Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle

Etherington, David J.; Taylor, Mark A.; Wakefield, Diane K.; Cousins, Anthony; Dransfield, Eric

doi:10.1016/0309-1740(90)90034-4

Cited by 55 publications

(23 citation statements)

References 17 publications

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“…Lysosomal enzymes were extracted according to the method of Etherington et al 30 A portion of ground muscle was homogenised with 50 mmol L −1 sodium acetate buffer, pH 5.0, containing 1 mmol L −1 EDTA and 2 mg mL −1 Triton X100 (1:4 w/v). The extract was stirred for 1 h at 4 • C and then centrifuged for 30 min at 10 000 × g. The supernatant was filtered to remove the debris and used as the source of enzymes.…”

Section: Extraction Of Lysosomal Enzymesmentioning

confidence: 99%

Influence of enrofloxacin administration on the proteolytic and antioxidant enzyme activities of raw and cooked turkey products

Carreras¹,

Castellari²,

Valero³

et al. 2005

J Sci Food Agric

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The objective of this study was to assess the effect of enrofloxacin administration with and without withdrawal period on the quality of fresh meat and cooked products from turkey breasts. Cathepsin B and L activities were inactivated by the thermal process but were not affected by the presence of enrofloxacin. The level of enrofloxacin in samples without withdrawal time was higher than the regulatory maximum residue limit (MRL). The antioxidant enzymes glutathione peroxidase (GSHPx) and catalase (CAT) were affected by both the thermal process and the antibiotic residues in cooked meat. In no cases were differences found in superoxide dismutase (SOD) activity, supporting the theory that this enzyme could play a major role in preventing lipid oxidation of cooked meat. Enrofloxacin residues could contribute to an increase in the oxidative stress produced by thermal processing, as can be deduced by the reduction in GSHPx and CAT activities.

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Section: Extraction Of Lysosomal Enzymesmentioning

confidence: 99%

Influence of enrofloxacin administration on the proteolytic and antioxidant enzyme activities of raw and cooked turkey products

Carreras¹,

Castellari²,

Valero³

et al. 2005

J Sci Food Agric

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“…Proteolytic enzymes are classified regarding their location: in lysosomes or in cytosol. Lysosomal and cytosol enzymes have been studied both in fresh meat and in various meat products [54][55][56][57][58][59][60].…”

Section: Proteolytic Enzymesmentioning

confidence: 99%

Manufacture of dry-cured ham: a review. Part 1. Biochemical changes during the technological process

Petrova

Aasen

Rustad

et al. 2015

Eur Food Res Technol

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various types of dry-cured ham are due to pig breed, feed of pigs, their weight and age, as well as differences in the production process. High-quality dry-cured hams, with a production length longer than 1 year, have distinct organoleptic characteristics: a rich, unique, and recognizable flavor and color in the range from rosy to maroon or brown red marbled with white fat. However, the sensorial, physical-chemical, aromatic, morphological, and textural characteristics of dry-cured ham vary significantly depending on the alterations in the technological process from producer to producer [1][2][3][4][5].The traditional technology for the production of dry-cured ham mainly consists of salting, postsalting (resting), and drying-ripening stages. In Northern Europe (Germany, Scandinavia), smoking is frequently applied. Salting and drying-ripening are the most important steps in the manufacture where the flavor of the final product is mainly formed.The duration of the postsalting and the drying-ripening stages varies depending on the type of dry-cured ham. The drying-ripening step lasts from 2-3 months to 2-3 years for the highest quality dry-cured hams. Increased time of ripening gives a higher degree of enzymatic degradation, contributing to taste and flavor of the final product and as a consequence of higher quality of dry-cured ham [6]. Shorter processing time allows faster production of drycured ham, but the quality characteristics will suffer. The technology for each particular kind of dry-cured ham is adjusted according to the desired priority: quality or high production capacity.During ripening, endogenous enzymes degrade proteins and lipids to amino and fatty acids correspondingly, which are mainly responsible for the flavor of dry-cured ham [7]. Free amino and fatty acids are further degraded and converted by enzymatic and chemical reactions, including oxidation, to volatile compounds. Free amino acids contribute Abstract Dry-cured ham is a traditional meat product highly appreciated by consumers. Production of dry-cured ham is a time-consuming process which varies between different ham types. There are many factors affecting the final characteristics of dry-cured ham. The quality of the raw material and the process conditions mainly influence the rate and the extent of biochemical reactions which are in turn responsible for the formation of specific flavor and texture. This review paper highlights the characteristics of the raw material, the enzymatic and chemical processes taking place during dry-cured ham manufacture and the compounds formed by these reactions. The rates of the enzymatic changes from fresh meat to the stage of final product are also described.

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“…This would be consistent with Etherington et al (1987), who suggested that the uniquely rapid conditioning rate of chicken muscle may involve speciesspecific differences in protease release, activation, and substrate susceptibility. Etherington et al (1990) later reported a 30% reduction in calpain II activity during storage of untreated chicken muscle.…”

Section: Methodsmentioning

confidence: 99%

“…Etherington et al (1990) reported that the activities of cathepsins B "-"Means within a column with no common superscript differ significantly (P < .05). fragmentation index = (residue weight/wet sample weight) x 1,000.…”

Section: Methodsmentioning

confidence: 99%

Biochemical and Structural Effects of Rigor Mortis-Accelerating Treatments in Broiler Pectoralis

et al. 1995

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This study was conducted to elucidate the mechanism of action of two selected rigor mortis-accelerating treatment systems employed in the prevention of the toughness associated with early-harvested (1 h post-mortem) broiler Pectoralis muscle. The treatments included 14 min of low voltage electrical stimulation (110 V, 1 A, pulsing 1 s on and 1 s off) combined with high temperature conditioning (39 C) and muscle tensioning (LV + HTC + MT); a 15-s high voltage stimulation (440 V, 1 A pulsing 2 s on and 1 s off) combined with muscle tensioning (HV + MT); and a control simulating commercial broiler processing practices. The rigor-accelerating treatments reduced pH and increased R-value (inosine:adenosine ratio) at 1 h post-mortem, but only the LV + HTC + MT treatment reduced sarcomere shortening. Both rigor treatments reduced the amount of measurable myofibrillar fragmentation. Cathepsin B and B + L activities were not affected by the rigor treatments. Calpain I activity was not detectable in any 24-h post-mortem sample. Calpain II activity at 24 h post-mortem was greater in muscles receiving HV + MT than from the LV + HTC + MT or control carcasses, but was reduced in all muscles by 24 h postmortem. An SDS-PAGE indicated a 30-kDa polypeptide that was absent at death and appeared in control and LV + HTC + MT muscles but to a lesser extent in HV + MT muscles. These results suggested that the LV + HTC + MT treatment has a greater tenderizing effect than the HV + MT treatment because the former achieves a better balance between reduced sarcomere shortening and myofibrillar fragmentation.

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Proteinase (Cathepsin B, D, L and Calpains) levels and conditioning rates in normal, electrically stimulated and high-ultimate-pH chicken muscle

Cited by 55 publications

References 17 publications

Influence of enrofloxacin administration on the proteolytic and antioxidant enzyme activities of raw and cooked turkey products

Influence of enrofloxacin administration on the proteolytic and antioxidant enzyme activities of raw and cooked turkey products

Manufacture of dry-cured ham: a review. Part 1. Biochemical changes during the technological process

Biochemical and Structural Effects of Rigor Mortis-Accelerating Treatments in Broiler Pectoralis

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