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Volumn 134, Issue 3, 2012, Pages 1650-1657

Optimisation of immobilisation conditions for chick pea β-galactosidase (CpGAL) to alkylamine glass using response surface methodology and its applications in lactose hydrolysis

Author keywords

Galactosidase; Cicer arietinum; Immobilisation; Lactose hydrolysis; Response surface methodology

Indexed keywords

CICER ARIETINUM; GALACTOSIDASES; IMMOBILISATION; LACTOSE HYDROLYSIS; RESPONSE SURFACE METHODOLOGY;

EID: 84861097377     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2012.03.055     Document Type: Article
Times cited : (57)

References (26)
  • 2
    • 0346640496 scopus 로고    scopus 로고
    • A rapid method for the estimation of damaged starch in wheat flours
    • I.H. BoyacI, P.C. Williams, and H. Köksel A rapid method for the estimation of damaged starch in wheat flours Journal of Cereal Science 39 2004 139 145
    • (2004) Journal of Cereal Science , vol.39 , pp. 139-145
    • Boyaci, I.H.1    Williams, P.C.2    Köksel, H.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Analytical Biochemistry 72 1976 248 254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0031033554 scopus 로고    scopus 로고
    • Prolonged retention of cross-linked trypsin in calcium alginate microspheres
    • W.K. Chui, and L.S.C. Wan Prolonged retention of cross-linked trypsin in calcium alginate microspheres Journal of Microencapsulation 14 1997 51 61
    • (1997) Journal of Microencapsulation , vol.14 , pp. 51-61
    • Chui, W.K.1    Wan, L.S.C.2
  • 6
    • 63749119165 scopus 로고    scopus 로고
    • Optimal immobilisation of β-galactosidase from Pea (PsBGAL) onto Sephadex and Chitosan beads using response surface methodology and its applications
    • A. Dwevedi, and A.M. Kayastha Optimal immobilisation of β-galactosidase from Pea (PsBGAL) onto Sephadex and Chitosan beads using response surface methodology and its applications Bioresource Technology 100 2009 2667 2675
    • (2009) Bioresource Technology , vol.100 , pp. 2667-2675
    • Dwevedi, A.1    Kayastha, A.M.2
  • 7
    • 59849127945 scopus 로고    scopus 로고
    • Stabilisation of β-galactosidase (from peas) by immobilisation onto Amberlite MB-150 beads and its application in lactose hydrolysis
    • A. Dwevedi, and A.M. Kayastha Stabilisation of β-galactosidase (from peas) by immobilisation onto Amberlite MB-150 beads and its application in lactose hydrolysis Journal of Agriculture and Food Chemistry 57 2009 682 688
    • (2009) Journal of Agriculture and Food Chemistry , vol.57 , pp. 682-688
    • Dwevedi, A.1    Kayastha, A.M.2
  • 10
    • 26444582266 scopus 로고    scopus 로고
    • Process optimisation for biodiesel production from mahua (Madhuca indica) oil using response surface methodology
    • S.V. Ghadge, and H. Raheman Process optimisation for biodiesel production from mahua (Madhuca indica) oil using response surface methodology Bioresource Technology 97 2006 379 384
    • (2006) Bioresource Technology , vol.97 , pp. 379-384
    • Ghadge, S.V.1    Raheman, H.2
  • 11
    • 51349133975 scopus 로고    scopus 로고
    • Optimisation of transesterification of animal fat ester using response surface methodology
    • G.-T. Jeong, H.-S. Yang, and D.-H. Park Optimisation of transesterification of animal fat ester using response surface methodology Bioresource Technology 100 2009 25 30
    • (2009) Bioresource Technology , vol.100 , pp. 25-30
    • Jeong, G.-T.1    Yang, H.-S.2    Park, D.-H.3
  • 12
    • 67649188397 scopus 로고    scopus 로고
    • Polymer-assisted iron oxide magnetic nanoparticle immobilized keratinase
    • N. Karak, R. Konwarh, S.K. Rai, and A.K. Mukherjee Polymer-assisted iron oxide magnetic nanoparticle immobilized keratinase Nanotechnology 20 2009 1 10
    • (2009) Nanotechnology , vol.20 , pp. 1-10
    • Karak, N.1    Konwarh, R.2    Rai, S.K.3    Mukherjee, A.K.4
  • 13
    • 79751533142 scopus 로고    scopus 로고
    • Immobilisation of soybean (Glycine max) α-amylase onto Chitosan and Amberlite MB-150 beads: Optimisation and characterisation
    • A. Kumari, and A.M. Kayastha Immobilisation of soybean (Glycine max) α-amylase onto Chitosan and Amberlite MB-150 beads: Optimisation and characterisation Journal of Molecular Catalysis B-Enzymatic 69 2011 8 14
    • (2011) Journal of Molecular Catalysis B-Enzymatic , vol.69 , pp. 8-14
    • Kumari, A.1    Kayastha, A.M.2
  • 14
    • 84860291807 scopus 로고    scopus 로고
    • A β-galactosidase from chick pea (Cicer arietinum) seeds: Its purification, biochemical properties and industrial applications
    • in press
    • Kishore, D.; & Kayastha, A. M. (2012). A β-galactosidase from chick pea (Cicer arietinum) seeds: Its purification, biochemical properties and industrial applications. Food Chemistry, in press. http://dx.doi.org/10.1016/j. foodchem.2012.03.032.
    • (2012) Food Chemistry
    • Kishore, D.1    Kayastha, A.M.2
  • 16
    • 0017221823 scopus 로고
    • Assay procedures for immobilized enzymes
    • B. Mattiasson, and K. Mosbach Assay procedures for immobilized enzymes Methods Enzymology 44 1976 335 353
    • (1976) Methods Enzymology , vol.44 , pp. 335-353
    • Mattiasson, B.1    Mosbach, K.2
  • 17
    • 8444230519 scopus 로고    scopus 로고
    • Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking
    • I. Migneault, C. Dartiguenave, M.J. Bertrand, and K.C. Waldron Glutaraldehyde: Behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking BioTechniques 37 2004 790 802
    • (2004) BioTechniques , vol.37 , pp. 790-802
    • Migneault, I.1    Dartiguenave, C.2    Bertrand, M.J.3    Waldron, K.C.4
  • 18
    • 0033054494 scopus 로고    scopus 로고
    • Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: A statistical approach
    • G.S.N. Naidu, and T. Panda Performance of pectolytic enzymes during hydrolysis of pectic substances under assay conditions: A statistical approach Enzyme and Microbial Technology 25 1999 116 124
    • (1999) Enzyme and Microbial Technology , vol.25 , pp. 116-124
    • Naidu, G.S.N.1    Panda, T.2
  • 19
    • 34547548919 scopus 로고    scopus 로고
    • Optimizing the production of cutinase by Fusarium oxysporum using response surface methodology
    • T.F. Pio, and G.A. Macedo Optimizing the production of cutinase by Fusarium oxysporum using response surface methodology Enzyme and Microbial Technology 41 2007 613 619
    • (2007) Enzyme and Microbial Technology , vol.41 , pp. 613-619
    • Pio, T.F.1    MacEdo, G.A.2
  • 20
    • 31044447624 scopus 로고    scopus 로고
    • Improved stability of urease upon coupling to alkylamine and arylamine glass and its analytical use
    • K.R.C. Reddy, and A.M. Kayastha Improved stability of urease upon coupling to alkylamine and arylamine glass and its analytical use Journal of Molecular Catalysis B-Enzymatic 38 2006 104 112
    • (2006) Journal of Molecular Catalysis B-Enzymatic , vol.38 , pp. 104-112
    • Reddy, K.R.C.1    Kayastha, A.M.2
  • 21
    • 77952585408 scopus 로고    scopus 로고
    • Performance of β-galactosidase pretreated with lactose to prevent activity loss during the enzyme immobilisation process
    • Y.S. Song, J.H. Lee, S.W. Kang, and S.W. Kim Performance of β-galactosidase pretreated with lactose to prevent activity loss during the enzyme immobilisation process Food Chemistry 123 2010 1 5
    • (2010) Food Chemistry , vol.123 , pp. 1-5
    • Song, Y.S.1    Lee, J.H.2    Kang, S.W.3    Kim, S.W.4
  • 23
    • 0017872783 scopus 로고
    • The principles of enzyme stabilisation. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymes
    • V.P. Torchilin, A.V. Maksimenko, V.N. Smirnov, I.V. Berezin, A.M. Klibanov, and K. Martinek The principles of enzyme stabilisation. III. The effect of the length of intra-molecular cross-linkages on thermostability of enzymes Biochimica et Biophysica Acta 522 1978 277 283
    • (1978) Biochimica et Biophysica Acta , vol.522 , pp. 277-283
    • Torchilin, V.P.1    Maksimenko, A.V.2    Smirnov, V.N.3    Berezin, I.V.4    Klibanov, A.M.5    Martinek, K.6
  • 24
    • 80054859888 scopus 로고    scopus 로고
    • Enzymatic synthesis of fructooligosaccharides with high 1-kestose concentrations using response surface methodology
    • R. Vega, and M.E. Zuniga-Hansen Enzymatic synthesis of fructooligosaccharides with high 1-kestose concentrations using response surface methodology Bioresource Technology 102 2011 10180 10186
    • (2011) Bioresource Technology , vol.102 , pp. 10180-10186
    • Vega, R.1    Zuniga-Hansen, M.E.2
  • 25
    • 77955662366 scopus 로고    scopus 로고
    • Optimisation of immobilisation for selective oxidation of benzyl alcohol by Gluconobacter oxydans using response surface methodology
    • J.A. Wu, J.L. Wang, M.H. Li, J.P. Lin, and D.Z. Wei Optimisation of immobilisation for selective oxidation of benzyl alcohol by Gluconobacter oxydans using response surface methodology Bioresource Technology 101 2010 8936 8941
    • (2010) Bioresource Technology , vol.101 , pp. 8936-8941
    • Wu, J.A.1    Wang, J.L.2    Li, M.H.3    Lin, J.P.4    Wei, D.Z.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.