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Volumn 62, Issue 34, 2014, Pages 8562-8570

Effect of pH and recombinant barley (Hordeum vulgare L.) endoprotease B2 on degradation of proteins in soaked barley

Author keywords

barley; cysteine endoprotease B2; Hordeum vulgare L.; pH; protein; rec HvEP B2; soaking

Indexed keywords

AMINO ACIDS; MAMMALS; PH; PROTEINS; PROTEOLYSIS; PROTEOMICS; MOLECULAR BIOLOGY; RECOMBINANT PROTEINS;

EID: 84906753012     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf502170v     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 84906758793 scopus 로고
    • Forskellige foderstoffers kemiske sammensætning, fordøjelighed, energi- og proteinværdi til svin. 556
    • København: Landhusholdningsselskabets Forl.
    • Just, A.; Jørgenssen, H.; Fernández, J. A.; Bech-Andersen, S. Forskellige foderstoffers kemiske sammensætning, fordøjelighed, energi- og proteinværdi til svin. 556. Beretning fra Statens Husdyrbrugsforsøg. København: Landhusholdningsselskabets Forl., 1983
    • (1983) Beretning Fra Statens Husdyrbrugsforsøg
    • Just, A.1    Jørgenssen, H.2    Fernández, J.A.3    Bech-Andersen, S.4
  • 2
    • 34547965811 scopus 로고    scopus 로고
    • Digesta transit in different segments of the gastrointestinal tract of pigs as affected by insoluble fibre supplied by wheat bran
    • Wilfart, A.; Montagne, L.; Simmins, H.; Noblet, J.; van Milgen, J. Digesta transit in different segments of the gastrointestinal tract of pigs as affected by insoluble fibre supplied by wheat bran Br. J. Nutr. 2007, 98, 54-62
    • (2007) Br. J. Nutr. , vol.98 , pp. 54-62
    • Wilfart, A.1    Montagne, L.2    Simmins, H.3    Noblet, J.4    Van Milgen, J.5
  • 3
    • 34248637916 scopus 로고    scopus 로고
    • Influence of soaking, fermentation and phytase supplementation on nutrient digestibility in pigs offered a grower diet based on wheat and barley
    • Lyberg, K.; Lundh, T.; Pedersen, C.; Lindberg, J. E. Influence of soaking, fermentation and phytase supplementation on nutrient digestibility in pigs offered a grower diet based on wheat and barley Anim. Sci. 2006, 82, 853-858
    • (2006) Anim. Sci. , vol.82 , pp. 853-858
    • Lyberg, K.1    Lundh, T.2    Pedersen, C.3    Lindberg, J.E.4
  • 4
    • 0002746215 scopus 로고
    • Prediction of the Apparent Ileal Digestibility of Protein and Amino-Acids in Feedstuffs and Feed Mixtures for Pigs by In-Vitro Analyses
    • Boisen, S.; Fernandez, J. A. Prediction of the Apparent Ileal Digestibility of Protein and Amino-Acids in Feedstuffs and Feed Mixtures for Pigs by In-Vitro Analyses Anim. Feed Sci. and Technol. 1995, 51, 29-43
    • (1995) Anim. Feed Sci. and Technol. , vol.51 , pp. 29-43
    • Boisen, S.1    Fernandez, J.A.2
  • 5
    • 0346042393 scopus 로고    scopus 로고
    • Different expressions of dietary protein and amino acid digestibility in pig feeds and their application in protein evaluation: A theoretical approach
    • Boisen, S.; Moughan, P. J. Different expressions of dietary protein and amino acid digestibility in pig feeds and their application in protein evaluation: A theoretical approach Acta Agric. Scand., Sect. A 1996, 46, 165-172
    • (1996) Acta Agric. Scand., Sect. A , vol.46 , pp. 165-172
    • Boisen, S.1    Moughan, P.J.2
  • 6
    • 2642543482 scopus 로고    scopus 로고
    • Refining in vitro digestibility assays: Fractionation of digestible and indisgestible peptides
    • Qiao, Y.; Lin, X.; Odle, A.; Whittaker, A.; van Kempen, T. A. T. G. Refining in vitro digestibility assays: Fractionation of digestible and indisgestible peptides J. Anim. Sci. 2004, 82, 1669-1677
    • (2004) J. Anim. Sci. , vol.82 , pp. 1669-1677
    • Qiao, Y.1    Lin, X.2    Odle, A.3    Whittaker, A.4    Van Kempen, T.A.T.G.5
  • 7
    • 84979447958 scopus 로고
    • Rate-Limiting Enzymes in the Liberation of Amino-Acids in Mashing
    • Sopanen, T.; Takkinen, P.; Mikola, J.; Enari, T. M. Rate-Limiting Enzymes in the Liberation of Amino-Acids in Mashing J. Inst. Brew. 1980, 86, 211-215
    • (1980) J. Inst. Brew. , vol.86 , pp. 211-215
    • Sopanen, T.1    Takkinen, P.2    Mikola, J.3    Enari, T.M.4
  • 8
    • 0000461336 scopus 로고
    • Hydrolysis of Storage Proteins in Barley Endosperms - Analysis of Soluble Products
    • Rastogi, V.; Oaks, A. Hydrolysis of Storage Proteins in Barley Endosperms-Analysis of Soluble Products Plant Physiol. 1986, 81, 901-906
    • (1986) Plant Physiol. , vol.81 , pp. 901-906
    • Rastogi, V.1    Oaks, A.2
  • 9
    • 0034773313 scopus 로고    scopus 로고
    • Proteolytic degradation of cereal prolamins - The problem with proline
    • Simpson, D. J. Proteolytic degradation of cereal prolamins-the problem with proline Plant Sci. 2001, 161, 825-838
    • (2001) Plant Sci. , vol.161 , pp. 825-838
    • Simpson, D.J.1
  • 10
    • 0002722711 scopus 로고
    • Mobilization of Endospermal Reserves during the Germination of Barley
    • Enari, T. M.; Sopanen, T. Mobilization of Endospermal Reserves During the Germination of Barley J. Inst. Brew. 1986, 92, 25-31
    • (1986) J. Inst. Brew. , vol.92 , pp. 25-31
    • Enari, T.M.1    Sopanen, T.2
  • 11
    • 0000902932 scopus 로고
    • The Peptide Pools of Germinating Barley Grains - Relation to Hydrolysis and Transport of Storage Proteins
    • Higgins, C. F.; Payne, J. W. The Peptide Pools of Germinating Barley Grains-Relation to Hydrolysis and Transport of Storage Proteins Plant Physiol. 1981, 67, 785-792
    • (1981) Plant Physiol. , vol.67 , pp. 785-792
    • Higgins, C.F.1    Payne, J.W.2
  • 12
    • 0032127987 scopus 로고    scopus 로고
    • Cloning and functional characterisation of a peptide transporter expressed in the scutellum of barley grain during the early stages of germination
    • West, C. E.; Waterworth, W. M.; Stephens, S. M.; Smith, C. P.; Bray, C. M. Cloning and functional characterisation of a peptide transporter expressed in the scutellum of barley grain during the early stages of germination Plant J. 1998, 15, 221-229
    • (1998) Plant J. , vol.15 , pp. 221-229
    • West, C.E.1    Waterworth, W.M.2    Stephens, S.M.3    Smith, C.P.4    Bray, C.M.5
  • 13
    • 0000491925 scopus 로고
    • Mobilization of Proline in the Starchy Endosperm of Germinating Barley-Grain
    • Mikola, L.; Mikola, J. Mobilization of Proline in the Starchy Endosperm of Germinating Barley-Grain Planta 1980, 149, 149-154
    • (1980) Planta , vol.149 , pp. 149-154
    • Mikola, L.1    Mikola, J.2
  • 14
    • 21744460353 scopus 로고    scopus 로고
    • Endoproteases of barley and malt
    • Jones, B. L. Endoproteases of barley and malt J. Cereal Sci. 2005, 42, 139-156
    • (2005) J. Cereal Sci. , vol.42 , pp. 139-156
    • Jones, B.L.1
  • 15
    • 84858286148 scopus 로고    scopus 로고
    • Fermented liquid feed-Microbial and nutritional aspects and impact on enteric diseases in pigs
    • Canibe, N.; Jensen, B. B. Fermented liquid feed-Microbial and nutritional aspects and impact on enteric diseases in pigs Anim. Feed Sci. Technol. 2012, 173, 17-40
    • (2012) Anim. Feed Sci. Technol. , vol.173 , pp. 17-40
    • Canibe, N.1    Jensen, B.B.2
  • 16
    • 34247479016 scopus 로고    scopus 로고
    • Fermented liquid feed and fermented grain to piglets- effect on gastrointestinal ecology and growth performance
    • Canibe, N.; Jensen, B. B. Fermented liquid feed and fermented grain to piglets- effect on gastrointestinal ecology and growth performance Livest. Sci. 2007, 108, 198-201
    • (2007) Livest. Sci. , vol.108 , pp. 198-201
    • Canibe, N.1    Jensen, B.B.2
  • 17
    • 44649113798 scopus 로고    scopus 로고
    • Biochemical and microbiological properties of a cereal mix fermented with whey, wet wheat distillers' grain or water at different temperatures
    • Lyberg, K.; Olstorpe, M.; Passoth, V.; Schnurer, J.; Lindberg, J. E. Biochemical and microbiological properties of a cereal mix fermented with whey, wet wheat distillers' grain or water at different temperatures Anim. Feed Sci. Technol. 2008, 144, 137-148
    • (2008) Anim. Feed Sci. Technol. , vol.144 , pp. 137-148
    • Lyberg, K.1    Olstorpe, M.2    Passoth, V.3    Schnurer, J.4    Lindberg, J.E.5
  • 18
    • 84890350323 scopus 로고    scopus 로고
    • Production of barley endoprotease B2 in Pichia pastoris and its proteolytic acticity against native and recombinant hordeins
    • Rosenkilde, A. L.; Dionisio, G.; Holm, P. B.; Brinch-Pedersen, H. Production of barley endoprotease B2 in Pichia pastoris and its proteolytic acticity against native and recombinant hordeins Phytochemistry 2014, 97, 11-19
    • (2014) Phytochemistry , vol.97 , pp. 11-19
    • Rosenkilde, A.L.1    Dionisio, G.2    Holm, P.B.3    Brinch-Pedersen, H.4
  • 19
    • 0033759066 scopus 로고    scopus 로고
    • Prediction of Protein Cleavage Sites by the Barley Cysteine Endoproteases EP-A and EP-B Based on the Kinetics of Synthetic Peptide Hydrolysis
    • Davy, A.; Sørensen, M. B.; Svendsen, I.; Cameron-Mills, V.; Simpson, D. J. Prediction of Protein Cleavage Sites by the Barley Cysteine Endoproteases EP-A and EP-B Based on the Kinetics of Synthetic Peptide Hydrolysis Plant Physiol. 2000, 122, 137-146
    • (2000) Plant Physiol. , vol.122 , pp. 137-146
    • Davy, A.1    Sørensen, M.B.2    Svendsen, I.3    Cameron-Mills, V.4    Simpson, D.J.5
  • 20
    • 84906758794 scopus 로고    scopus 로고
    • Knowlegde Centre for Agriculture. Sortinfo, (accessed January, 11, 2010).
    • Knowlegde Centre for Agriculture. Sortinfo, www.sortinfo.dk. 2012, (accessed January, 11, 2010).
    • (2012)
  • 21
    • 0004202155 scopus 로고    scopus 로고
    • AOAC. 17 th ed. Association of Official Analytical Chemists International: Gaithersburg, MD.
    • AOAC. Official Methods of Analysis of AOAC International No. 984.13, 17 th ed.; Association of Official Analytical Chemists International: Gaithersburg, MD., 2000.
    • (2000) Official Methods of Analysis of AOAC International No. 984.13
  • 22
    • 39349090282 scopus 로고    scopus 로고
    • Converting nitrogen into protein-Beyond 6.25 and Jones' factors
    • Mariotti, F.; Tome, D.; Mirand, P. P. Converting nitrogen into protein-Beyond 6.25 and Jones' factors Critical Rev. Food Sci. Nutr. 2008, 48, 177-184
    • (2008) Critical Rev. Food Sci. Nutr. , vol.48 , pp. 177-184
    • Mariotti, F.1    Tome, D.2    Mirand, P.P.3
  • 23
    • 78549236797 scopus 로고    scopus 로고
    • Effect of heat-treatment, phytase, xylanase and soaking time on inositol phosphate degradation in vitro in wheat, soybean meal and rapeseed cake
    • Blaabjerg, K.; Carlsson, N. G.; Hansen-M?ller, J.; Poulsen, H. D. Effect of heat-treatment, phytase, xylanase and soaking time on inositol phosphate degradation in vitro in wheat, soybean meal and rapeseed cake Anim. Feed Sci. Technol. 2010, 162, 123-134
    • (2010) Anim. Feed Sci. Technol. , vol.162 , pp. 123-134
    • Blaabjerg, K.1    Carlsson, N.G.2    Hansen-Mller, J.3    Poulsen, H.D.4
  • 24
    • 84906770746 scopus 로고    scopus 로고
    • American Association of Cereal Chemists (AACC). 11 th ed. Method 46-15.01. Biuret. American Association of Cereal Chemists: St. Paul, MN.
    • American Association of Cereal Chemists (AACC). Approved Methods of American Association of Cereal Chemists, 11 th ed.; Method 46-15.01. Biuret. American Association of Cereal Chemists: St. Paul, MN, 2013.
    • (2013) Approved Methods of American Association of Cereal Chemists
  • 25
    • 84906758781 scopus 로고    scopus 로고
    • GELFREE 8100 Fractionation System Molecular weight fractionation with liquid phase recovery. Expedeon 2013. (accessed October 17.
    • GELFREE 8100 Fractionation System Molecular weight fractionation with liquid phase recovery. Expedeon 2013. http://www.expedeon.com/Portals/0/ product%20manuals/G8100-Manual-v1-4.pdf (accessed October 17, 2013.
    • (2013)
  • 27
    • 84876691193 scopus 로고    scopus 로고
    • Set-point control of RD21 protease activity by AtSerpin1 controls cell death in Arabidopsis
    • Lampl, N.; Alkan, N.; Davydov, O.; Fluhr, R. Set-point control of RD21 protease activity by AtSerpin1 controls cell death in Arabidopsis Plant J. 2013, 74, 498-510
    • (2013) Plant J. , vol.74 , pp. 498-510
    • Lampl, N.1    Alkan, N.2    Davydov, O.3    Fluhr, R.4
  • 28
    • 70350686335 scopus 로고    scopus 로고
    • Characterization of the Entire Cystatin Gene Family in Barley and Their Target Cathepsin L-Like Cysteine-Proteases, Partners in the Hordein Mobilization during Seed Germination
    • Martinez, M.; Cambra, I.; Carrillo, L.; Diaz-Mendoza, M.; Diaz, I. Characterization of the Entire Cystatin Gene Family in Barley and Their Target Cathepsin L-Like Cysteine-Proteases, Partners in the Hordein Mobilization during Seed Germination Plant Physiol. 2009, 151, 1531-1545
    • (2009) Plant Physiol. , vol.151 , pp. 1531-1545
    • Martinez, M.1    Cambra, I.2    Carrillo, L.3    Diaz-Mendoza, M.4    Diaz, I.5
  • 29
    • 0000700014 scopus 로고
    • Characterization of Germinated Barley Endoproteolytic Enzymes by 2-Dimensional Gel-Electrophoresis
    • Zhang, N. Y.; Jones, B. L. Characterization of Germinated Barley Endoproteolytic Enzymes by 2-Dimensional Gel-Electrophoresis J. Cereal Sci. 1995, 21, 145-153
    • (1995) J. Cereal Sci. , vol.21 , pp. 145-153
    • Zhang, N.Y.1    Jones, B.L.2
  • 30
    • 0025465440 scopus 로고
    • Hormonal-Regulation, Processing, and Secretion of Cysteine Proteinases in Barley Aleurone Layers
    • Koehler, S. M.; Ho, T. H. D. Hormonal-Regulation, Processing, and Secretion of Cysteine Proteinases in Barley Aleurone Layers Plant Cell 1990, 2, 769-783
    • (1990) Plant Cell , vol.2 , pp. 769-783
    • Koehler, S.M.1    Ho, T.H.D.2
  • 31
    • 0344198038 scopus 로고    scopus 로고
    • Effect of Reducing and Oxidizing Agents and pH on Malt Endoproteolytic Activities and Brewing Mashes
    • Jones, B. L.; Budde, A. D. Effect of Reducing and Oxidizing Agents and pH on Malt Endoproteolytic Activities and Brewing Mashes J. Agric. Food Chem. 2003, 51, 7504-7512
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 7504-7512
    • Jones, B.L.1    Budde, A.D.2
  • 32
    • 0027175339 scopus 로고
    • Activation of Oxidized Cysteine Proteinases by Thioredoxin-Mediated Reduction Invitro
    • Stephen, A. G.; Powls, R.; Beynon, R. J. Activation of Oxidized Cysteine Proteinases by Thioredoxin-Mediated Reduction Invitro Biochem. J. 1993, 291, 345-347
    • (1993) Biochem. J. , vol.291 , pp. 345-347
    • Stephen, A.G.1    Powls, R.2    Beynon, R.J.3
  • 33
    • 0035543051 scopus 로고    scopus 로고
    • Interactions of malt and barley (Hordeum vulgare L.) endoproteinases with their endogenous inhibitors
    • Jones, B. L. Interactions of malt and barley (Hordeum vulgare L.) endoproteinases with their endogenous inhibitors J. Agric. Food Chem. 2001, 49, 5975-5981
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 5975-5981
    • Jones, B.L.1


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