메뉴 건너뛰기




Volumn 59, Issue 21, 2011, Pages 11621-11628

Optimization of the enzymatic deamidation of soy protein by protein-glutaminase and its effect on the functional properties of the protein

Author keywords

circular dichroism; enzyme; protein deamidation; protein functional properties; protein glutaminase; response surface methodology; soy protein

Indexed keywords

CIRCULAR DICHROISM SPECTRA; DEAMIDATED; DEAMIDATION; EMULSIFYING PROPERTY; FUNCTIONAL PROPERTIES; HELIX STRUCTURES; LOW DEGREE; NEUTRAL CONDITIONS; OPTIMAL CONDITIONS; PROTEIN-GLUTAMINASE; RESPONSE SURFACE METHODOLOGY; SDS-PAGE; SHEET STRUCTURE; SOY PROTEIN; SOY PROTEIN ISOLATES;

EID: 80455173785     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf2028973     Document Type: Article
Times cited : (93)

References (36)
  • 1
    • 0028250433 scopus 로고
    • Deamidation of food proteins to improve functionality
    • Hamada, J. S. Deamidation of food proteins to improve functionality Crit. Rev. Food Sci. Nutr. 1994, 34 (3) 283-292
    • (1994) Crit. Rev. Food Sci. Nutr. , vol.34 , Issue.3 , pp. 283-292
    • Hamada, J.S.1
  • 2
    • 84985224923 scopus 로고
    • Preparation and functional properties of enzymatically deamidated soy proteins
    • Hamada, J. S.; Marshall, W. E. Preparation and functional properties of enzymatically deamidated soy proteins J. Food Sci. 1989, 54 (598-601) 635
    • (1989) J. Food Sci. , vol.54 , Issue.598-601 , pp. 635
    • Hamada, J.S.1    Marshall, W.E.2
  • 3
    • 0035079176 scopus 로고    scopus 로고
    • Protein-glutaminase from Cryseobacterium proteolyticum, an enzyme that deamidates glutamyl residues in proteins. Purification, characterization and gene cloning
    • Yamaguchi, S.; Jeenes, D. J.; Archer, D. B. Protein-glutaminase from Cryseobacterium proteolyticum, an enzyme that deamidates glutamyl residues in proteins. Purification, characterization and gene cloning Eur. J. Biochem. 2001, 268, 1410-1421
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1410-1421
    • Yamaguchi, S.1    Jeenes, D.J.2    Archer, D.B.3
  • 4
    • 0033855441 scopus 로고    scopus 로고
    • A novel protein-deamidating enzyme from Cryseobacterium proteolyticum sp. nov., a newly isolated bacterium from soil
    • Yamaguchi, S.; Yokoe, M. A novel protein-deamidating enzyme from Cryseobacterium proteolyticum sp. nov., a newly isolated bacterium from soil Appl. Environ. Microbiol. 2000, 66, 3337-3343
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3337-3343
    • Yamaguchi, S.1    Yokoe, M.2
  • 5
    • 0035543058 scopus 로고    scopus 로고
    • Action of protein-glutaminase on a-lactalbumin in the native and molten globule states
    • Gu, Y. S.; Matsumura, Y.; Yamaguchi, S.; Mori, T. Action of protein-glutaminase on a-lactalbumin in the native and molten globule states J. Agric. Food Chem. 2001, 49, 5999-6005
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 5999-6005
    • Gu, Y.S.1    Matsumura, Y.2    Yamaguchi, S.3    Mori, T.4
  • 6
    • 8544266059 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of α-zein
    • Yong, Y. H.; Yamaguchi, S.; Gu, Y. S.; Mori, T.; Matsumura, Y. Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of α-zein J. Agric. Food Chem. 2004, 52, 7094-7100
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 7094-7100
    • Yong, Y.H.1    Yamaguchi, S.2    Gu, Y.S.3    Mori, T.4    Matsumura, Y.5
  • 7
    • 33748437518 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten
    • Yong, Y. H.; Yamaguchi, S.; Matsumura, Y. Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten J. Agric. Food Chem. 2006, 54, 6034-6040
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 6034-6040
    • Yong, Y.H.1    Yamaguchi, S.2    Matsumura, Y.3
  • 8
    • 77950340810 scopus 로고    scopus 로고
    • Effect of deamidation by protein-glutaminase on physicochemical and functional properties of skim milk
    • Miwa, N.; Yokoyama, K.; Wakabayashi, H.; Nio, N. Effect of deamidation by protein-glutaminase on physicochemical and functional properties of skim milk Int. Dairy J. 2010, 20, 393-399
    • (2010) Int. Dairy J. , vol.20 , pp. 393-399
    • Miwa, N.1    Yokoyama, K.2    Wakabayashi, H.3    Nio, N.4
  • 9
    • 0003737812 scopus 로고
    • Elsevier Applied Science Publishers Ltd. London, England
    • Adler-Nissen, J. Enzymic hydrolysis of food proteins; Elsevier Applied Science Publishers Ltd.: London, England, 1986; 427 pp.
    • (1986) Enzymic Hydrolysis of Food Proteins , pp. 427
    • Adler-Nissen, J.1
  • 10
    • 0028526562 scopus 로고
    • Enzymatic production of protein hydrolysatess for food use. Choice of materials, processing methods, and quality control are key aspects of the hydrolysis process
    • Lahl, W. J.; Braun, S. Enzymatic production of protein hydrolysatess for food use. Choice of materials, processing methods, and quality control are key aspects of the hydrolysis process Food Technol. 1994, 48 (10) 68-71
    • (1994) Food Technol. , vol.48 , Issue.10 , pp. 68-71
    • Lahl, W.J.1    Braun, S.2
  • 11
    • 0242666847 scopus 로고    scopus 로고
    • Response surface methods and other approaches to process optimization
    • 4 th ed. John Wiley & Sons, Inc. New York, NY
    • Montgomery, D. C. Response surface methods and other approaches to process optimization. In Design and Analysis of Experiments, 4 th ed.; John Wiley & Sons, Inc.: New York, NY, 1996; pp 575-651.
    • (1996) Design and Analysis of Experiments , pp. 575-651
    • Montgomery, D.C.1
  • 12
    • 0002510086 scopus 로고
    • Enzymatic hydrolysis of crayfish processing by-products
    • Baek, H. H.; Cadwallader, K. R. Enzymatic hydrolysis of crayfish processing by-products J. Food Sci. 1995, 60, 929-935
    • (1995) J. Food Sci. , vol.60 , pp. 929-935
    • Baek, H.H.1    Cadwallader, K.R.2
  • 13
    • 18844397356 scopus 로고    scopus 로고
    • Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases
    • Nilsang, S.; Lertsiri, S.; Suphantharika, M.; Assavanig, A. Optimization of enzymatic hydrolysis of fish soluble concentrate by commercial proteases J. Food Eng. 2005, 70, 571-578
    • (2005) J. Food Eng. , vol.70 , pp. 571-578
    • Nilsang, S.1    Lertsiri, S.2    Suphantharika, M.3    Assavanig, A.4
  • 14
    • 44949183612 scopus 로고    scopus 로고
    • Optimization of the enzymatic hydrolysis of chicken meat using response surface methodology
    • Kurozawa, L. E.; Park, K. J.; Hubinger, M. D. Optimization of the enzymatic hydrolysis of chicken meat using response surface methodology J. Food Sci. 2008, 73 (5) C405-C412
    • (2008) J. Food Sci. , vol.73 , Issue.5
    • Kurozawa, L.E.1    Park, K.J.2    Hubinger, M.D.3
  • 15
    • 74249096679 scopus 로고    scopus 로고
    • Optimization of the enzymatic hydrolysis of mussel meat
    • Silva, V. M.; Park, K. J.; Hubinger, M. D. Optimization of the enzymatic hydrolysis of mussel meat J. Food Sci. 2010, 75 (1) C36-C42
    • (2010) J. Food Sci. , vol.75 , Issue.1
    • Silva, V.M.1    Park, K.J.2    Hubinger, M.D.3
  • 16
    • 79956119286 scopus 로고
    • A modified preparation of the universal buffer described by Teorell and Stenhagen
    • Östling, S.; Virtama, P. A modified preparation of the universal buffer described by Teorell and Stenhagen Acta Physiol. Scand. 1946, 11 (4) 289-293
    • (1946) Acta Physiol. Scand. , vol.11 , Issue.4 , pp. 289-293
    • Östling, S.1    Virtama, P.2
  • 17
    • 34047236353 scopus 로고    scopus 로고
    • Effect of alkaline deamidation on the structure, surface hydrophobicity, and emulsifying properties of the z19 α-zein
    • Cabra, V.; Arreguin, R.; Vazquez-Duhalt, R.; Farres, A. Effect of alkaline deamidation on the structure, surface hydrophobicity, and emulsifying properties of the z19 α-zein J. Agric. Food Chem. 2007, 55, 439-445
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 439-445
    • Cabra, V.1    Arreguin, R.2    Vazquez-Duhalt, R.3    Farres, A.4
  • 18
    • 58149522343 scopus 로고    scopus 로고
    • Isolation, purification and characterisation of lunasin from defatted soybean flour and in vitro evaluation of its anti-inflammatory activity
    • Dia, V. P.; Wang, W.; Oh, V. L.; de Lumen, B. O.; de Mejia, E. G. Isolation, purification and characterisation of lunasin from defatted soybean flour and in vitro evaluation of its anti-inflammatory activity Food Chem. 2009, 114 (1) 108-115
    • (2009) Food Chem. , vol.114 , Issue.1 , pp. 108-115
    • Dia, V.P.1    Wang, W.2    Oh, V.L.3    De Lumen, B.O.4    De Mejia, E.G.5
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Leammli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227 (5259) 680-685
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Leammli, U.K.1
  • 20
  • 21
    • 0037677275 scopus 로고    scopus 로고
    • Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: A new scaling method
    • Raussens, V.; Ruysschaert, J. -M.; Goormaghtigh, E. Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method Anal. Biochem. 2003, 319, 114-121
    • (2003) Anal. Biochem. , vol.319 , pp. 114-121
    • Raussens, V.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 23
    • 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 J. Agric. Food Chem. 1978, 26, 716-723
    • (1978) J. Agric. Food Chem. , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 24
    • 33646364376 scopus 로고    scopus 로고
    • Composition and functional properties of soy protein isolates prepared using alternative defatting and extraction procedures
    • L'Hocine, L.; Boye, J. I.; Arcand, Y. Composition and functional properties of soy protein isolates prepared using alternative defatting and extraction procedures J. Food Sci. 2006, 71 (3) C137-C145
    • (2006) J. Food Sci. , vol.71 , Issue.3
    • L'Hocine, L.1    Boye, J.I.2    Arcand, Y.3
  • 25
    • 70450173061 scopus 로고    scopus 로고
    • Optimization of enzymatic hydrolysis of defatted sesame flour by deifferent proteases and their effect on the functional properties of the resulting protein hydrolysate
    • Kanu, P. J.; Kanu, J. B.; Sandy, E. H.; Kandeh, J. B. A.; Mornya, P. M. P.; Huiming, Z. Optimization of enzymatic hydrolysis of defatted sesame flour by deifferent proteases and their effect on the functional properties of the resulting protein hydrolysate Am. J. Food Technol. 2009, 4 (6) 226-240
    • (2009) Am. J. Food Technol. , vol.4 , Issue.6 , pp. 226-240
    • Kanu, P.J.1    Kanu, J.B.2    Sandy, E.H.3    Kandeh, J.B.A.4    Mornya, P.M.P.5    Huiming, Z.6
  • 26
    • 0000058708 scopus 로고
    • Effect of pH on rates of enzyme-catalyzed reactions
    • 2 nd ed. Marcel Dekker, Inc. New York, NY
    • Whitaker, J. R. Effect of pH on rates of enzyme-catalyzed reactions. In Principles of Enzymology for the Food Sciences, 2 nd ed.; Marcel Dekker, Inc.: New York, NY, 1994; pp 271-300.
    • (1994) Principles of Enzymology for the Food Sciences , pp. 271-300
    • Whitaker, J.R.1
  • 27
    • 0000058708 scopus 로고
    • Effect of substrate concentration on rates of enzyme-catalyzed reactions
    • 2 nd ed. Marcel Dekker, Inc. New York, NY
    • Whitaker, J. R. Effect of substrate concentration on rates of enzyme-catalyzed reactions. In Principles of Enzymology for the Food Sciences, 2 nd ed.; Marcel Dekker, Inc.: New York, NY, 1994; pp 167-199.
    • (1994) Principles of Enzymology for the Food Sciences , pp. 167-199
    • Whitaker, J.R.1
  • 28
    • 33846688056 scopus 로고    scopus 로고
    • Optimization of extraction and isolation for 11s and 7s globulins of soybean seed storage protein
    • Liu, C.; Wang, H.; Cui, Z.; He, X.; Wang, X.; Zeng, X.; Ma, H. Optimization of extraction and isolation for 11s and 7s globulins of soybean seed storage protein Food Chem. 2007, 102, 1310-1316
    • (2007) Food Chem. , vol.102 , pp. 1310-1316
    • Liu, C.1    Wang, H.2    Cui, Z.3    He, X.4    Wang, X.5    Zeng, X.6    Ma, H.7
  • 30
    • 0001042101 scopus 로고    scopus 로고
    • Amino acids, peptides, and proteins
    • 3 rd ed. Fennema, O. R. CRC Press: Boca Raton, FL
    • Damodaran, S. Amino acids, peptides, and proteins. In Food Chemistry, 3 rd ed.; Fennema, O. R., Ed.; CRC Press: Boca Raton, FL, 1996; pp 321-429.
    • (1996) Food Chemistry , pp. 321-429
    • Damodaran, S.1
  • 31
    • 0035247893 scopus 로고    scopus 로고
    • Functional properties of hydrothermally cooked soy protein products
    • Wang, C.; Johnson, L. A. Functional properties of hydrothermally cooked soy protein products J. Am. Oil Chem. Soc. 2001, 78 (2) 189-195
    • (2001) J. Am. Oil Chem. Soc. , vol.78 , Issue.2 , pp. 189-195
    • Wang, C.1    Johnson, L.A.2
  • 32
    • 0025475008 scopus 로고
    • Functional and nutritional properties of acylated rapeseed proteins
    • Ponnampalam, R.; Delisle, J.; Gagne, Y.; Amiot, J. Functional and nutritional properties of acylated rapeseed proteins J. Am. Oil Chem. Soc. 1990, 67 (8) 531-535
    • (1990) J. Am. Oil Chem. Soc. , vol.67 , Issue.8 , pp. 531-535
    • Ponnampalam, R.1    Delisle, J.2    Gagne, Y.3    Amiot, J.4
  • 33
    • 58149498555 scopus 로고    scopus 로고
    • Effects of succinylation and deamidation on functional properties of oat protein isolate
    • Mirmoghtadaie, L.; Kadivar, M.; Shahedi, M. Effects of succinylation and deamidation on functional properties of oat protein isolate Food Chem. 2009, 114, 127-131
    • (2009) Food Chem. , vol.114 , pp. 127-131
    • Mirmoghtadaie, L.1    Kadivar, M.2    Shahedi, M.3
  • 34
    • 0030127886 scopus 로고    scopus 로고
    • Enhancing the functionality of food proteins by enzymatic modification
    • Panyam, D.; Kilara, A. Enhancing the functionality of food proteins by enzymatic modification Trends Food Sci. Technol. 1996, 7, 120-125
    • (1996) Trends Food Sci. Technol. , vol.7 , pp. 120-125
    • Panyam, D.1    Kilara, A.2
  • 36
    • 0032850080 scopus 로고    scopus 로고
    • Acid modification of proteins from soymilk residue (okara)
    • Chan, W.-M.; Ma, C.-Y. Acid modification of proteins from soymilk residue (okara) Food Res. Int. 1999, 32, 119-127
    • (1999) Food Res. Int. , vol.32 , pp. 119-127
    • Chan, W.-M.1    Ma, C.-Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.