메뉴 건너뛰기




Volumn 40, Issue 1, 2017, Pages 1-7

Immobilization of proline-specific endoprotease on nonporous silica nanoparticles functionalized with amino group

Author keywords

Beer; Chill haze; Enzymatic activity; Enzyme immobilization; Proline specific endoprotease

Indexed keywords

BEER; BREWING; ENZYME ACTIVITY; NANOPARTICLES; SILICA; SILICA NANOPARTICLES; SYNTHESIS (CHEMICAL);

EID: 84983528571     PISSN: 16157591     EISSN: 16157605     Source Type: Journal    
DOI: 10.1007/s00449-016-1669-7     Document Type: Article
Times cited : (8)

References (29)
  • 2
    • 0000619450 scopus 로고
    • Hydrophobic interaction in tannin-protein complexes
    • COI: 1:CAS:528:DyaL3cXht1elsb8%3D
    • Oh HI, Hoff JE, Armstrong GS, Haff LA (1980) Hydrophobic interaction in tannin-protein complexes. J Agric Food Chem 28:394–398
    • (1980) J Agric Food Chem , vol.28 , pp. 394-398
    • Oh, H.I.1    Hoff, J.E.2    Armstrong, G.S.3    Haff, L.A.4
  • 3
    • 0030515619 scopus 로고    scopus 로고
    • Natural polyphenols (vegetable tannins) as drugs: possible modes of action
    • COI: 1:CAS:528:DyaK28XnvFeiuw%3D%3D
    • Haslam E (1996) Natural polyphenols (vegetable tannins) as drugs: possible modes of action. J Nat Prod 59:205–215
    • (1996) J Nat Prod , vol.59 , pp. 205-215
    • Haslam, E.1
  • 4
    • 0038386063 scopus 로고    scopus 로고
    • Beer polypeptides and silica gel - Part I. Polypeptides involved in haze formation
    • COI: 1:CAS:528:DC%2BD3sXltlKhurc%3D
    • Leiper KA, Stewart GG, McKeown IP (2003) Beer polypeptides and silica gel - Part I. Polypeptides involved in haze formation. J Inst Brew 109:57–72
    • (2003) J Inst Brew , vol.109 , pp. 57-72
    • Leiper, K.A.1    Stewart, G.G.2    McKeown, I.P.3
  • 5
    • 0003150884 scopus 로고    scopus 로고
    • Mechanisms of beer colloidal stabilization
    • COI: 1:CAS:528:DyaK2sXks1GlsLo%3D
    • Siebert KJ, Lynn PY (1997) Mechanisms of beer colloidal stabilization. J Am Soc Brew Chem 55:73–78
    • (1997) J Am Soc Brew Chem , vol.55 , pp. 73-78
    • Siebert, K.J.1    Lynn, P.Y.2
  • 6
    • 0032967327 scopus 로고    scopus 로고
    • Effects of protein–polyphenol interactions on beverage haze, stabilization and analysis
    • COI: 1:CAS:528:DyaK1MXos1Cl
    • Siebert KJ (1999) Effects of protein–polyphenol interactions on beverage haze, stabilization and analysis. J Agric Food Chem 47:353–362
    • (1999) J Agric Food Chem , vol.47 , pp. 353-362
    • Siebert, K.J.1
  • 7
    • 0000112275 scopus 로고    scopus 로고
    • Formation of protein–polyphenol haze in beverages
    • COI: 1:CAS:528:DyaK28XksV2lt7Y%3D
    • Siebert KJ, Carrasco A, Lynn PY (1996) Formation of protein–polyphenol haze in beverages. J Agric Food Chem 44:1997–2005
    • (1996) J Agric Food Chem , vol.44 , pp. 1997-2005
    • Siebert, K.J.1    Carrasco, A.2    Lynn, P.Y.3
  • 8
    • 79952495648 scopus 로고    scopus 로고
    • Turbidity and haze formation in beer-insights and overview
    • COI: 1:CAS:528:DC%2BC3MXmtVKhtbo%3D
    • Steiner E, Becker T, Gastl M (2010) Turbidity and haze formation in beer-insights and overview. J Inst Brew 116:360–368
    • (2010) J Inst Brew , vol.116 , pp. 360-368
    • Steiner, E.1    Becker, T.2    Gastl, M.3
  • 9
    • 84878744996 scopus 로고    scopus 로고
    • Precursors and formation of colloidal haze in beer
    • COI: 1:CAS:528:DC%2BC3sXosVOrsr0%3D
    • Kotlikova B, Jelinek L, Karabin M, Dostalek P (2013) Precursors and formation of colloidal haze in beer. Chem Listy 107:362–368
    • (2013) Chem Listy , vol.107 , pp. 362-368
    • Kotlikova, B.1    Jelinek, L.2    Karabin, M.3    Dostalek, P.4
  • 11
    • 19944387652 scopus 로고    scopus 로고
    • A comparison of polyvinylpolypyrrolidone (PVPP), silica xerogel and a polyvinylpyrrolidone (PVP)–silica co-product for their ability to remove polyphenols from beer
    • COI: 1:CAS:528:DC%2BD2MXlsFSlt7Y%3D
    • Mitchell AE, Hong YJ, May JC, Wright CA, Bamforth CW (2005) A comparison of polyvinylpolypyrrolidone (PVPP), silica xerogel and a polyvinylpyrrolidone (PVP)–silica co-product for their ability to remove polyphenols from beer. J Inst Brew 111:20–25
    • (2005) J Inst Brew , vol.111 , pp. 20-25
    • Mitchell, A.E.1    Hong, Y.J.2    May, J.C.3    Wright, C.A.4    Bamforth, C.W.5
  • 12
    • 27144513766 scopus 로고    scopus 로고
    • Effective prevention of chill-haze in beer using an acid proline-specific endoprotease from Aspergillus niger
    • COI: 1:CAS:528:DC%2BD2MXpsl2qsrg%3D
    • Lopez M, Edens L (2005) Effective prevention of chill-haze in beer using an acid proline-specific endoprotease from Aspergillus niger. J Agric Food Chem 53:7944–7949
    • (2005) J Agric Food Chem , vol.53 , pp. 7944-7949
    • Lopez, M.1    Edens, L.2
  • 13
    • 0018852213 scopus 로고
    • Proline specific endo-and exopeptidases
    • COI: 1:CAS:528:DyaL3cXkvFSksr8%3D
    • Walter R, Simmons WH, Yoshimoto T (1980) Proline specific endo-and exopeptidases. Mol Cell Biochem 30:111–127
    • (1980) Mol Cell Biochem , vol.30 , pp. 111-127
    • Walter, R.1    Simmons, W.H.2    Yoshimoto, T.3
  • 15
    • 80755126760 scopus 로고    scopus 로고
    • The effects of hop-alpha-acids and proline-specific endoprotease (PSEP) treatments on the foam quality of beer
    • COI: 1:CAS:528:DC%2BC38XhtlKmsL8%3D
    • Evans DE, Finn JEC, Robinson LH, Eglinton JK, Sheehy M, Stewart DC (2011) The effects of hop-alpha-acids and proline-specific endoprotease (PSEP) treatments on the foam quality of beer. J Inst Brew 117:335–342
    • (2011) J Inst Brew , vol.117 , pp. 335-342
    • Evans, D.E.1    Finn, J.E.C.2    Robinson, L.H.3    Eglinton, J.K.4    Sheehy, M.5    Stewart, D.C.6
  • 16
    • 14944340300 scopus 로고    scopus 로고
    • The relative significance of physics and chemistry for beer foam excellence: theory and practice
    • COI: 1:CAS:528:DC%2BD2MXis12gtL0%3D
    • Bamforth C (2004) The relative significance of physics and chemistry for beer foam excellence: theory and practice. J Inst Brew 110:259–266
    • (2004) J Inst Brew , vol.110 , pp. 259-266
    • Bamforth, C.1
  • 17
    • 0036720751 scopus 로고    scopus 로고
    • The foaming properties of proteins isolated from barley
    • COI: 1:CAS:528:DC%2BD38XmsFalurY%3D
    • Kapp GR, Bamforth CW (2002) The foaming properties of proteins isolated from barley. J Sci Food Agric 82:1276–1281
    • (2002) J Sci Food Agric , vol.82 , pp. 1276-1281
    • Kapp, G.R.1    Bamforth, C.W.2
  • 18
    • 0038047702 scopus 로고    scopus 로고
    • Beer polypeptides and silica gel: part II. Polypeptides involved in foam formation
    • COI: 1:CAS:528:DC%2BD3sXltlKhu74%3D
    • Leiper KA, Stewart GG, McKeown IP (2003) Beer polypeptides and silica gel: part II. Polypeptides involved in foam formation. J Inst Brew 109:73–79
    • (2003) J Inst Brew , vol.109 , pp. 73-79
    • Leiper, K.A.1    Stewart, G.G.2    McKeown, I.P.3
  • 19
    • 62449121836 scopus 로고    scopus 로고
    • Understanding enzyme immobilisation
    • COI: 1:CAS:528:DC%2BD1MXksVSntLc%3D
    • Hanefeld U, Gardossi L, Magner E (2009) Understanding enzyme immobilisation. Chem Soc Rev 38:453–468
    • (2009) Chem Soc Rev , vol.38 , pp. 453-468
    • Hanefeld, U.1    Gardossi, L.2    Magner, E.3
  • 20
    • 84880122011 scopus 로고    scopus 로고
    • Enzyme immobilisation in biocatalysis: why, what and how
    • COI: 1:CAS:528:DC%2BC3sXhtVKhtrzO
    • Sheldon RA, van Pelt S (2013) Enzyme immobilisation in biocatalysis: why, what and how. Chem Soc Rev 42:6223–6235
    • (2013) Chem Soc Rev , vol.42 , pp. 6223-6235
    • Sheldon, R.A.1    van Pelt, S.2
  • 21
    • 84948743746 scopus 로고    scopus 로고
    • CRGO/alginate microbeads: an enzyme immobilization system and its potential application for a continuous enzymatic reaction
    • COI: 1:CAS:528:DC%2BC2MXhslCks7jM
    • Zhao F, Li H, Wang X, Wu L, Hou T, Guan J, Jiang Y, Xu H, Mu X (2015) CRGO/alginate microbeads: an enzyme immobilization system and its potential application for a continuous enzymatic reaction. J Mater Chem B 3:9315–9322
    • (2015) J Mater Chem B , vol.3 , pp. 9315-9322
    • Zhao, F.1    Li, H.2    Wang, X.3    Wu, L.4    Hou, T.5    Guan, J.6    Jiang, Y.7    Xu, H.8    Mu, X.9
  • 22
    • 84878698340 scopus 로고    scopus 로고
    • Immobilisation of enzymes on mesoporous silicate materials
    • COI: 1:CAS:528:DC%2BC3sXhtVKhtrvK
    • Magner E (2013) Immobilisation of enzymes on mesoporous silicate materials. Chem Soc Rev 42:6213–6222
    • (2013) Chem Soc Rev , vol.42 , pp. 6213-6222
    • Magner, E.1
  • 23
    • 84921784930 scopus 로고    scopus 로고
    • Stability of proteins on hydrophilic surfaces
    • COI: 1:CAS:528:DC%2BC2cXitFehsbbL
    • Grimaldi J, Radhakrishna M, Kumar SK, Belfort G (2015) Stability of proteins on hydrophilic surfaces. Langmuir 31:1005–1010
    • (2015) Langmuir , vol.31 , pp. 1005-1010
    • Grimaldi, J.1    Radhakrishna, M.2    Kumar, S.K.3    Belfort, G.4
  • 24
    • 84899443582 scopus 로고    scopus 로고
    • Co-immobilization of multi-enzyme on control-reduced graphene oxide by non-covalent bonds: an artificial biocatalytic system for the one-pot production of gluconic acid from starch
    • COI: 1:CAS:528:DC%2BC2cXmsFahsr0%3D
    • Zhao FH, Li H, Jiang YJ, Wang XC, Mu XD (2014) Co-immobilization of multi-enzyme on control-reduced graphene oxide by non-covalent bonds: an artificial biocatalytic system for the one-pot production of gluconic acid from starch. Green Chem 16:2558–2565
    • (2014) Green Chem , vol.16 , pp. 2558-2565
    • Zhao, F.H.1    Li, H.2    Jiang, Y.J.3    Wang, X.C.4    Mu, X.D.5
  • 25
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • COI: 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 26
    • 85029012368 scopus 로고    scopus 로고
    • Method for the prevention or reduction of haze in beverages
    • Lopez M, Edens L (2004) Method for the prevention or reduction of haze in beverages. US patent 20040115306 A1
    • (2004) US patent , pp. A1
    • Lopez, M.1    Edens, L.2
  • 27
    • 53949106970 scopus 로고    scopus 로고
    • Nanobiocatalysis and its potential applications
    • COI: 1:CAS:528:DC%2BD1cXht12lsLjJ
    • Kim J, Grate JW, Wang P (2008) Nanobiocatalysis and its potential applications. Trends Biotechnol 26:639–646
    • (2008) Trends Biotechnol , vol.26 , pp. 639-646
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 28
    • 0742323370 scopus 로고    scopus 로고
    • Enzyme immobilization in a biomimetic silica support
    • COI: 1:CAS:528:DC%2BD2cXnvFeitA%3D%3D
    • Luckarift HR, Spain JC, Naik RR, Stone MO (2004) Enzyme immobilization in a biomimetic silica support. Nat Biotechnol 22:211–213
    • (2004) Nat Biotechnol , vol.22 , pp. 211-213
    • Luckarift, H.R.1    Spain, J.C.2    Naik, R.R.3    Stone, M.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.