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  • 1
    Electronic Resource
    Electronic Resource
    Enzymatic Control of Metability in a Direct Acidified Cheese Product (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An enzymatic method based on a fungal protease derived from A. oryzae was developed to control the meltability of a direct acidified cheese product. The kinetics of activation and inactivation were delineated. Meltability values, as determined by the standard L.D. Schrieber test, were strongly correlated with proteolysis as measured in terms of nonprotein nitrogen (NPN). Excessive proteolysis resulted in textural and organoleptic defects (short and grainy texture, bitterness). Optimum conditions for enzymatic action were delineated in terms of desirable rheological characteristics and overall product quality.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1981.tb04855.x
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  • 2
    Electronic Resource
    Electronic Resource
    EFFECT OF MILK CONSTITUENTS ON THE HYDROLYSIS OF LACTOSE BY LACTASE FROM Kluyveromyces fragilis (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 45 (1980), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Lactase activity in cold milk and whey is controlled by the ionic environment; maximum activity occurred in the presence of manganous ions. Of the major cations present in milk, sodium and calcium were inhibitory while potassium and magnesium were activating. Milk proteins strongly activated lactase in potassium phosphate buffer and the effect was enhanced in the presence of manganous ions; however the activation was masked by the milk salts in dairy products. Lactase activity in whey heated to 85°C was about 50% higher than in unheated whey, but no changes were observed in heated milk. There was no evidence for a thermolabile lactase inhibitor among the whey proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1980.tb07487.x
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  • 3
    Electronic Resource
    Electronic Resource
    PURIFICATION AND PHYSICOCHEMICAL PROPERTIES OF β-GALACTOSIDASE FROM Kluyveromyces fragilis (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: β-Galactosidase was purified to apparent homogeneity from cell-free extracts of Kluyveromyces fragilis by acetone precipitation, pseudo-affinity chromatography, hydroxylapatite chromatography and DEAE-Sephadex A-50 chromatography. The molecular weight was 201,000 and the partial specific volume was 0.715. No carbohydrate was detected. Electron microscopy indicated a molecular diameter of about 160Å with 9-10 subunits present. Isoelectric point of the major isozyme was 5.1. The extinction coefficient was 1.58 cm3 mg protein-1 at 280 nm. The amino-acid composition was quite different from the β-galactosidase of Escherichia coli. Enzyme activity was rapidly lost on incubation with p-chloromercuribenzoate; formation of 5-6 moles of mercaptide per mole of protein gave complete loss of activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1978.tb02360.x
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  • 4
    Electronic Resource
    Electronic Resource
    Production and Characterization of β-Galactosidase from Streptococcus thermophilus (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 47 (1982), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Crude β-galatosidase was produced by lysis of cells of Streptococcus thermophilus grown on deproteinized whey. The enzyme was partially purified by ammonium sulfate precipitation and ion-exchange chromatography to yield a preparation free of protease activity. Highest activity was observed at pH 7.1, in the presence of potassium and manganese ions. Both monovalent and divalent cations were required for maximum activity but not for stability. The Km for o-nitrophenyl-β-galactopyranoside and lactose was 0.98 mM and 6.9 mM, respectively. Galactose was a competitive inhibitor with Ki of 60 mM. Gel-filtration indicated a molecular weight of 530,000. The enzyme seems well suited to hydrolysis of lactose in milk.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1982.tb12891.x
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  • 5
    Electronic Resource
    Electronic Resource
    Protein Size and Meltability in Enzyme-Treated, Direct-Acidified Cheese Products (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 47 (1982), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: SDS-electrophoresis was used to follow changes in protein size in a direct-acidified cheese product treated with protease. Increased meltability was related to decreased protein size. Excessive proteolysis preferentially eliminated most of the intermediate-sized proteins producing a short, grainy texture and a bitter flavor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1982.tb10149.x
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  • 6
    Electronic Resource
    Electronic Resource
    Rapid Purfication of β -Galactosidase (Aspergillus Niger) from a Commercial Preparation (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 46 (1981), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: β-Galactosidase (A. niger) was purified from a commercial source in order to study the protein nature of the enzyme and some of its kinetic properties. The enzyme was rapidly purified by acetone precipitation, gel filtratior, and affinity chromatography. The specific activity of the purified enzyme was twice as high as that found in previous studies. The Km and Vmax for o-nitrophenyl β-D-galactopyranoside were 2.02 mM and 345 μmoles/min/mg protein respectively at pH 4.5 and 37°C. The procedure described yields a highly active enzyme which may be suitable for immobilization and hydrolysis of lactose. The molecular weight of the enzyme was 117,000 and the isolectric point was 4.9. The enzyme appears to be a glycoprotein and may contain multiple molecular forms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1981.tb15324.x
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  • 7
    Electronic Resource
    Electronic Resource
    THERMAL STABILIZATION OF FOUR MICROBIAL β-GALACTOSIDASES BY HISTIDINE, CASEIN AMINO ACIDS AND CASEIN (1991)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 15 (1991), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Thermal stability of four microbial β-galactosidases was evaluated in the presence of casein, casein amino acids and histidine. The enzymes from Esch-erichia coli, Kluyveromyces marxianus and Streptococcus thermophilus were stabilized up to 60 fold by these additives, but there was little effect on the enzyme from Aspergillus oryzae. Stabilization by casein amino acids and histidine was largely lactose dependent. Casein amino acids were not as effective as casein for any enzyme. For the K. marxianus enzyme, histidine alone was as effective as casein and the stabilizing effect was proportional to the logarithm of the histidine concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1991.tb00155.x
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  • 8
    Electronic Resource
    Electronic Resource
    NUMBER AND NATURE OF THE SULPHYDRYL GROUPS OF β-GALACTOSIDASE FROM KLUYVEROMYCES FRAGILIS (1980)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 4 (1980), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Theβ-galactosidase from Kluyveromyces fragilis contains 6 sulphydryl groups, all of which are modified by 5,5-dithiobis (2-nitrobenzoic acid) (DTNB) before all activity is lost. Activity losses can be largely (〉 70%) reversed by dithiothreitol when the number of sulphydryls reacted is 4 or less. Kinetic studies with DTNB suggest that none of the sulphydryls are in the active site, but that their modification leads to changes in the tertiary structure of the enzyme and hence gradual loss of activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1980.tb00657.x
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  • 9
    Electronic Resource
    Electronic Resource
    Production of α-Galactosidase from Aspergilus oryzae Grown in Solid State Culture (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 51 (1986), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Aspergillus oryzae QM 6737 was grown in solid state culture to produce α-galactosidase extracellularly. An optimum enzyme yield of ∼ 3 units/g solid was obtained on wheat bran, 35% initial moisture, after 5 days at 32°C, with agitation. Higher initial moisture levels reduced enzyme production. Higher yields were obtained by adding glucose (73% increase), sucrose (39% increase), or melibiose (39% increase) to the bran, but raffinose and stachyose had little or no effect. Enzyme yield increased three times when soy flour or soy beans was used as substrate but no enzyme production was observed using rice. Enzyme production on soy beans decreased with increased initial moisture levels and with decreased particle size.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1986.tb13127.x
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  • 10
    Electronic Resource
    Electronic Resource
    Determination of D-Amino Acids in Some Processed Foods and Effect of Racemization on In Vitro Digestibility of Casein (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 47 (1982), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Several processed foods and controls were analyzed by gas chromatography for the presence of D-amino acids. The concentration of each of the D-amino acids detected in the processed foods was approximately the same as that in the controls except that D-aspartic acid was significantly higher in dark toast surface and extruded soy flour. In vitro digestibility of casein which was alkali-treated to cause racemization, but without lysinoalanine (LAL) formation, was essentially the same as that of racemized casein containing LAL, but was lower than that of nonracemized control casein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1982.tb07654.x
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