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  • 1
    Electronic Resource
    Electronic Resource
    CHANGES IN FRESHNESS OF CHILIPEPPER ROCKFISH (SEBASTES GOODEI) DURING STORAGE AS MEASURED BY CHEMICAL SENSORS AND BIOSENSORS (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 16 (1992), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Trimethylamine (TMA) and ammonia contents in Chilipepper rockfishes were determined by ion specific electrodes, as a late indicator of fish freshness. After 9 days of storage in ice, TMA contents significantly increased, indicating that bacterial spoilage was in progress. The pattern of changes in ammonia contents was similar to that of TMA. Determination of ATP degradation products in Chilipepper rockfish by HPLC showed that AMP and hypoxanthine levels were low and did not change much during storage. The concentration of IMP initially increased and then continuously decreased as inosine accumulated. Only trace amounts of hypoxanthine were detected in rockfish tissues. Chilipepper rockfish appears to differ from other Sebastes species in that ATP degradation results in inosine accumulation rather than hypoxanthine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1992.tb00439.x
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  • 2
    Electronic Resource
    Electronic Resource
    EDITORIAL (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 20 (1996), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1996.tb00573.x
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  • 3
    Electronic Resource
    Electronic Resource
    INFLUENCE OF WOUND INJURY ON ACCUMULATION OF PROTEINASE INHIBITORS IN LEAF AND STEM TISSUES OF TWO PROCESSING TOMATO CULTIVARS (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 20 (1996), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Serine proteinase inhibitor(s) and small amounts of cysteine proteinase inhibitor were detected in both leaf and stem tissue 48 h after mechanical injury to the lower leaf of 21–25 day old tomato cultivars (cv). Leaves accumulated about 2–15 times more trypsin inhibitor than stem tissue. Approximately 10 times more trypsin inhibitor (TIU) accumulated in plants held at 30C in continuous light compared to plants held under ambient greenhouse conditions after injury. Uninjured plants held at 30C under continuous light accumulated less proteinase inhibitor(s) than injured plants. Holding Bonnie Best in the dark at 30C for 48 h resulted in less inhibitor(s) accumulation in response to mechanical wounding than holding plants at 30C in continuous light. TIU/g tissue recovered from injured plants held at 30C under continuous light varied with cultivar, i.e., for leaves: Bonnie Best (33.61), Alta (21.00; 25.43), Castlemart (16.00; 13.17) and Halley (1.96); and for stems: Castlemart (8.29), Alta (4.47) and Bonnie Best (2.59). SDS-PAGE assayed for inhibitor activity revealed the main trypsin and chymotrypsin inhibitor(s) in injured leaves both had a molecular mass (Mr) of 19.1 KD on SDS-PAGE substrate gels. Treatment of the inhibitors with 2.0% SDS at 100C prior to electrophoresis revealed a second major trypsin inhibitor (Mr = 16.4 KD) and two additional major α-chymotrypsin inhibitors (Mr = 16.4; 6.2 KD).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1996.tb00579.x
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  • 4
    Electronic Resource
    Electronic Resource
    EDITORIAL (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 21 (1997), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1997.tb00197.x
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  • 5
    Electronic Resource
    Electronic Resource
    Editorial (2000)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 24 (2000), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.2000.tb00713.x
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  • 6
    Electronic Resource
    Electronic Resource
    NUCLEOTIDE CATABOLISM AND CHANGES IN TEXTURE INDICES DURING ICE STORAGE OF CULTURED STURGEON, ACIPENSER TRANSMONTANUS (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 16 (1992), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: ATP depletion and other biochemical changes were related to texture indices of cooked sturgeon meat from struggled and anesthetized fish. The rates of ATP depletion, pH decline and time of rigor onset were slow in both sturgeon groups compared to other finfish. ATP depletion and accumulation of inosine and hypoxanthine were significantly faster in sturgeon allowed to struggle before death than in anesthetized fish. Penetrometer tests revealed that cooked sturgeon meat was firmer prior to ATP depletion and the onset of rigor than in the postrigor state. Fish allowed to struggle prior to death had a softer cooked meat than anesthetized fish during the first few days of iced storage. Compression tests showed that texture of cooked meat was firmest when the muscle was in rigor and also showed that meat from struggled fish was softer than that from anesthetized fish. These findings suggested that the tough texture problem, sometimes observed in farmed sturgeon, may be minimized by allowing the sturgeon meat to go through rigor prior to cooking.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1992.tb00444.x
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  • 7
    Electronic Resource
    Electronic Resource
    TEMPERATURE ACCLIMATION OF ATLANTIC COD (GADUS MORHUA) AND ITS INFLUENCE ON FREEZING POINT AND BIOCHEMICAL DAMAGE OF POSTMORTEM MUSCLE DURING STORAGE AT 0° and -3°C (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food biochemistry 11 (1987), S. 0 
    Details
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The freezing point of muscle fluid from Newfoundland Atlantic cod held at ambient sea water temperature was as low as - 1.30°C in March and as high as - 0.80°C in July. Muscle fluid from cod held live at 0°C for 3 weeks had a freezing point of - 1.02°C in contrast to a muscle fluid freezing point of - 0.90°C for cod acclimated at 10°C prior to sacrifice. Muscle fluid from cold acclimated cod exhibited 0.40°C thermal hysteresis indicating freezing point depression was influenced by antifreeze substances. The following indices of deterioration were measured in muscle sections stored at 0°C or - 3°C for 21 days: extractable protein (EP), free drip (FD), extracellular area (EA), trimethylamineoxide (TMAO), trimethylamine (TMA), dimethylamine (DMA), free amino acids (AA), and pH. Muscle sections at the anterior end of fillets, from myotomes 9–20, prepared using aseptic technique and treated with antibiotic showed less evidence of biochemical deterioration: (a) when stored at - 3°C compared to 0°C with respect to EP, AA, EA; (b) when prepared from fish acclimated at 0°C compared to at 10°C and stored at 0°C or - 3°C with respect to EP, EA, FD, AA. Negligible changes in pH, TMA and DMA occurred during 21 days storage at either temperature. TMAO decreased more during storage at-3°C than at 0°C.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-4514.1987.tb00113.x
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  • 8
    Electronic Resource
    Electronic Resource
    Accelerated Cheddar Cheese Ripening with an Aminopeptidase Fraction from Squid Hepatopancreas (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 67 (2002), 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 aminopeptidase (AP) fraction from squid (Illex illecebrosus) hepatopancreas was added to Cheddar cheese at 2 levels, and its influence on ripening indices was determined for up to 3-mo storage at 11 °C. Two commercial enzymes (Neutrase ® and Flavourzyme ®) were similarly tested. Cheese with the higher level of squid AP contained more soluble N, amino acids, and Cheddar flavor after 1 mo, but it developed defects in texture and bitterness as ripening progressed. Cheese with less squid AP did not differ from the control with respect to all ripening indices over 3-mo storage. Ripening Cheddar contains cysteine protease inhibitor(s) that inhibit low levels of squid AP but not Neutrase ® and Flavourzyme ®.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.2002.tb09429.x
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  • 9
    Electronic Resource
    Electronic Resource
    Properties of Trypsin from the Pyloric Ceca of Atlantic Cod (Gadus morhua) (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: Trypsin (EC 3.4.21.4) was isolated from the pyloric ceca of Atlantic cod and purified to homogeneity by affinity chromatography. The enzyme catalyzed the hydrolysis of benzoyl arginine p-nitroanilide (BAPA, pH 8.2 and 25°C) such that Vmax was 250 BAPA units per micromole trypsin and Km was 1.48 mM. For the hydrolysis of tosyl arginine methyl ester (TAME, pH 8.1 and 25°C), Vmax was 18.2 × 103 TAME units/micromole trypsin, and Km 0.22 mM. The pH and temperature optima with BAPA substrate were 7.5 and 40°C, respectively. Atlantic cod trypsin was most active and stable at alkaline pH. The enzyme was heat labile, losing more than 50% of its activity after incubation at 50°C for 30 min. Amino acid analysis of Atlantic cod trypsin revealed that the enzyme was rich in residues such as serine, glycine, glutamate and aspartate, but poor in basic amino acid residues compared to trypsins from warm blooded animals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1990.tb01574.x
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  • 10
    Electronic Resource
    Electronic Resource
    Isolation and characterization of pepsin from polar cod (Boreogadus saida)
    Amsterdam : Elsevier
    Comparative Biochemistry and Physiology -- Part B: Biochemistry and 80 (1985), S. 467-473 
    Details
    ISSN: 0305-0491
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0305-0491(85)90274-3
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