메뉴 건너뛰기




Volumn 50, Issue 8, 2015, Pages 1284-1292

Native-state pea albumin and globulin behavior upon transglutaminase treatment

Author keywords

Cross linking degree; Microbial transglutaminase properties; Optimum parameters; Pea albumins; Pea globulins

Indexed keywords

BIOTECHNOLOGY;

EID: 84933278260     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2015.04.021     Document Type: Article
Times cited : (53)

References (56)
  • 2
    • 84907221129 scopus 로고    scopus 로고
    • Action of microbial transglutaminase (MTGase) in the modification of food proteins: A review
    • A.L.C. Gaspar, and S.P. de Goes-Favoni Action of microbial transglutaminase (MTGase) in the modification of food proteins: a review Food Chem 171 2015 315 322
    • (2015) Food Chem , vol.171 , pp. 315-322
    • Gaspar, A.L.C.1    De Goes-Favoni, S.P.2
  • 3
    • 1842408970 scopus 로고    scopus 로고
    • Production of restructured meat using microbial transglutaminase without salt or cooking
    • C. Kuraishi, J. Sakamoto, K. Yamazaki, Y. Susa, C. Kuhara, and T. Soeda Production of restructured meat using microbial transglutaminase without salt or cooking J Food Sci 62 1997 488 490
    • (1997) J Food Sci , vol.62 , pp. 488-490
    • Kuraishi, C.1    Sakamoto, J.2    Yamazaki, K.3    Susa, Y.4    Kuhara, C.5    Soeda, T.6
  • 5
    • 0035021486 scopus 로고    scopus 로고
    • Influence of transglutaminase treatment on the thermoreversible gelation of gelatin
    • H. Babin, and E. Dickinson Influence of transglutaminase treatment on the thermoreversible gelation of gelatin Food Hydrocoll 15 2001 271 276
    • (2001) Food Hydrocoll , vol.15 , pp. 271-276
    • Babin, H.1    Dickinson, E.2
  • 7
    • 84933283557 scopus 로고    scopus 로고
    • Inventors; Campina Melkunie BV, assignee. Protein preparation. WO patent 0165948; 13 September
    • Bronts HM, Hendrickx AC, Mallee LF, Inventors; Campina Melkunie BV, assignee. Protein preparation. WO patent 0165948; 13 September 2001.
    • (2001)
    • Bronts, H.M.1    Hendrickx, A.C.2    Mallee, L.F.3
  • 8
    • 56449121365 scopus 로고    scopus 로고
    • Transglutaminase-induced caseinate gelation for the microencapsulation of probiotic cells
    • T. Heidebach, P. Forst, and U. Kulozik Transglutaminase-induced caseinate gelation for the microencapsulation of probiotic cells Int Dairy J 19 2009 77 84
    • (2009) Int Dairy J , vol.19 , pp. 77-84
    • Heidebach, T.1    Forst, P.2    Kulozik, U.3
  • 9
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: Impact on food applications
    • G.A.H. DeJong, and S.J. Koppelman Transglutaminase catalyzed reactions: impact on food applications J Food Sci 67 2002 2798 2806
    • (2002) J Food Sci , vol.67 , pp. 2798-2806
    • Dejong, G.A.H.1    Koppelman, S.J.2
  • 10
    • 34248180100 scopus 로고    scopus 로고
    • Texturisation and modification of vegetable proteins for food applications using microbial transglutaminase
    • M. Dube, C. Schäfer, S. Neidhart, and R. Carle Texturisation and modification of vegetable proteins for food applications using microbial transglutaminase Eur Food Res Technol 225 2007 287 299
    • (2007) Eur Food Res Technol , vol.225 , pp. 287-299
    • Dube, M.1    Schäfer, C.2    Neidhart, S.3    Carle, R.4
  • 11
    • 17144410327 scopus 로고    scopus 로고
    • Effects of grinding and thermal treatments on hydrolysis susceptibility of pea proteins (Pisum sativum L.)
    • M. Le Gall, J. Gueguen, B. Seve, and L. Quillien Effects of grinding and thermal treatments on hydrolysis susceptibility of pea proteins (Pisum sativum L.) J Agric Food Chem 53 2005 3057 3064
    • (2005) J Agric Food Chem , vol.53 , pp. 3057-3064
    • Le Gall, M.1    Gueguen, J.2    Seve, B.3    Quillien, L.4
  • 12
    • 75149128950 scopus 로고    scopus 로고
    • Pulse proteins: Processing, characterization, functional properties and applications in food and feed
    • J. Boye, F. Zare, and A. Pletch Pulse proteins: processing, characterization, functional properties and applications in food and feed Food Res Int 43 2010 414 431
    • (2010) Food Res Int , vol.43 , pp. 414-431
    • Boye, J.1    Zare, F.2    Pletch, A.3
  • 13
    • 0004068127 scopus 로고
    • Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.). I. Legumin
    • R.R.D. Croy, J.A. Gatehouse, I.M. Evans, and D. Boulter Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.). I. Legumin Planta 148 1980 49 56
    • (1980) Planta , vol.148 , pp. 49-56
    • Croy, R.R.D.1    Gatehouse, J.A.2    Evans, I.M.3    Boulter, D.4
  • 14
    • 84986782859 scopus 로고
    • Dissociation and aggregation of pea legumin induced by pH and ionic strength
    • J. Gueguen, M. Chevalier, J.B. And, and F. Schaeffer Dissociation and aggregation of pea legumin induced by pH and ionic strength J Sci Food Agric 44 1988 167 182
    • (1988) J Sci Food Agric , vol.44 , pp. 167-182
    • Gueguen, J.1    Chevalier, M.2    Schaeffer, F.3
  • 15
    • 0001863958 scopus 로고
    • Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.). II Vicilin
    • R.D. Croy, J. Gatehouse, I. Marta Evans, and D. Boulter Characterisation of the storage protein subunits synthesised in vitro by polyribosomes and RNA from developing pea (Pisum sativum L.). II Vicilin Planta 148 1980 57 63
    • (1980) Planta , vol.148 , pp. 57-63
    • Croy, R.D.1    Gatehouse, J.2    Marta Evans, I.3    Boulter, D.4
  • 16
    • 0019082050 scopus 로고
    • The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)
    • R.R. Croy, J.A. Gatehouse, M. Tyler, and D. Boulter The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.) Biochem J 191 1980 509 516
    • (1980) Biochem J , vol.191 , pp. 509-516
    • Croy, R.R.1    Gatehouse, J.A.2    Tyler, M.3    Boulter, D.4
  • 17
    • 34250242404 scopus 로고
    • The genetics of pea seed storage proteins
    • R. Casey The genetics of pea seed storage proteins Plant Foods Hum Nutr 31 1982 281 295
    • (1982) Plant Foods Hum Nutr , vol.31 , pp. 281-295
    • Casey, R.1
  • 18
    • 0021763035 scopus 로고
    • The major albumin proteins from pea (Pisum sativum L). Purification and some properties
    • R.R. Croy, M.S. Hoque, J.A. Gatehouse, and D. Boulter The major albumin proteins from pea (Pisum sativum L). Purification and some properties Biochem J 218 1984 795 803
    • (1984) Biochem J , vol.218 , pp. 795-803
    • Croy, R.R.1    Hoque, M.S.2    Gatehouse, J.A.3    Boulter, D.4
  • 19
    • 33846230450 scopus 로고    scopus 로고
    • Centrifugal partition chromatography as a tool for preparative purification of pea albumin with enhanced yields
    • S. Bérot, E. Le Goff, A. Foucault, and L. Quillien Centrifugal partition chromatography as a tool for preparative purification of pea albumin with enhanced yields J Chromatogr B 845 2007 205 209
    • (2007) J Chromatogr B , vol.845 , pp. 205-209
    • Bérot, S.1    Le Goff, E.2    Foucault, A.3    Quillien, L.4
  • 20
    • 0020134622 scopus 로고
    • Albumin proteins of eight edible grain legume species. Electrophoretic patterns and amino acid composition
    • R.S. Bhatty Albumin proteins of eight edible grain legume species. Electrophoretic patterns and amino acid composition J Agric Food Chem 30 1982 620 622
    • (1982) J Agric Food Chem , vol.30 , pp. 620-622
    • Bhatty, R.S.1
  • 21
    • 84908540846 scopus 로고    scopus 로고
    • 9 - Peas and other legume proteins
    • G.O. Phillips, P.A. Williams, Woodhead Publishing
    • S.D. Arntfield, and H.D. Maskus 9 - peas and other legume proteins G.O. Phillips, P.A. Williams, Handbook of food proteins 2011 Woodhead Publishing 233 266
    • (2011) Handbook of Food Proteins , pp. 233-266
    • Arntfield, S.D.1    Maskus, H.D.2
  • 22
    • 36148929800 scopus 로고    scopus 로고
    • Transglutaminase treatment of pea proteins: Effect on physicochemical and rheological properties of heat-induced protein gels
    • P.J. Shand, H. Ya, Z. Pietrasik, and P.K.J.P.D. Wanasundara Transglutaminase treatment of pea proteins: effect on physicochemical and rheological properties of heat-induced protein gels Food Chem 107 2008 692 699
    • (2008) Food Chem , vol.107 , pp. 692-699
    • Shand, P.J.1    Ya, H.2    Pietrasik, Z.3    Wanasundara, P.K.J.P.D.4
  • 23
    • 77957774479 scopus 로고    scopus 로고
    • Gelation properties of salt-extracted pea protein isolate catalyzed by microbial transglutaminase cross-linking
    • X.D. Sun, and S.D. Arntfield Gelation properties of salt-extracted pea protein isolate catalyzed by microbial transglutaminase cross-linking Food Hydrocoll 25 2011 25 31
    • (2011) Food Hydrocoll , vol.25 , pp. 25-31
    • Sun, X.D.1    Arntfield, S.D.2
  • 24
    • 0347469014 scopus 로고    scopus 로고
    • Large scale procedure for fractionation of albumins and globulins from pea seeds
    • I. Crévieu, S. Berot, and J. Guéguen Large scale procedure for fractionation of albumins and globulins from pea seeds Food/Nahr 40 1996 237 244
    • (1996) Food/Nahr , vol.40 , pp. 237-244
    • Crévieu, I.1    Berot, S.2    Guéguen, J.3
  • 25
    • 33751553722 scopus 로고
    • Nitrogen-to-protein conversion factor for ten cereals and six legumes or oilseeds. A reappraisal of its definition and determination. Variation according to species and to seed protein content
    • J. Mosse Nitrogen-to-protein conversion factor for ten cereals and six legumes or oilseeds. A reappraisal of its definition and determination. Variation according to species and to seed protein content J Agric Food Chem 38 1990 18 24
    • (1990) J Agric Food Chem , vol.38 , pp. 18-24
    • Mosse, J.1
  • 26
    • 79958034324 scopus 로고    scopus 로고
    • Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate
    • A.P. Adebiyi, and R.E. Aluko Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate Food Chem 128 2011 902 908
    • (2011) Food Chem , vol.128 , pp. 902-908
    • Adebiyi, A.P.1    Aluko, R.E.2
  • 27
    • 0000326990 scopus 로고
    • Transglutaminase (Guinea pig liver)
    • H. Tabor, W.C. Tabor, Academic Press New York
    • J.E. Folk Transglutaminase (Guinea pig liver) H. Tabor, W.C. Tabor, Methods in enzymology 1970 Academic Press New York 889 894
    • (1970) Methods in Enzymology , pp. 889-894
    • Folk, J.E.1
  • 28
    • 3142651429 scopus 로고    scopus 로고
    • Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme
    • A.S. Eissa, S. Bisram, and S.A. Khan Polymerization and gelation of whey protein isolates at low pH using transglutaminase enzyme J Agric Food Chem 52 2004 4456 4464
    • (2004) J Agric Food Chem , vol.52 , pp. 4456-4464
    • Eissa, A.S.1    Bisram, S.2    Khan, S.A.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0019864780 scopus 로고
    • A fluorimetric assay for available lysine in proteins
    • C.C. Goodno, H.E. Swaisgood, and G.L. Catignani A fluorimetric assay for available lysine in proteins Anal Biochem 115 1981 203 211
    • (1981) Anal Biochem , vol.115 , pp. 203-211
    • Goodno, C.C.1    Swaisgood, H.E.2    Catignani, G.L.3
  • 31
    • 0036348648 scopus 로고    scopus 로고
    • Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein
    • C. Dinnella, M.T. Gargaro, R. Rossano, and E. Monteleone Spectrophotometric assay using o-phtaldialdehyde for the determination of transglutaminase activity on casein Food Chem 78 2002 363 368
    • (2002) Food Chem , vol.78 , pp. 363-368
    • Dinnella, C.1    Gargaro, M.T.2    Rossano, R.3    Monteleone, E.4
  • 32
    • 17144368764 scopus 로고    scopus 로고
    • Identification and quantification of ε-(γ-glutamyl)-lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS)
    • C. Schafer, M. Schott, F. Brandl, S. Neidhart, and R. Carle Identification and quantification of ε-(γ-glutamyl)-lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS) J Agric Food Chem 53 2005 2830 2837
    • (2005) J Agric Food Chem , vol.53 , pp. 2830-2837
    • Schafer, C.1    Schott, M.2    Brandl, F.3    Neidhart, S.4    Carle, R.5
  • 33
    • 84986467761 scopus 로고
    • ε-(γ-Glutamyl)lysine crosslink distribution in foods as determined by improved method
    • H. Sakamoto, Y. Kumazawa, H. Kawajiri, and M. Motoki ε-(γ-Glutamyl)lysine crosslink distribution in foods as determined by improved method J Food Sci 60 1995 416 420
    • (1995) J Food Sci , vol.60 , pp. 416-420
    • Sakamoto, H.1    Kumazawa, Y.2    Kawajiri, H.3    Motoki, M.4
  • 34
    • 84986799915 scopus 로고
    • Quantitative and qualitative variability of pea (Pisum sativum L.) protein composition
    • J. Gueguen, and J. Barbot Quantitative and qualitative variability of pea (Pisum sativum L.) protein composition J Sci Food Agric 42 1988 209 224
    • (1988) J Sci Food Agric , vol.42 , pp. 209-224
    • Gueguen, J.1    Barbot, J.2
  • 35
    • 84860604080 scopus 로고    scopus 로고
    • Effect of pea proteins extraction and vicilin/legumin fractionation on the phase behavior in admixture with alginate
    • J.L. Mession, A. Assifaoui, P. Cayot, and R. Saurel Effect of pea proteins extraction and vicilin/legumin fractionation on the phase behavior in admixture with alginate Food Hydrocoll 29 2012 335 346
    • (2012) Food Hydrocoll , vol.29 , pp. 335-346
    • Mession, J.L.1    Assifaoui, A.2    Cayot, P.3    Saurel, R.4
  • 36
    • 77957016943 scopus 로고    scopus 로고
    • Functional properties of protein isolates, globulin and albumin extracted from Ginkgo biloba seeds
    • Q. Deng, L. Wang, F. Wei, B. Xie, F. Huang, and W. Huang Functional properties of protein isolates, globulin and albumin extracted from Ginkgo biloba seeds Food Chem 124 2011 1458 1465
    • (2011) Food Chem , vol.124 , pp. 1458-1465
    • Deng, Q.1    Wang, L.2    Wei, F.3    Xie, B.4    Huang, F.5    Huang, W.6
  • 37
    • 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, and E. Farnworth 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
  • 38
    • 0039392089 scopus 로고    scopus 로고
    • Emulsifying properties, surface hydrophobicity and thermal denaturation of pea protein fractions
    • Z. Cserhalmi, B. Czukor, and I. Gajzago-Schuster Emulsifying properties, surface hydrophobicity and thermal denaturation of pea protein fractions Acta Aliment 27 1998 357 363
    • (1998) Acta Aliment , vol.27 , pp. 357-363
    • Cserhalmi, Z.1    Czukor, B.2    Gajzago-Schuster, I.3
  • 39
    • 13844299405 scopus 로고    scopus 로고
    • Physicochemical properties of 2S albumins and the corresponding protein isolate from sunflower (Helianthus annuus)
    • S.G. Pérez, J.M. Vereijken, G.A. Koningsveld, H. Gruppen, and A.G.J. Voragen Physicochemical properties of 2S albumins and the corresponding protein isolate from sunflower (Helianthus annuus) J Food Sci 70 2005 C98 C103
    • (2005) J Food Sci , vol.70 , pp. C98-C103
    • Pérez, S.G.1    Vereijken, J.M.2    Koningsveld, G.A.3    Gruppen, H.4    Voragen, A.G.J.5
  • 40
    • 17444385279 scopus 로고    scopus 로고
    • On the functional properties of globulin and albumin protein fractions and flours of African locust bean (Parkia biglobossa)
    • O.S. Lawal, K.O. Adebowale, B.M. Ogunsanwo, O.A. Sosanwo, and S.A. Bankole On the functional properties of globulin and albumin protein fractions and flours of African locust bean (Parkia biglobossa) Food Chem 92 2005 681 691
    • (2005) Food Chem , vol.92 , pp. 681-691
    • Lawal, O.S.1    Adebowale, K.O.2    Ogunsanwo, B.M.3    Sosanwo, O.A.4    Bankole, S.A.5
  • 41
    • 0033933592 scopus 로고    scopus 로고
    • Soy glycinin: Influence of pH and ionic strength on solubility and molecular structure at ambient temperatures
    • C.M.M. Lakemond, H.H.J. de Jongh, M. Hessing, H. Gruppen, and A.G.J. Voragen Soy glycinin: Influence of pH and ionic strength on solubility and molecular structure at ambient temperatures J Agric Food Chem 48 2000 1985 1990
    • (2000) J Agric Food Chem , vol.48 , pp. 1985-1990
    • Lakemond, C.M.M.1    De Jongh, H.H.J.2    Hessing, M.3    Gruppen, H.4    Voragen, A.G.J.5
  • 42
    • 51249180057 scopus 로고
    • Functional properties of soy proteins
    • J. Kinsella Functional properties of soy proteins J Am Oil Chem Soc 56 1979 242 258
    • (1979) J Am Oil Chem Soc , vol.56 , pp. 242-258
    • Kinsella, J.1
  • 43
    • 0033473950 scopus 로고    scopus 로고
    • Pilot scale isolation of proteins from field peas (Pisum sativum L.) for use as food ingredients
    • S. Tian, W.S.A. Kyle, and D.M. Small Pilot scale isolation of proteins from field peas (Pisum sativum L.) for use as food ingredients Int J Food Sci Technol 34 1999 33 39
    • (1999) Int J Food Sci Technol , vol.34 , pp. 33-39
    • Tian, S.1    Kyle, W.S.A.2    Small, D.M.3
  • 44
    • 0346346394 scopus 로고    scopus 로고
    • Comparison of enzymatic properties of microbial transglutaminase from Streptomyces sp
    • Y. Umezawa, T. Ohtsuka, K. Yokoyama, and N. Nio Comparison of enzymatic properties of microbial transglutaminase from Streptomyces sp Food Sci Technol Res 8 2002 113 118
    • (2002) Food Sci Technol Res , vol.8 , pp. 113-118
    • Umezawa, Y.1    Ohtsuka, T.2    Yokoyama, K.3    Nio, N.4
  • 45
    • 77956873001 scopus 로고    scopus 로고
    • Optimization of microbial transglutaminase activity in ice cream using response surface methodology
    • P.N. Rossa, E.M.F. De Sà, V.M. Burin, and M.T. Bordignon-Luiz Optimization of microbial transglutaminase activity in ice cream using response surface methodology LWT - Food Sci Technol 44 2011 29 34
    • (2011) LWT - Food Sci Technol , vol.44 , pp. 29-34
    • Rossa, P.N.1    De Sà, E.M.F.2    Burin, V.M.3    Bordignon-Luiz, M.T.4
  • 46
    • 34147113294 scopus 로고    scopus 로고
    • Comparative study of gelation and cross-link formation during enzymatic texturisation of leguminous proteins
    • C. Schafer, C. Zacherl, K.-H. Engel, S. Neidhart, and R. Carle Comparative study of gelation and cross-link formation during enzymatic texturisation of leguminous proteins Innov Food Sci Emerg Technol 8 2007 269 278
    • (2007) Innov Food Sci Emerg Technol , vol.8 , pp. 269-278
    • Schafer, C.1    Zacherl, C.2    Engel, K.-H.3    Neidhart, S.4    Carle, R.5
  • 47
    • 0242720522 scopus 로고    scopus 로고
    • Characterisation and quantification of the reaction(s) catalysed by transglutaminase using the o-phthaldialdehyde reagent
    • J. Flanagan, and R.J. FitzGerald Characterisation and quantification of the reaction(s) catalysed by transglutaminase using the o-phthaldialdehyde reagent Food/Nahr 47 2003 207 212
    • (2003) Food/Nahr , vol.47 , pp. 207-212
    • Flanagan, J.1    Fitzgerald, R.J.2
  • 48
    • 62549155305 scopus 로고    scopus 로고
    • Assessment of crosslinking in combined crosslinked soy protein isolate gels by microbial transglutaminase and Maillard reaction
    • C.Y. Gan, L.H. Cheng, and A.M. Easa Assessment of crosslinking in combined crosslinked soy protein isolate gels by microbial transglutaminase and Maillard reaction J Food Sci 74 2009 C141 C146
    • (2009) J Food Sci , vol.74 , pp. C141-C146
    • Gan, C.Y.1    Cheng, L.H.2    Easa, A.M.3
  • 49
    • 0005536606 scopus 로고
    • Action of transglutaminase on an 11 S seed protein (pea legumin): Influence of the substrate conformation
    • C. Larre, Z.M. Kedzior, M.G. Chenu, G. Viroben, and J. Gueguen Action of transglutaminase on an 11 S seed protein (pea legumin): influence of the substrate conformation J Agric Food Chem 40 1992 1121 1126
    • (1992) J Agric Food Chem , vol.40 , pp. 1121-1126
    • Larre, C.1    Kedzior, Z.M.2    Chenu, M.G.3    Viroben, G.4    Gueguen, J.5
  • 50
    • 0027142694 scopus 로고
    • Action of transglutaminase on the constitutive polypeptides of pea legumin
    • C. Larre, M. Chiarello, S. Dudek, M. Chenu, and J. Gueguen Action of transglutaminase on the constitutive polypeptides of pea legumin J Agric Food Chem 41 1993 1816 1820
    • (1993) J Agric Food Chem , vol.41 , pp. 1816-1820
    • Larre, C.1    Chiarello, M.2    Dudek, S.3    Chenu, M.4    Gueguen, J.5
  • 51
    • 0034854587 scopus 로고    scopus 로고
    • Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense
    • G.A.H. De Jong, G. Wijngaards, H. Boumans, S.J. Koppelman, and M. Hessing Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense J Agric Food Chem 49 2001 3389 3393
    • (2001) J Agric Food Chem , vol.49 , pp. 3389-3393
    • De Jong, G.A.H.1    Wijngaards, G.2    Boumans, H.3    Koppelman, S.J.4    Hessing, M.5
  • 53
    • 0000371853 scopus 로고    scopus 로고
    • Transglutaminase cross-linked egg white protein films: Tensile properties and oxygen permeability
    • L.-T. Lim, Y. Mine, and M.A. Tung Transglutaminase cross-linked egg white protein films: tensile properties and oxygen permeability J Agric Food Chem 46 1998 4022 4029
    • (1998) J Agric Food Chem , vol.46 , pp. 4022-4029
    • Lim, L.-T.1    Mine, Y.2    Tung, M.A.3
  • 55
    • 0028139777 scopus 로고
    • Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions
    • H. Sakamoto, Y. Kumazawa, and M. Motoki Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions J Food Sci 59 1994 866 871
    • (1994) J Food Sci , vol.59 , pp. 866-871
    • Sakamoto, H.1    Kumazawa, Y.2    Motoki, M.3
  • 56
    • 0041524989 scopus 로고    scopus 로고
    • Reflections about the functional potential of legume proteins: A Review
    • K.D. Schwenke Reflections about the functional potential of legume proteins: a Review Food/Nahr 45 2001 377 381
    • (2001) Food/Nahr , vol.45 , pp. 377-381
    • Schwenke, K.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.