Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • 1985-1989  (5)
Source
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    CHEMICAL COMPOSITION AND POSTMORTEM CHANGES IN SOFT TEXTURED MUSCLE FROM INTENSELY FEEDING ATLANTIC COD (GADIUS MORHUA, L) (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 9 (1985), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Soft textured fillets from postspawning Atlantic cod caught during the influx of capelin exhibited significantly more drip than fillets from fish caught at other times of the 1983 inshore fishing season. The extent and rate of pH decline, protein, collagen and temperature of the muscle were not distinctive in fish caught during the influx of capelin. The muscle from these fish were unique in exhibiting a rapid and relatively low ultimate pH together with a stable pH after the onset of rigor mortis. The number of capelin present in the stomach of cod at the time of catch was positively related (r = 0.92) to the amount of free drip recovered from the fillets.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1985.tb00338.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    KINETIC AND THERMODYNAMIC CHARACTERISTICS OF A DIGESTIVE PROTEASE FROM ATLANTIC COD, GADUS MORHUA (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 13 (1989), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: A 23,500 dalton protease was isolated from the pyloric ceca of Atlantic cod by the successive steps of ammonium sulfate fractionation, acetone precipitation and affinity chromatography. The protein fraction recovered after affinity chromatography migrated as one band in both Davis and Laemmli gels. The protease was classified as trypsin (EC 3.4.21.4) on the basis of its substrate specificity, molecular weight and response to known trypsin inhibitors. For trypsin hydrolysis of benzoyl-DL-arginine p-nitroanilide, the substrate turnover number was 250 BAPA units per micromole trypsin (25°C), Km1 was 1.48 mM, the Arrhenius energy of activation (Ea) was 8.9 kcal/mol, and the free energy of activation (ΔG*) was 12.8 kcal/mol. The Vmax for the hydrolysis of tosylarginine methyl ester was 18,210 TAME units per micromole trypsin and the Km1 for the same reaction was 0.22 mM at 25°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1989.tb00394.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    FAILURE OF SEPHAROSE-PEPSIN AS AN IMMOBILIZED MILK CLOTTING ENZYME (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 10 (1986), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Porcine pepsinogen A was attached to CNBr-activated Sepharose 4B and self activated to form Sepharose-pepsin A. Immobilized pepsin is active in hydrolyzing hemoglobin at acidic pH but has very low milk clotting activity. The low milk clotting activity of freshly prepared Sepharose-pepsin can be accounted for by leaching of small amounts of free pepsin during contact of the complex with milk substrate. The failure of bound pepsin to catalyze milk clotting appears to be due to part of the micellar casein in milk substrate being inaccessible to the immobilized rennet and may also be influenced by differences in pH optima with casein substrate for pepsin and Sepharose-pepsin.Porcine pepsin A, which is electrophoretically pure, and casein substrate exhibit a distinct bimodal optimum reaction pH at 2 and 6. The reaction at pH6 is not evident when the products are assayed by A280nm because the specific products formed at this pH exhibit low A280nm. The finding that a pure isoenzyme of pepsin can exhibit a bimodal pH profile for hydrolysis has probably been overlooked by other investigators because of the frequent assay by A280nm of products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1986.tb00086.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Effect of Heat-Stable Proteases on the Kinetic Parameters of Milk Clotting by Chymosin (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 50 (1985), 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: The milk clotting per unit casein hydrolytic activities of proteases from 14 psychrotrophic pseudomonad isolates of raw milk ranged from 0.77 to 9.97 at 30°C. The milk clotting activities of chymodn and T16 protease were not completely additive, especially at high chymosin concentration when clotting time was relatively fast. The T16 protease was not effective in catalyzing the enzymic step of milk clbtting at O°C in the time expected on the basis of its milk clotting at 30°C. Milk incubated with the T25 motease for 8 days at 4°C and then clotted with chymosin at 30°C exhibited weak curd consistency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1985.tb13754.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Astaxanthin formation by the yeastPhaffia rhodozyma on molasses (1988)
    Springer
    Biotechnology letters 10 (1988), S. 609-614 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Phaffia rhodozyma grown on 7–10% B or C garde molasses contained 2 to 3 times more astaxanthin than reported earlier for this red yeast. Yield of astaxanthin with 10% molasses as fermentation substrate was 15.3 μg/ml which was about 3 times higher than with glucose and 2 times higher than with a sugar blend representative of the molasses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024710
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...