Determination of useful lifetime of immobilized beta-galactosidase for hydrolysis of lactose in permeate obtained from ultrafiltration of cottage cheese whey

Scott, T C; Hill, Jr, C G; Amundson, C H; Scott, C D

Title: Determination of useful lifetime of immobilized beta-galactosidase for hydrolysis of lactose in permeate obtained from ultrafiltration of cottage cheese whey

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Abstract

Beta-galactosidase immobolized on a porous silica carrier was used to effect the hydrolysis of lactose in permeate that results from the ultrafiltration of cottage cheese whey. Results obtained from analyzing kinetics of the immobilized enzyme have led to the formulation of a model that can be used to assess catalyst performance when utilizing a specified reactor operating strategy. The model predicts a lifetime of 90 days for the catalyst bed when starting production at 30 degrees and maintaining a constant production rate by raising the operating temperature as a function of time-on-stream. The useful lifetime of the catalyst was not significantly affected by the extent of lactose conversion carried out in the reactor. This model has the potential for use in optimization of reactor operating conditions for industrial applications of the immobilized enzyme.

Authors:

Scott, T C; Hill, Jr, C G; Amundson, C H; Scott, C D ^[1]

Publication Date:: Wed Jan 01 00:00:00 EST 1986

Research Org.:: Oak Ridge National Lab., Oak Ridge, TN 37831, USA. Chemical Technology Div.

OSTI Identifier:: 5812564

Report Number(s):: CONF-860508-
Journal ID: CODEN: BIBSB

Resource Type:: Conference

Journal Name:: Biotechnol. Bioeng. Symp.; (United States)

Additional Journal Information:: Journal Volume: 17; Conference: 8. symposium on biotechnology for fuels and chemicals, Gatlinburg, TN, USA, 13 May 1986

Country of Publication:: United States

Language:: English

Subject:: 09 BIOMASS FUELS; GALACTOSIDASE; IMMOBILIZED ENZYMES; PERFORMANCE TESTING; WHEY; ENZYMATIC HYDROLYSIS; SACCHARIFICATION; BIOREACTORS; CATALYSTS; CHEMICAL REACTION KINETICS; FOOD INDUSTRY; LACTOSE; MATHEMATICAL MODELS; OPTIMIZATION; TEMPERATURE DEPENDENCE; TIME DEPENDENCE; CARBOHYDRATES; CHEMICAL REACTIONS; DECOMPOSITION; DISACCHARIDES; ENZYMES; GLYCOSYL HYDROLASES; HYDROLASES; HYDROLYSIS; INDUSTRIAL WASTES; INDUSTRY; KINETICS; LYSIS; O-GLYCOSYL HYDROLASES; OLIGOSACCHARIDES; ORGANIC COMPOUNDS; REACTION KINETICS; SACCHARIDES; SOLVOLYSIS; TESTING; WASTES; 140504* - Solar Energy Conversion- Biomass Production & Conversion- (-1989)

Citation Formats


                    Scott, T C, Hill, Jr, C G, Amundson, C H, and Scott, C D. Determination of useful lifetime of immobilized beta-galactosidase for hydrolysis of lactose in permeate obtained from ultrafiltration of cottage cheese whey.  United States: N. p., 1986. 
        Web.

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                    Scott, T C, Hill, Jr, C G, Amundson, C H, & Scott, C D. Determination of useful lifetime of immobilized beta-galactosidase for hydrolysis of lactose in permeate obtained from ultrafiltration of cottage cheese whey.  United States.

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                    Scott, T C, Hill, Jr, C G, Amundson, C H, and Scott, C D. 1986.  
        "Determination of useful lifetime of immobilized beta-galactosidase for hydrolysis of lactose in permeate obtained from ultrafiltration of cottage cheese whey".  United States.

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@article{osti_5812564,

  title        = {Determination of useful lifetime of immobilized beta-galactosidase for hydrolysis of lactose in permeate obtained from ultrafiltration of cottage cheese whey},

  author       = {Scott, T C and Hill, Jr, C G and Amundson, C H and Scott, C D},

  abstractNote = {Beta-galactosidase immobolized on a porous silica carrier was used to effect the hydrolysis of lactose in permeate that results from the ultrafiltration of cottage cheese whey. Results obtained from analyzing kinetics of the immobilized enzyme have led to the formulation of a model that can be used to assess catalyst performance when utilizing a specified reactor operating strategy. The model predicts a lifetime of 90 days for the catalyst bed when starting production at 30 degrees and maintaining a constant production rate by raising the operating temperature as a function of time-on-stream. The useful lifetime of the catalyst was not significantly affected by the extent of lactose conversion carried out in the reactor. This model has the potential for use in optimization of reactor operating conditions for industrial applications of the immobilized enzyme.},

  doi          = {},

  url          = {https://www.osti.gov/biblio/5812564},
  journal      = {Biotechnol. Bioeng. Symp.; (United States)},
number       = ,

  volume       = 17,

  place        = {United States},

  year         = {Wed Jan 01 00:00:00 EST 1986},

  month        = {Wed Jan 01 00:00:00 EST 1986}

}

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