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Volumn 85, Issue 15, 2005, Pages 2587-2594

Quality of dried white salted noodles affected by microbial transglutaminase

Author keywords

Dried white salted noodles; Microbial transglutaminase (MTGase); Rheological properties; Scanning electron microscopy (SEM); Textural properties

Indexed keywords

TRITICUM AESTIVUM;

EID: 29844457552     PISSN: 00225142     EISSN: None     Source Type: Journal    
DOI: 10.1002/jsfa.2311     Document Type: Article
Times cited : (82)

References (40)
  • 1
    • 0015777139 scopus 로고
    • Molecular and catalytic properties of transglutaminase
    • Folk JE and Chung SI, Molecular and catalytic properties of transglutaminase. Adv Enzymol 38:109-191 (1973).
    • (1973) Adv Enzymol , vol.38 , pp. 109-191
    • Folk, J.E.1    Chung, S.I.2
  • 2
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • Yokoyama K, Nio N and Kikuchi Y, Properties and applications of microbial transglutaminase. Appl Microbiol Biot 64:447-454 (2004).
    • (2004) Appl Microbiol Biot , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 3
    • 0031690193 scopus 로고    scopus 로고
    • Transglutaminase and its use for food processing
    • Motoki M and Seguro K, Transglutaminase and its use for food processing. Trends Food Sci Technol 9:204-210 (1998).
    • (1998) Trends Food Sci Technol , vol.9 , pp. 204-210
    • Motoki, M.1    Seguro, K.2
  • 4
    • 0000633489 scopus 로고    scopus 로고
    • Recent trends in transglutaminase technology for food processing
    • Motoki M and Kumazawa Y, Recent trends in transglutaminase technology for food processing. Food Sci Technol Res 6:151-160 (2000).
    • (2000) Food Sci Technol Res , vol.6 , pp. 151-160
    • Motoki, M.1    Kumazawa, Y.2
  • 6
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: Its utilization in the food industry
    • Kuraishi C, Yamazaki K and Susa Y, Transglutaminase: its utilization in the food industry. Food Rev Int 17:221-246 (2001).
    • (2001) Food Rev Int , vol.17 , pp. 221-246
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 7
    • 29844443500 scopus 로고    scopus 로고
    • Novel transglutaminase manufacture for preparation of protein gelling compounds. Japan Patent 0 127 471 (1989)
    • Motoki M, Okiyama A, Nonaka M, Tanaka H, Uchio R, Matsuura A, Ando H and Umeda K, Novel transglutaminase manufacture for preparation of protein gelling compounds. Japan Patent 0 127 471 (1989).
    • Motoki, M.1    Okiyama, A.2    Nonaka, M.3    Tanaka, H.4    Uchio, R.5    Matsuura, A.6    Ando, H.7    Umeda, K.8
  • 9
    • 0029608871 scopus 로고
    • Microbial transglutaminase - A review of its production and application in food processing
    • Zhu Y, Rinzema A, Tramper J and Bol J, Microbial transglutaminase - a review of its production and application in food processing. Appl Microbial Biotechnol 44:277-282 (1995).
    • (1995) Appl Microbial Biotechnol , vol.44 , pp. 277-282
    • Zhu, Y.1    Rinzema, A.2    Tramper, J.3    Bol, J.4
  • 10
    • 0036236205 scopus 로고    scopus 로고
    • Transglutaminase in baking applications
    • Poza OD, Transglutaminase in baking applications. Cereal Foods World 47:93-95 (2002).
    • (2002) Cereal Foods World , vol.47 , pp. 93-95
    • Poza, O.D.1
  • 11
    • 0036813333 scopus 로고    scopus 로고
    • Transglutaminase catalyzed reactions: Impact on food applications
    • de Jong GAH and Koppelman SJ, Transglutaminase catalyzed reactions: impact on food applications. J Food Sci 67:2798-2806 (2002).
    • (2002) J Food Sci , vol.67 , pp. 2798-2806
    • De Jong, G.A.H.1    Koppelman, S.J.2
  • 13
    • 0007383003 scopus 로고
    • The world of ingredients
    • Losche IK, The world of ingredients. Enzymes in Baking May-June: 22-25 (1995).
    • (1995) Enzymes in Baking , vol.MAY-JUNE , pp. 22-25
    • Losche, I.K.1
  • 14
    • 0031832353 scopus 로고    scopus 로고
    • Dough properties and crumb strength of white pan bread as affected by microbial transglutaminase
    • Gerrard JA, Fayle SE, Wilson AJ, Newberry MP, Ross M and Kavale S, Dough properties and crumb strength of white pan bread as affected by microbial transglutaminase. J Food Sci 63:472-475 (1998).
    • (1998) J Food Sci , vol.63 , pp. 472-475
    • Gerrard, J.A.1    Fayle, S.E.2    Wilson, A.J.3    Newberry, M.P.4    Ross, M.5    Kavale, S.6
  • 16
    • 0034853832 scopus 로고    scopus 로고
    • Effects of microbial transglutaminase on the wheat proteins of bread and croissant dough
    • Gerrard JA, Fayle SE, Brown PA, Sutton KH, Simmons L and Rasiah I, Effects of microbial transglutaminase on the wheat proteins of bread and croissant dough. J Food Sci 66:782-786 (2001).
    • (2001) J Food Sci , vol.66 , pp. 782-786
    • Gerrard, J.A.1    Fayle, S.E.2    Brown, P.A.3    Sutton, K.H.4    Simmons, L.5    Rasiah, I.6
  • 17
    • 0036221891 scopus 로고    scopus 로고
    • Physicochemical properties of wheat flour dough modified by microbial transglutaminase
    • Tseng CS and Lai HM, Physicochemical properties of wheat flour dough modified by microbial transglutaminase. J Food Sci 67:750-755 (2002).
    • (2002) J Food Sci , vol.67 , pp. 750-755
    • Tseng, C.S.1    Lai, H.M.2
  • 19
    • 0242525781 scopus 로고    scopus 로고
    • Identification of wheat protein components involved in polymer formation on incubation with transglutaminase
    • Mujoo R and Ng PKW, Identification of wheat protein components involved in polymer formation on incubation with transglutaminase. Cereal Chem 80:703-776 (2003).
    • (2003) Cereal Chem , vol.80 , pp. 703-776
    • Mujoo, R.1    Ng, P.K.W.2
  • 20
    • 0242575228 scopus 로고    scopus 로고
    • Studies on effects of microbial transglutaminase on gluten proteins of wheat. I. Biochemical analysis
    • Bauer N, Koehler P, Wieser H and Schieberle P, Studies on effects of microbial transglutaminase on gluten proteins of wheat. I. Biochemical analysis. Cereal Chem 80:781-786 (2003).
    • (2003) Cereal Chem , vol.80 , pp. 781-786
    • Bauer, N.1    Koehler, P.2    Wieser, H.3    Schieberle, P.4
  • 21
    • 0242610504 scopus 로고    scopus 로고
    • Studies on effects of microbial transglutaminase on gluten proteins of wheat. II. Rheological properties
    • Bauer N, Koehler P, Wieser H and Schieberle P, Studies on effects of microbial transglutaminase on gluten proteins of wheat. II. Rheological properties. Cereal Chem 80:787-790 (2003).
    • (2003) Cereal Chem , vol.80 , pp. 787-790
    • Bauer, N.1    Koehler, P.2    Wieser, H.3    Schieberle, P.4
  • 22
    • 0004698272 scopus 로고    scopus 로고
    • Wheat products 1. Noodles
    • ed by Ang C, Liu KS and Huang YW. Technomic, Lancaster, PA
    • Corke H and Bhattacharya M, Wheat products 1. Noodles, in Asian Foods and Beverages, ed by Ang C, Liu KS and Huang YW. Technomic, Lancaster, PA, pp. 43-71 (1999).
    • (1999) Asian Foods and Beverages , pp. 43-71
    • Corke, H.1    Bhattacharya, M.2
  • 23
    • 29844432939 scopus 로고
    • The People's Republic of China
    • Chinese Ministry of Commerce. Dried Noodle Standard (SB/T 10 068-92). The People's Republic of China (1992).
    • (1992) Dried Noodle Standard (SB/T 10 068-92)
  • 24
    • 0038804058 scopus 로고    scopus 로고
    • China - The world's largest consumer of paste products
    • ed by Kruger JE, Matsuo RB and Dick JW. American Association of Cereal Chemists, St Paul, MN
    • Huang SD, China - the world's largest consumer of paste products, in Pasta and Noodle Technology, ed by Kruger JE, Matsuo RB and Dick JW. American Association of Cereal Chemists, St Paul, MN, pp. 301-325 (1996).
    • (1996) Pasta and Noodle Technology , pp. 301-325
    • Huang, S.D.1
  • 25
    • 0001764929 scopus 로고
    • Noodles. I. Measuring the textural characteristics of cooked noodles
    • Oh NH, Seib PA, Deyoe CW and Ward AB, Noodles. I. Measuring the textural characteristics of cooked noodles. Cereal Chem 60:433-438 (1983).
    • (1983) Cereal Chem , vol.60 , pp. 433-438
    • Oh, N.H.1    Seib, P.A.2    Deyoe, C.W.3    Ward, A.B.4
  • 26
    • 0001023989 scopus 로고
    • Noodles. II. The surface firmness of cooked noodles from soft and hard wheat flours
    • Oh NH, Seib PA, Deyoe CW and Ward AB, Noodles. II. The surface firmness of cooked noodles from soft and hard wheat flours. Cereal Chem 62:431-436 (1985).
    • (1985) Cereal Chem , vol.62 , pp. 431-436
    • Oh, N.H.1    Seib, P.A.2    Deyoe, C.W.3    Ward, A.B.4
  • 27
    • 0003859691 scopus 로고    scopus 로고
    • 44-15A approved October 1975, revised October 1981; 46-11A approved October 1976, revised October 1985; 76-13 approved November 1995; 76-31 approved January 1995; 30-25 approved April 1961, revised October 1991; 54-40A approved November 1995; 08-01 approved April 1961, revised October 1981. AACC, St Paul, MN, USA
    • AACC, Approved Methods of the American Association of Cereal Chemistry, 10th edn; 44-15A approved October 1975, revised October 1981; 46-11A approved October 1976, revised October 1985; 76-13 approved November 1995; 76-31 approved January 1995; 30-25 approved April 1961, revised October 1991; 54-40A approved November 1995; 08-01 approved April 1961, revised October 1981. AACC, St Paul, MN, USA, (2000).
    • (2000) Approved Methods of the American Association of Cereal Chemistry, 10th Edn
  • 28
    • 0002653224 scopus 로고
    • A modified screening test for rapid estimation of gluten strength in early-generation durum wheat breeding lines
    • Dick JW and Quick JS, A modified screening test for rapid estimation of gluten strength in early-generation durum wheat breeding lines. Cereal Chem 60:315-318 (1983).
    • (1983) Cereal Chem , vol.60 , pp. 315-318
    • Dick, J.W.1    Quick, J.S.2
  • 29
    • 0030826494 scopus 로고    scopus 로고
    • Contribution of wheat flour fractions to peak hot pasting viscosity
    • Morris CE, King GE and Rubenthaler GL, Contribution of wheat flour fractions to peak hot pasting viscosity. Cereal Chem 74:147-153 (1997).
    • (1997) Cereal Chem , vol.74 , pp. 147-153
    • Morris, C.E.1    King, G.E.2    Rubenthaler, G.L.3
  • 30
    • 0030044861 scopus 로고    scopus 로고
    • Enhanced susceptibility to transglutaminase reaction of alpha-lactabumin in the molten state
    • Matsumura Y, Chanyongvorakui Y, Kumazawa Y, Ohtsuka T and Mori T, Enhanced susceptibility to transglutaminase reaction of alpha-lactabumin in the molten state. Biochim Biophys Acta 1292:69-76 (1996).
    • (1996) Biochim Biophys Acta , vol.1292 , pp. 69-76
    • Matsumura, Y.1    Chanyongvorakui, Y.2    Kumazawa, Y.3    Ohtsuka, T.4    Mori, T.5
  • 31
    • 0030868670 scopus 로고    scopus 로고
    • Diversity of starch pasting properties in Iranian hexaploid wheat landraces
    • Bhattacharya M, Jafari-Shabestrari J, Qualset C and Corke H, Diversity of starch pasting properties in Iranian hexaploid wheat landraces. Cereal Chem 74:417-423 (1997).
    • (1997) Cereal Chem , vol.74 , pp. 417-423
    • Bhattacharya, M.1    Jafari-Shabestrari, J.2    Qualset, C.3    Corke, H.4
  • 33
    • 0030728262 scopus 로고    scopus 로고
    • Physicochemical properties of Australian flours influencing the texture of yellow alkaline noodles
    • Ross AS, Quail KJ and Crosbie GB, Physicochemical properties of Australian flours influencing the texture of yellow alkaline noodles. Cereal Chem 74:814-820 (1997).
    • (1997) Cereal Chem , vol.74 , pp. 814-820
    • Ross, A.S.1    Quail, K.J.2    Crosbie, G.B.3
  • 35
    • 0000058286 scopus 로고
    • A mechanism of bread firming. II. Role of starch hydrolyzing enzymes
    • Martin ML and Hoseney RC, A mechanism of bread firming. II. Role of starch hydrolyzing enzymes. Cereal Chem 68:503-507 (1991).
    • (1991) Cereal Chem , vol.68 , pp. 503-507
    • Martin, M.L.1    Hoseney, R.C.2
  • 36
    • 0742323261 scopus 로고    scopus 로고
    • Effect of various dextrin substitutions for wheat flour on dough properties and bead qualities
    • Miyazaki M, Maeda T and Morita N, Effect of various dextrin substitutions for wheat flour on dough properties and bead qualities. Food Res Int 37:59-65 (2004).
    • (2004) Food Res Int , vol.37 , pp. 59-65
    • Miyazaki, M.1    Maeda, T.2    Morita, N.3
  • 37
    • 0033008701 scopus 로고    scopus 로고
    • Impact of maltodextrins and antistaling enzymes on the differential scanning calorimetry staling endotherm of baked bread doughs
    • Defloor I and Delcour J, Impact of maltodextrins and antistaling enzymes on the differential scanning calorimetry staling endotherm of baked bread doughs. J Agric Food Chem 47:737-741 (1999).
    • (1999) J Agric Food Chem , vol.47 , pp. 737-741
    • Defloor, I.1    Delcour, J.2
  • 38
    • 0035083462 scopus 로고    scopus 로고
    • Comparison of deamidase activity of transglutaminase
    • Ohtsuka T, Umezawa Y, Nio N and Kubota K, Comparison of deamidase activity of transglutaminase. J Food Sci 66:25-29 (2001).
    • (2001) J Food Sci , vol.66 , pp. 25-29
    • Ohtsuka, T.1    Umezawa, Y.2    Nio, N.3    Kubota, K.4
  • 39
    • 84986771093 scopus 로고
    • Flour components affecting paste and noodle colour
    • Miskelly DM, Flour components affecting paste and noodle colour. J Sci Food Agric 35:463-471 (1984).
    • (1984) J Sci Food Agric , vol.35 , pp. 463-471
    • Miskelly, D.M.1


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