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Volumn 52, Issue 23, 2004, Pages 7094-7100

Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of α-zein

Author keywords

Zein; Antioxidation; Deamidation; Emulsification; Protein glutaminase; Secondary structure; Solubility

Indexed keywords

ALCOHOL; GLUTAMINASE; PEROXIDE; POTASSIUM DIHYDROGEN PHOSPHATE; ZEIN;

EID: 8544266059     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf040133u     Document Type: Article
Times cited : (94)

References (37)
  • 2
    • 0034824517 scopus 로고    scopus 로고
    • Zein: The industrial protein from corn
    • Shukla, R.; Cheryan, M. Zein: the industrial protein from corn. Ind. Crops Prod. 2001, 13, 171-192.
    • (2001) Ind. Crops Prod. , vol.13 , pp. 171-192
    • Shukla, R.1    Cheryan, M.2
  • 3
    • 84986465411 scopus 로고
    • Enzymatically and chemically modified zein for improvement of functional properties
    • Cassella, M. L. A.; Whitaker, J. R. Enzymatically and chemically modified zein for improvement of functional properties. J. Food Biochem. 1990, 14, 453-475.
    • (1990) J. Food Biochem. , vol.14 , pp. 453-475
    • Cassella, M.L.A.1    Whitaker, J.R.2
  • 6
    • 84963187703 scopus 로고
    • Functional properties of proteins in foods: A survey
    • Kinsella, J. E. Functional properties of proteins in foods: A survey. CRC Crit. Rev. Food Sci. Nutr. 1976, 7, 219-280.
    • (1976) CRC Crit. Rev. Food Sci. Nutr. , vol.7 , pp. 219-280
    • Kinsella, J.E.1
  • 7
    • 0000522837 scopus 로고
    • Antioxidative mechanism of maize zein in powder model systems against methyl linoleate: Effect of water activity and coexistence of antioxidants
    • Wang, J. Y.; Fujimoto, K.; Miyazawa, T.; Endo, Y. Antioxidative mechanism of maize zein in powder model systems against methyl linoleate: effect of water activity and coexistence of antioxidants. J. Agric. Food Chem. 1991, 39, 51-355.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 51-355
    • Wang, J.Y.1    Fujimoto, K.2    Miyazawa, T.3    Endo, Y.4
  • 8
  • 9
    • 0013086446 scopus 로고
    • Modification of food proteins by non-enzymatic methods
    • Hudson, B. J. F., Ed.; Elsevier Applied Science: London, U.K.
    • Shih, F. F. Modification of food proteins by non-enzymatic methods. In Biochemistry of Food Proteins; Hudson, B. J. F., Ed.; Elsevier Applied Science: London, U.K., 1992: pp 235-248.
    • (1992) Biochemistry of Food Proteins , pp. 235-248
    • Shih, F.F.1
  • 10
    • 85052718156 scopus 로고    scopus 로고
    • Enzyme and chemical modification of proteins
    • Damodaran, S., Paraf, A., Eds.; Dekker. New York
    • Schwenke, K. D. Enzyme and chemical modification of proteins. In Food Proteins and Their Applications; Damodaran, S., Paraf, A., Eds.; Dekker. New York, 1997; pp 393-423.
    • (1997) Food Proteins and Their Applications , pp. 393-423
    • Schwenke, K.D.1
  • 12
    • 0003000024 scopus 로고
    • Modification of food proteins by enzymatic methods
    • Hudson, B. J. F., Ed.; Elsevier Applied Science: London, U.K.
    • Hamada, J. S. Modification of food proteins by enzymatic methods. In Biochemistry of Food Proteins; Hudson, B. J. F., Ed.; Elsevier Applied Science: London, U.K., 1992; pp 249-270.
    • (1992) Biochemistry of Food Proteins , pp. 249-270
    • Hamada, J.S.1
  • 13
    • 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, 283-292.
    • (1994) Crit. Rev. Food Sci. Nutr. , vol.34 , pp. 283-292
    • Hamada, J.S.1
  • 14
    • 0033855441 scopus 로고    scopus 로고
    • A novel protein-deamidating enzyme from Chryseobacterium proteolyticum sp. nov., a newly isolated bacterium from soil
    • Yamaguchi, S.; Yokoe, M. A novel protein-deamidating enzyme from Chryseobacterium 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
  • 15
    • 0035079176 scopus 로고    scopus 로고
    • Protein-glutaminase from Chryseobacterium proteolyticum, an enzyme that deamidates glutaminyl residues in proteins: Purification, characterization and gene cloning
    • Yamaguchi, S.; Jeenes, D. J.; Archer, D. B. Protein-glutaminase from Chryseobacterium proteolyticum, an enzyme that deamidates glutaminyl 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
  • 16
    • 0015245042 scopus 로고
    • Peptidoglutaminase. Enzymes for selective deamidation of γ-amido of peptide-bound glutamine
    • Kikuchi, M.; Hayashida, H.; Nakano, E.; Sakaguchi, K. Peptidoglutaminase. Enzymes for selective deamidation of γ-amido of peptide-bound glutamine. Biochemistry 1971, 10, 1222-1229.
    • (1971) Biochemistry , vol.10 , pp. 1222-1229
    • Kikuchi, M.1    Hayashida, H.2    Nakano, E.3    Sakaguchi, K.4
  • 17
    • 84987285063 scopus 로고
    • Deamidation of soy peptides and proteins by Bacillus circulans peptidoglutaminase
    • Hamada, J. S.; Shih, F. F.; Frank, A. W.; Marshall, W. E. Deamidation of soy peptides and proteins by Bacillus circulans peptidoglutaminase. J. Food Sci. 1988, 53, 671-672.
    • (1988) J. Food Sci. , vol.53 , pp. 671-672
    • Hamada, J.S.1    Shih, F.F.2    Frank, A.W.3    Marshall, W.E.4
  • 18
    • 0025357314 scopus 로고
    • The prolamin storage proteins of cereal seeds: Structure and evolution
    • Shewry, P. R.; Tatham, A. S. The prolamin storage proteins of cereal seeds: structure and evolution. Biochem. J. 1990, 267, 1-12.
    • (1990) Biochem. J. , vol.267 , pp. 1-12
    • Shewry, P.R.1    Tatham, A.S.2
  • 19
    • 0000587863 scopus 로고
    • A proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays L.)
    • Esen. A. A proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays L.). J. Cereal Sci. 1987, 5, 117-128.
    • (1987) J. Cereal Sci. , vol.5 , pp. 117-128
    • Esen, A.1
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0019599157 scopus 로고
    • Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours
    • Kauppinen, J. K.; Moffat, D. J.; Mantsch, H. H.; Cameron, D. G. Fourier transforms in the computation of self-deconvoluted and first-order derivative spectra of overlapped band contours. Anal. Biochem. 1981, 53, 1454-1457.
    • (1981) Anal. Biochem. , vol.53 , pp. 1454-1457
    • Kauppinen, J.K.1    Moffat, D.J.2    Mantsch, H.H.3    Cameron, D.G.4
  • 23
    • 0001368617 scopus 로고
    • Prominent antioxidant effect of wheat gliadin on linoleate peroxidation in powder model systems at high water activity
    • Iwami, K.; Hattori, M.; Ibuki, F. Prominent antioxidant effect of wheat gliadin on linoleate peroxidation in powder model systems at high water activity. J. Agric. Food Chem. 1987, 35, 628-631.
    • (1987) J. Agric. Food Chem. , vol.35 , pp. 628-631
    • Iwami, K.1    Hattori, M.2    Ibuki, F.3
  • 24
    • 0012395825 scopus 로고    scopus 로고
    • Comparison of antioxidative activity among three types of prolamin subunits
    • Kawase, S.-I.; Matsumura, Y.; Murakami, H., Mon, T. Comparison of antioxidative activity among three types of prolamin subunits. J. Cereal Sci. 1998, 28, 33-41.
    • (1998) J. Cereal Sci. , vol.28 , pp. 33-41
    • Kawase, S.-I.1    Matsumura, Y.2    Murakami, H.3    Mon, T.4
  • 25
    • 0000876432 scopus 로고
    • Acid deamidation and enzymatic modification at pH 10 of wheat gliadins: Influence on their functional properties
    • Bollecker, S.; Viroben, G.; Popineau, Y.; Gueguen, J. Acid deamidation and enzymatic modification at pH 10 of wheat gliadins: influence on their functional properties. Sci. Aliments 1990, 10, 343-356.
    • (1990) Sci. Aliments , vol.10 , pp. 343-356
    • Bollecker, S.1    Viroben, G.2    Popineau, Y.3    Gueguen, J.4
  • 28
    • 0027507052 scopus 로고
    • Studies of the zein-like α-prolamins based on an analysis of amino acid sequences: Implications for their evolution and three-dimensional structure
    • Garratt, R.; Oliva, G.; Caracelli, I.; Leite, A.; Arruda, P. Studies of the zein-like α-prolamins based on an analysis of amino acid sequences: implications for their evolution and three-dimensional structure. Proteins 1993, 15, 88-99.
    • (1993) Proteins , vol.15 , pp. 88-99
    • Garratt, R.1    Oliva, G.2    Caracelli, I.3    Leite, A.4    Arruda, P.5
  • 29
    • 0030896382 scopus 로고    scopus 로고
    • Three-dimensional structure of maize α-zein proteins studied by small-angle X-ray scattering
    • Matsushima, N.; Danno, G.-I.; Takezawa, H.; Izumi, Y. Three-dimensional structure of maize α-zein proteins studied by small-angle X-ray scattering. Biochim. Biophys. Acta 1997, 1339, 14-22.
    • (1997) Biochim. Biophys. Acta , vol.1339 , pp. 14-22
    • Matsushima, N.1    Danno, G.-I.2    Takezawa, H.3    Izumi, Y.4
  • 30
    • 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
  • 32
    • 0002047256 scopus 로고
    • Protein interactions in emulsions: Protein-lipid interactions
    • Hettiarachchy, N. S., Ziegler, G. R., Eds.; Dekker: New York
    • Mangino, M. E. Protein interactions in emulsions: protein-lipid interactions. In Protein Functionality in Food Systems; Hettiarachchy, N. S., Ziegler, G. R., Eds.; Dekker: New York, 1994; pp 147-180.
    • (1994) Protein Functionality in Food Systems , pp. 147-180
    • Mangino, M.E.1
  • 33
    • 0031062448 scopus 로고    scopus 로고
    • Antioxidative activity of barley hordein and its loss by deamidation
    • Chiue, H.; Kusano, T.; Iwami, K. Antioxidative activity of barley hordein and its loss by deamidation. J. Nutr. Sci. Vitaminol. 1997, 43, 145-154.
    • (1997) J. Nutr. Sci. Vitaminol. , vol.43 , pp. 145-154
    • Chiue, H.1    Kusano, T.2    Iwami, K.3
  • 34
    • 0001121879 scopus 로고
    • Inhibition of methyl linoleate peroxidation by maize zein in powder model system at high water activity
    • Wang, J. Y.; Miyazawa, T.; Fujimoto, K. Inhibition of methyl linoleate peroxidation by maize zein in powder model system at high water activity. Agric. Biol. Chem. 1991, 55, 1531-1536.
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1531-1536
    • Wang, J.Y.1    Miyazawa, T.2    Fujimoto, K.3
  • 35
    • 0012396424 scopus 로고
    • Antioxidant activities of zeins from different maize varieties against docosahexaenoic acid ethyl ester
    • Matsumura, Y.; Andonova, P. P.; Hayashi, Y.; Murakami, H.; Mori, T. Antioxidant activities of zeins from different maize varieties against docosahexaenoic acid ethyl ester. Cereal Chem. 1994, 71, 428-433.
    • (1994) Cereal Chem. , vol.71 , pp. 428-433
    • Matsumura, Y.1    Andonova, P.P.2    Hayashi, Y.3    Murakami, H.4    Mori, T.5
  • 36
    • 85007969084 scopus 로고
    • Decreased antioxidative activity of maize zein in response to deamidation rate
    • Chiue, H.; Iwami, K.; Kusano, T.; Ibuki, F. Decreased antioxidative activity of maize zein in response to deamidation rate. Biosci., Biotechnol., Biochem. 1994, 55, 198-199.
    • (1994) Biosci., Biotechnol., Biochem. , vol.55 , pp. 198-199
    • Chiue, H.1    Iwami, K.2    Kusano, T.3    Ibuki, F.4
  • 37
    • 0031031544 scopus 로고    scopus 로고
    • Deamidation-induced fragmentation of maize zein, and its linked reduction in fatty acid-binding capacity as well as antioxidative effect
    • Chiue, H.; Kusano, T.; Iwami, K. Deamidation-induced fragmentation of maize zein, and its linked reduction in fatty acid-binding capacity as well as antioxidative effect. Food Chem. 1997, 58, 111-117.
    • (1997) Food Chem. , vol.58 , pp. 111-117
    • Chiue, H.1    Kusano, T.2    Iwami, K.3


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