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  • 1
    ISSN: 1520-5045
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 54 (1989), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Aqueous two-phase systems comprising a pair of a polymer and a salt were investigated as a means to clarify Cheddar cheese whey. Fat in cheese why could partition exclusively into the bottom phase of a polyethylene glycol/KH2PO4 aqueous two-phase system, resulting in a clear top phase containing whey proteins. Several parameters have been studied to optimize the recovery of whey proteins in such a system. Decreasing solute concentrations to 11.7% polyethylene glycol/10% KH2PO4, lowering pH to 3.8, and lowering temperature to 7°C all contributed to enhance the yield. This method should be able to remove ca. 98% fat in Cheddar cheese whey and to recover 〉 90% whey proteins.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Enzymatic hydrolysis of milk fat was studied in a reversed-micelle system consisting of lecithin, water (1% total volume) and butteroil. Candida cylindracea lipase entrapped in the water pools of reversed micelles hydrolyzed surrounding triglycerides. The optimum temperature for enzyme activity was 55°C with an activation energy of 15.4 kcal/mole, while maximum enzyme activity was observed between pH 4 to 6. The molar ratio of water to surfactant (R value) in the system influenced enzyme activity with maximum activity at R = 10. Enzyme activity also increased with increasing surfactant or enzyme concentration.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 56 (1991), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A process combining affinity chromatography with membrane filtration was used to isolate lactoferrin and immunoglobulin G from Cheddar cheese whey. Heparin Sepharose, protein G Sepharose, and protein G bearing Streptococcal cells were used as adsorbents to form affinity complexes with target proteins. These could be retained by 0.2 μm microfiltration membranes and separated from unbound whey proteins. Binding capacities and binding constants of adsorbents determined by Langmuir-type adsorption isotherms were 124 mg/mL gel and 5.4 × 10−6M for heparin Sepharose, 17.8 mg/mL gel and 3.5 × 10−7M for protein G Sepharose, and 148 μ.g/mL cell suspension and 1.1 × 10−7M for protein G cells. Lactoferrin with 95% purity and 92% iron-binding capacity, and immunoglobulin G with 90% purity and 86% activity could be obtained with reasonable yields.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 0268-2575
    Keywords: affinity ; sensor ; mathematical modeling ; acid proteases ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Affinity sensors with detection principle of competitive displacement of a responsive protein from an immobilised receptor by an analyte were subject to mathematical analysis. The model considered two competing binding reactions between the analyte and the responsive protein for the immobilised receptor in the solid phase. A cubic algebraic equation generated from the analysis was solved to get theoretical calibration curves for the sensor relating the signal generated, which is the bulk concentration of the responsive protein detected in solution, to the analyte concentration. The simulated results indicated several important system variables to consider when optimising the sensor's performance. They are the concentration of the responsive protein initially loaded, the density of the immobilised receptor, and the relative binding strength of both the analyte and the responsive protein toward the receptor. To test this model, experiments were carried out with a hypothetical sensor system, using bovine chymosin as the responsive protein, pepstatin-agarose as the immobilised receptor, and pepsin as the analyte. The model in general can describe the behavior of this type of affinity sensor reasonably well. From kinetic study of chymosin displacement in the model system, the effect of binding strength between responsive protein and receptor on the response of the sensor was also discussed.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0268-2575
    Keywords: N-isopropylacrylamide ; temperature-sensitive ; α-amylase ; LCST ; immobilized enzyme ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: --Temperature-responsive N-isopropylacrylamide (NIPAAm) polymer (PNIPAAm) with a free carboxyl functional end group and a copolymer (NIPNAS) of NIPAAm and N-acryloxysuccinimide (NAS) were synthesized and used for immobilization of α-amylase. The enzyme forms covalent bonds with the former polymer by single point attachment and with the latter polymer by multiple point attachment. Such a difference influences the enzyme activity and properties of the immobilized enzymes. The polymers are temperature-sensitive with lower critical solution temperatures (LCST) of 34·7 and 36·0°C for NIPNAS and PNIPAAm, respectively. The immobilized enzyme exhibited an LCST of 35·5°C for NIPNAS-amylase and 37·1°C for PNIPAAm-amylase. They precipitated and flocculated in aqueous solution above the LCST and redissolved when cooled below that temperature. The activity of the immobilized enzyme depended on the pH of the coupling buffer, with 8·0 being the optimum value. The specific activities of the immobilized enzymes were 87% and 108% compared with that of free enzyme with soluble starch as the substrate for NIPNAS-amylase and PNIPAAm-amylase, respectively. By characterizing the properties of the immobilized enzymes and comparing with those of free enzyme, no diffusion limitation of substrate was found for the immobilized enzymes and they are more thermal stable than the free enzyme. Within the two immobilized enzymes, NIPNAS-amylase showed better thermal stability and reusability. Repeated batch hydrolysis of soluble starch can be carried out efficiently with the immobilized enzymes by intermittent thermal precipitation and recycle of the enzyme. © 1997 SCI.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Alcoholysis of olive oil was carried out with lauryl and palmityl alcohols for producing wax esters. The reaction can be catalyzed efficiently by cell-bound lipase of Rhizopus niveous fungus cells immobilized within cellulose biomass support particles. Influences of reaction conditions such as water content, temperature, and substrate concentrations on reaction rates and yields were investigated.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary An affinity polymer derivative was synthesized with the group specific acid protease inhibitor pepstatin attached to dextran (M.W. 500,0001). This derivative was used in an aqueous two-phase system with hydroxypropyldextran to purify crude solutions of chymosin and Endothia parasitica (EP) acid proteases. Chymosin was purified by a factor of 6.2 with an overall yield of 83%. EP protease was similarly purified. A new pepstatin binding protease was discovered in crude EP extracts.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Hen egg white lysozyme was immobilized by covalent binding to a polymer showing reversibly soluble-insoluble characteristics with pH change. The retention of the specific activity of the immobilized enzyme can be as high as 41% of that of the free enzyme. The immobilized enzyme could be used in repeated batch lysis of M. lysodeikticus cells and to enhance the release of intracellular proteins 1.4 folds when compared with batch operation.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Isoamylase recovered from the fermentation broth of Pseudomonas amyloderamosa was immobilized onto water-insoluble carriers (chitin, CM-cellulose), and a temperature-sensitive reversibly soluble copolymer (N-isopropylacrylamide-co-N-acryloxysuccinimide). The characteristics and costs of the immobilized enzymes were analyzed. Enzyme coupled to the soluble copolymer showed the best performance among all supports.
    Type of Medium: Electronic Resource
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