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  • 1
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    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
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    E-BOOK
  • 2
    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
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  • 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
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  • 4
    Electronic Resource
    Electronic Resource
    Aminopeptidase Activities from Lactobacillus sake in Models of Curing Ingredients and Processing Conditions for Dry Sausage (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: The effect of curing agents and dry sausage processing parameters on four aminopeptidases (AP 1, AP 2, AP 3, and AP 4) of Lactobacillus sake was investigated. NaCl exerted a strong inhibitory effect against AP 1 but activated the remaining aminopeptidases. NaNO3 caused inhibition of AP 3 and AP 4. Ascorbic acid inhibited AP 1 and AP 3 while glucose only reduced AP 3 activity. Water activities and processing temperatures affected activity of all aminopeptidases. Acid pH decreased aminopeptidase activity except for AP 4. The combined effects of curing agents and process parameters to simulate different stages during dry sausage processing indicated that AP 2 and AP 4 may remain active throughout the process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1997.tb12246.x
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  • 5
    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
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  • 6
    Electronic Resource
    Electronic Resource
    Polyamines Affect Activity of Aminopeptidases from Lactobacillus sake (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: The effects of polyamines (agmatine, cadaverine, putrescine, spermidine and spermine) on the activity of the main aminopeptidases (AP I and AP II) from Lactobacillus sake were determined. Concentrations in the range of 1 mM caused 6–25% inhibition of AP I except for spermine (45% inhibition). Higher polyamine levels (5–10 mM), except for putrescine, exerted a stronger inhibition (20–60%) on AP I. Agmatine and putrescine also reduced AP II activity (6–25%) at concentrations of 0.1–10 mM while cadaverine did not have a notable effect. Spermidine and spermine stimulated (15–70%) the activity of AP II at concentrations 〉1 mM. Thus, control of polyamine levels is important because they are a potential hazard for human health and also because of their effects on aminopeptidase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1997.tb15475.x
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  • 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
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  • 8
    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
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  • 9
    Electronic Resource
    Electronic Resource
    Muscle and Adipose Tissue Aminopeptidase Activities in Raw and 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: Free amino acids have been analyzed in biceps femoris muscle and adipose tissue from raw and dry-cured ham. A high increase was observed for all amino acids except glutamine and taurine. Major increases were in glutamic acid, arginine, alanine, valine, leucine, and lysine. A survey of five aminopeptidase activities of muscle and adipose tissue from raw and dry-cured ham was performed by using 7-amino-4-methylcoumarin derivatives of five amino acids (Leu, Arg, Ala, Tyr and pGlu) as substrates. Optimum activity was found at neutral pH and around 37°C, except the leucyl hydrolyzing activity which was 45°C. High recoveries of activity (25–75%) were obtained in the dry-cured ham. These enzymes might be responsible for free amino acids increasing during dry-curing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1992.tb14301.x
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  • 10
    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
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