ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
  • 1
    Unknown
    Meat Biotechnology (2008)
    New York, NY : Springer
    Details
    Keywords: Biotechnology ; Chemistry ; Food science
    ISBN: 9780387793825
    URL: https://doi.org/10.1007/978-0-387-79382-5
    Language: English
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    E-BOOK
  • 2
    Electronic Resource
    Electronic Resource
    Non-Volatile Components Effects on Quality of “Serrano” Dry-cured Ham as Related to Processing Time (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 62 (1997), 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: Following long dry-curing periods, Spanish “Serrano” ham develops a specific “dry-cured ham” flavor. To determine the effects of length of curing on flavor generation, replicate hams were processed for 7 or 12 mo prior to amino acid, peptide, and flavor evaluation by reverse phase HPLC, capillary zone electrophoresis, and sensory analysis, respectively. Generation of dry-cured and pork flavors correlated with the accumulation of amino acids. The relation of these components with sensory descriptors was examined by factor analysis. Results indicated that combinations and proportions of taste-active components produced the specific dry-cured flavor characteristic rather than an accumulation of any single flavor component.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1997.tb12252.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Simple, Sensitive Assay for Microbial Aminopeptidase (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 62 (1997), 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 fluorimetric assay has been developed using several aminoacyl-7-amido-4-methyl coumarin (AMC) substrates (L-leucine-, L-alanine-, L-arginine-, L-tyrosine-, L-phenylalanine-, L-serine- and L-valine-AMC) in black multi-well plates to measure microbial aminopeptidase activity in lactobacilli intact cell suspensions (109–1010 CFU/mL). The fluorescence emission was visually evaluated by panelists and showed that substrate concentrations of 0.01 mM were optimal for visual detection and thus useful for rapid screening of many strains. The different ratios of activities quantitated in a multiscan fluorimeter showed a potential for differentiation among strains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1997.tb04436.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Study of the White Film Developed on the Cut Surface of Vacuum-packed Dry-cured Ham Slices (1990)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 55 (1990), 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: Scanning electron microscopy of the white film developed on the cut surface of some vacuum-packed dry-cured ham slices showed a fibrous structure composed of protein materials. Gradient SDS-PAGE revealed the main components in the film were proteins with molecular weight in the range 26000–87000, but especially 37000, 41000, 56000, and 65000. Free amino acids were also in the film in low proportions (250 μg total free amino acids per mg of protein). The main amino acids were proline methionine, isoleucine, leucine, phenylalanine, histidine and tyrosine. 11.7% of the total free amino acids was tyrosine, thus indicating its minor role in formation of white film.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb01637.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Deproteinization techniques for HPLC amino acid analysis in fresh pork muscle and dry-cured ham (1991)
    s.l. : American Chemical Society
    Journal of agricultural and food chemistry 39 (1991), S. 1792-1795 
    Details
    ISSN: 1520-5118
    Source: ACS Legacy Archives
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/jf00010a020
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Specificity of the second binding protein of the peptide ABC-transporter (Dpp) of Lactococcus lactis IL1403 (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 227 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The genome sequence of Lactococcus lactis IL1403 revealed the presence of a putative peptide-binding protein-dependent ABC-transporter (Dpp). The genes for two peptide-binding proteins (dppA and dppP) precede the membrane components, which include two transmembrane protein genes (dppB and dppC) and two ATP-binding protein genes (dppD and dppF). In this work, the gene specifying the second peptide-binding protein (DppP) was cloned under the control of the nisin promoter. The protein fused to a carboxyl-terminal histidine tag (DppP-His6) was purified and its binding properties were determined by monitoring the intrinsic fluorescence changes observed upon ligand binding. The major features of peptide binding to DppP-His6 include: (i) a requirement for a free N-terminal α-amino group in the ligand; (ii) a high affinity for di-, tri- and tetra-peptides; (iii) affinity constants for peptide binding independent of pH; and (iv) a high affinity for d-isomer-containing peptides. Remarkably, the features (ii), (iii) and (iv) differ from those previously reported for DppA-His6, suggesting that DppP-His6 is a more versatile peptide-binding protein that could have additional functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00662-1
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Biogenic Polyamines Affect Activity of Aminopeptidase B and Alanyl Aminopeptidase from Porcine Skeletal Muscle (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 61 (1996), 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 effect of biogenic polyamines (agmatine, cadaverine, putrescine, spermidine, and spermine) on the activity of pork muscle aminopeptidase and alanyl aminopeptidase was investigated. Agmatine (5 mM) showed a powerful inhibitory effect for both enzymes (more than 50% inhibition). Cadaverine and less intensely putrescine showed similar inhibitory effects for both enzymes. All assayed polyamines inhibited activity of both aminopeptidases except spermine and spermidine which did not affect aminopeptidase B. Thus, one of these inhibitors could be used to avoid the interference of alanyl aminopeptidase when assaying aminopeptidase B in muscle extracts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1996.tb14715.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Pre-freezing Hams Affects Lipolysis during Dry-curing (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 59 (1994), 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 initial freezing/thawing treatment of raw hams prior to dry-curing was compared to the standard process (refrigerated hams) by assaying free fatty acid generation and carbonyl index in both biceps femoris muscle and adipose tissues throughout curing. More intense lipolysis occurred between 0 and 5 mo for muscle, and 0 and 10 mo for adipose tissue. Lipid oxidation in adipose tissue was higher than in muscle. No significant differences (p〈0.05) were observed in lipolysis between refrigerated and frozen/thawed hams at the end of the process. Ham sensory evaluation after 15 mo showed that initial freezing/thawing treatment did not affect final sensory quality except for a more salty taste.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1994.tb06953.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Detection of Proteolytic Activity in Microorganisms Isolated from Dry-Cured Ham (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 57 (1992), 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: Different assays were tested for the detection of proteolytic activity in both Pediococcus pentosaceus and Staphylococcus xylosus, two major microorganisms isolated from dry-cured ham. Absence of endopeptidase activity was found even when using raw sarcoplasmic and myofibrillar proteins. However, P. pentosaceus showed strong leucine and valine arylamidase activities while St. xylosus showed a very weak leucine arylamidase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1992.tb06843.x
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Porcine Aminopeptidase Activity as Affected by Curing Agents (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 58 (1993), 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 effect of common curing agents (salt, nitrate, nitrite, ascorbic acid and glucose) on porcine muscle leucyl, arginyl, alanyl, pyroglu-tamyl and tyrosyl hydrolyzing activities was studied. Salt, ascorbate and nitrite had inhibitory effects on most enzyme activities. All activities decreased as salt increased (to 1.25 M) and/or water activity decreased (from 1.00 to 0.81). Nitrite inhibited only alanyl, pyroglu-tamyl and tyrosyl hydrolyzing activities. An in-vitro study using model conditions of three stages of dry-curing of ham, revealed that leucyl hydrolyzing activity may be important through the complete process. Other enzymes may also be involved in later stages of curing but are less important.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1993.tb09344.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...