ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
Language
Number of Hits per Page
Default Sort Criterion
Default Sort Ordering
Size of Search History
Default Email Address
Default Export Format
Default Export Encoding
Facet list arrangement
Maximum number of values per filter
Auto Completion
Topics (search only within journals and journal articles that belong to one or more of the selected topics)
Show more topics
Feed Format
Maximum Number of Items per Feed
Permalink If you want to be able to use settings permanently, you must save your settings and then set a Bookmark to the permalink
feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Collagen as the Major Edible Component of Jellyfish (Stomolophus nomural) (1983)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 48 (1983), 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 mesogloea and skin of a common edible jellyfish, Stomolophus nomurai, were characterized with respect to amino acid composition and compared with a commercially salted jellyfish. Then the mesogloea was digested with pepsin at 3°C for 48 hr and its solubilized protein was isolated and subjected to biochemical analyses. These composite results have shown that the major edible component of jellyfish was the connective tissue protein, collagen, characterized by its high content of hydroxylysine and its glycosides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1983.tb05078.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    ISOENZYMES OF POLYPHENOL OXIDASE FROM HIGH L-DOPA CONTAINING VELVET BEAN (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: The seeds, leaves, and stem of velvet bean (Stizolobium aterrimum) contained high concentrations of L-DOPA and polyphenol oxidase. Polyacrylamide-gel electrophoresis revealed three polyphenol oxidase isoenzymes in the seeds of velvet bean, two in the leaves and stem. All isoenzymes were active with o-diphenols such as catechol, caffeic acid, d-catechin and L-DOPA. L-Tyrosine was not active to the isoenzymes. Polyphenol oxidase semipurified by ammonium sulfate fractionation exhibits a smaller Km for L-DOPA than other substrates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1978.tb02379.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    CHARACTERIZATION OF CELL BOUND GLUCOSE ISOMERASE OF Streptomyces bikiniensis (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 41 (1976), 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: Numerous microorganisms were screened for d-glucose isomerizing activity from soil by this laboratory. It was found that a strain of Streptomyces bikiniensis produced high activity of glucose isomerase in culture medium containing xylose or xylan as inducer. The cell bound glucose isomerase was prepared using cells of S. bikiniensis. The cell bound enzyme also efficiently catalyzes the isomerization of d-xylose and d-ribose and to a lesser extent L-rhamnose and d-arabinose to their respective ketoses. Isomerization of glucose to fructose by the enzyme was stimulated most effectively by Mg2+ and CO2+ combined or singly, and slightly by Mn2+. Cobalt and Mg2+ also inhibited thermal denaturation of the enzyme. The optimum pH for the enzyme was between 8 and 9, and optimum temperature was found to be 80°C. The enzyme is highly thermostable. The cell bound glucose isomerase was examined for isomerization of glucose to fructose in a batch system by incubating a mixture of the enzyme and various concentrations of glucose in 0.05M phosphate buffer, pH 7.2 containing 5 mM MgSO4 and 0.5 mM CoCl2 at various temperatures. It was found that maximum isomerization of glucose to fructose (50%) was reached when optimum concentration of enzyme and substrate was incubated at 70°C for 70 hr. The cell bound enzyme can be recovered after the operation and used for successive operations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1976.tb01177.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    VIABILITY OF Staphylococcus aureus IN INTERMEDIATE MOISTURE MEATS (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 38 (1973), 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
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1973.tb02134.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    ISOMERIZATION OF GLUCOSE TO FRUCTOSE BY SEMIPURIFIED, CELL BOUND AND IMMOBILIZED GLUCOSE ISOMERASE FROM STREPTOMYCES sp. (1975)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 40 (1975), 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
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1975.tb01029.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    DYNAMIC LOT SIZING FOR A SINGLE-FACILITY MULTIPRODUCT PROBLEM IN A ROLLING-HORIZON ENVIRONMENT (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Decision sciences 18 (1987), S. 0 
    Details
    ISSN: 1540-5915
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Economics
    Notes: This paper considers a production planning model for a single-facility multiproduct problem where backlogging is not allowed. A planning-horizon theorem is derived. From that theorem, a forward algorithm for finding an optimal solution over a finite horizon and a procedure for selecting the first-period production in a rolling-horizon environment are developed. Computational results from a set of simulation experiments designed to investigate the cost effectiveness of the procedure demonstrate its effectiveness.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1540-5915.1987.tb01521.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Photoinactivation and photoprotection of photosystem II in nature (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 100 (1997), S. 0 
    Details
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Photosystem II plays a central role not only in energy transduction, but also in monitoring the molecular redox mechanisms involved in signal transduction for acclimation to environmental stresses. Central to the regulation of photosystem II (PSII) function as a light-driven molecular machine in higher plant leaves, is an inevitable photo-inactivation of one PSII after 106–107 photons have been delivered to the leaf, although the act of photoinactivation per se requires only one photon. PSII function in acclimated pea leaves shows a reciprocity between irradiance and the time of illumination, demonstrating that the photoinactivation of PSII is a light dosage effect, depending on the number of photons absorbed rather than the rate of photon absorption. Hence, PSII photoinactivation will occur at low as well as high irradiance. There is a heterogeneity of PSII functional stability, possibly with less stable PSII monomers being located in grana margins and more stable PSII dimers in appressed granal domains. Matching the inevitable photoinactivation of PSII, green plants have an intrinsic capacity for D1 protein synthesis to restore PSII function which is saturated at very low light. Photoinhibition of PSII in vivo is often a photoprotective strategy rather than a damaging process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1399-3054.1997.tb04777.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Potential of Near Infrared Reflectance (NIR) Spectroscopy for Estimating Nutrient Content of Dehydrated Vegetables (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: A near infrared reflectance (NIR) spectrophotometric procedure was evaluated for potential use in assaying nutrient contents of vegetables. Dried ground samples of cauliflower, broccoli, Brussels sprouts, spinach, asparagus, peas, green beans, and squash were analyzed chemically for crude protein, crude fat, ash, and neutral detergent fiber (NDF) and then scanned to develop NIR prediction equations. For the 75 calibration foods samples, the respective correlation coefficients between actual and NIR predicted values of these food components were 0.97, 0.77, 0.91, 0.81. Predictions for 26 unknown samples, which included cabbage, carrots, chard, corn, onions and rhubarb, were based on NIR equations developed from the first 75 samples. The resultant correlations were 0.95, 0.49, 0.85, and 0.78, respectively, for crude protein, crude fat, ash and NDF. NIR prediction detected incorrect chemical values of crude protein in several samples.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1982.tb04982.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    PRODUCTION AND CHARACTERIZATION OF β-GALACTOSIDASE FROM ASPERGILLUS ORYZAE (1979)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 44 (1979), 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: A strain of Aspergillus oryzae producing extracellular β-galactosidase that hydrolyzes lactose in whey and dairy products was selected. The crude lactase concentrates were prepared by both semisolid and submerged fermentation. Yields of the enzyme from semisolid fermentation were much higher than submerged fermentation. The crude enzyme hydrolyzed lactose efficiently in acid whey and 83% lactose hydrolysis was obtained at 55°C. However, the activity of the crude enzyme is greatly reduced in cow's milk. A. oryzae lactase was purified by ammonium sulfate fractionation, chromatography on DEAE-cellulose, chromatography on CM-cellulose, and DEAE-Sephadex A-50 column chromatography. The purified enzyme had an optimum pH of 5. The optimum temperature was 5°C, whereas, for the crude enzyme preparation, it was 55°C. The pH stability of the enzyme was between 3.5 and 8.0 at room temperature for overnight. The Michaelis constant is 0.77 mM for o-nitrophenyl-p-D-galactopyranoside (ONPG) and 50 mM for lactose. The values of Vmax are 55.6 μg/min/mg of protein for ONPG and 2.4 μg/min/mg for lactose. Metal ions in the range 0.01-l mM and sulfhydryl reagent (0.01–0.1 mM of p-chloromercuribenzoate) have no effect on the enzyme activity. Galactose inhibited competitively the enzyme activity, whereas glucose did not.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1979.tb10016.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    CONTINUOUS CONVERSION OF STARCH TO GLUCOSE BY AN AMYLOGLUCOSIDASE-RESIN COMPLEX (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 38 (1973), 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
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1973.tb01428.x
    Location Call Number Expected 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...