins as affected by pH and/or salt concentration. Food Chem 84 : 207 12.
    • (2004) Food Chem , vol.84 , pp. 207-12
    • Ragab, D.M.1    Babiker, E.E.2    El Tinay, A.H.3
  • 26
    • 17444376394 scopus 로고    scopus 로고
    • The effects of acidulant type on the rheological properties of beta-lactoglobulin gels and powders derived from these gels
    • Resch JJ, Daubert CR, Foegeding EA. 2005. The effects of acidulant type on the rheological properties of beta-lactoglobulin gels and powders derived from these gels. Food Hydrocoll 19 : 851 60.
    • (2005) Food Hydrocoll , vol.19 , pp. 851-60
    • Resch, J.J.1    Daubert, C.R.2    Foegeding, E.A.3
  • 27
    • 0033666883 scopus 로고    scopus 로고
    • Cross-linking casein micelles by a microbial transglutaminase. Conditions for formation of transglutaminase-induced gels
    • Schorsch C, Carrie H, Clark AH, Norton IT. 2000. Cross-linking casein micelles by a microbial transglutaminase. Conditions for formation of transglutaminase-induced gels. Int Dairy J 10 : 519 28.
    • (2000) Int Dairy J , vol.10 , pp. 519-28
    • Schorsch, C.1    Carrie, H.2    Clark, A.H.3    Norton, I.T.4
  • 29
    • 0031252090 scopus 로고    scopus 로고
    • Physical properties of directly expanded extrudates formulated from partially defatted peanut flour and different types of starch
    • Suknark K, Phillips RD, Chinnan MS. 1997. Physical properties of directly expanded extrudates formulated from partially defatted peanut flour and different types of starch. Food Res Int 30 : 575 83.
    • (1997) Food Res Int , vol.30 , pp. 575-83
    • Suknark, K.1    Phillips, R.D.2    Chinnan, M.S.3
  • 30
    • 26844437327 scopus 로고    scopus 로고
    • Formation of properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase
    • Tang CH, Wu H, Chen Z, Yang XQ. 2006. Formation of properties of glycinin-rich and β-conglycinin-rich soy protein isolate gels induced by microbial transglutaminase. Food Res Int 39 : 87 97.
    • (2006) Food Res Int , vol.39 , pp. 87-97
    • Tang, C.H.1    Wu, H.2    Chen, Z.3    Yang, X.Q.4
  • 31
    • 1542286959 scopus 로고    scopus 로고
    • Cross-linking and rheological changes of whey proteins treated with microbial transglutaminase
    • Truong VD, Clare DA, Catignani GL, Swaisgood HE. 2004. Cross-linking and rheological changes of whey proteins treated with microbial transglutaminase. J Agric Food Chem 52 : 1170 6.
    • (2004) J Agric Food Chem , vol.52 , pp. 1170-6
    • Truong, V.D.1    Clare, D.A.2    Catignani, G.L.3    Swaisgood, H.E.4
  • 32
    • 3242762842 scopus 로고    scopus 로고
    • The major peanut allergen Ara h 1 and its cleaved-off n-terminal peptide; Possible implications for peanut allergen detection
    • Wichers HJ, De Beijer T, Savelkoul HFJ, van Amerongen A. 2004. The major peanut allergen Ara h 1 and its cleaved-off n-terminal peptide; possible implications for peanut allergen detection. J Agric Food Chem 52 : 4903 7.
    • (2004) J Agric Food Chem , vol.52 , pp. 4903-7
    • Wichers, H.J.1    De Beijer, T.2    Savelkoul, H.F.J.3    Van Amerongen, A.4
  • 33
    • 0037174466 scopus 로고    scopus 로고
    • Modification of the rheological properties of whey protein isolate through the use of an immobilized microbial transglutaminase
    • Wilcox CP, Swaisgood HE. 2002. Modification of the rheological properties of whey protein isolate through the use of an immobilized microbial transglutaminase. J Agric Food Chem 50 : 5546 51.
    • (2002) J Agric Food Chem , vol.50 , pp. 5546-51
    • Wilcox, C.P.1    Swaisgood, H.E.2
  • 34
    • 0003069615 scopus 로고
    • Protein-polyelectrolytic complexes
    • In: Dublin, P.L., Bock, J., Davis, R., Schulz, D.N., Thiec, C., editors. Berlin: Springer-Verlag. p
    • Xia J, Dubin PL. 1994. Protein-polyelectrolytic complexes. In : Dublin PL, Bock J, Davis R, Schulz DN, Thiec C, editors. Macromolecular complexes in chemistry and biology. Berlin : Springer-Verlag. p 247 71.
    • (1994) Macromolecular Complexes in Chemistry and Biology. , pp. 247-71
    • Xia, J.1    Dubin, P.L.2
  • 35
    • 0029608871 scopus 로고
    • Microbial transglutaminase - A review of its production and application in food processing
    • Zhu Y, Rinzema A, Tramper J, Bol J. 1995. Microbial transglutaminase - a review of its production and application in food processing. Appl Microbiol Biotechnol 44 : 277 82.
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 277-82
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.