An analysis of the influence of various tenderising treatments on the tenderness of meat from Polish Holstein-Friesian bulls and the course of changes in collagen

Mikołajczak, Beata; Iwańska, E.; Spychaj, Anita; Danyluk, B.; Montowska, Magdalena; Grześ, B.; Banach, Joanna; Żywica, Ryszard; Pośpiech, E.

doi:10.1016/j.meatsci.2019.107906

Cited by 15 publications

(10 citation statements)

References 47 publications

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“…To the best of our knowledge, there is no previous study on pork proteoglycans. The present findings on proteoglycans fell within the range for beef LTL and BF ( Dubost et al, 2013 ; Mikołajczak et al, 2019 ; Stanton and Light, 1990 ), but they did not differ between pork LTL and BF in this study. In the present study, IMF content did not differ between muscles.…”

Section: Discussionsupporting

confidence: 49%

Collagen characteristics affect the texture of pork Longissimus and Biceps femoris

Warner

et al. 2022

Translational Animal Science

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Connective tissue is considered to influence the toughness of pork, but most studies on connective tissue focus on the loin muscle. Cooking loss, Warner-Bratzler shear force (WBSF), texture profile analysis (hardness, springiness, chewiness, resilience and cohesiveness), total and insoluble collagen content, the percentage of type III collagen relative to the total of type I and III collagen, proteoglycan content and intramuscular fat (IMF) content were measured for pork Biceps femoris (BF) and Longissimus thoracis et lumborum (LTL) and Pearson’s correlation was performed. The results showed that BF had higher WBSF, resilience, total and insoluble collagen content than LTL (P<0.05). When considering both muscles, total and insoluble collagen content were positively correlated (P<0.05) with WBSF (r = 0.47 and 0.49, respectively), hardness (r = 0.49 and 0.50, respectively), cohesiveness (r = 0.50 and 0.50, respectively), chewiness (r = 0.58 and 0.59, respectively) and resilience (r = 0.63 and 0.63, respectively). The percentage of type III collagen content was negatively correlated (P<0.05) with WBSF (r = -0.68) and hardness (r = -0.58). Collagen content was correlated (P<0.05) with WBSF (r = 0.75) and hardness (r = 0.61) in LTL and with cohesiveness and resilience in BF. Collagen characteristics differ between muscles and contribute to pork texture in both LTL and BF.

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Section: Discussionsupporting

confidence: 49%

Collagen characteristics affect the texture of pork Longissimus and Biceps femoris

Warner

et al. 2022

Translational Animal Science

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“…However, soluble collagen and collagen solubility percentage were not affected by aging time ( p > 0.05, Table 3 ). The effect of aging on collagen solubility is controversial, as [ 44 ] found that post-mortem aging does not affect collagen content, while [ 55 ] reported that collagen is damaged and partially solubilized during aging.…”

Section: Resultsmentioning

confidence: 99%

Effects of Dietary Energy Density in a Fermented Total Mixed Ration Formulated with Different Ratios of Rice Straw and Cassava Pulp on 2- or 14-Day-Aged Meat Quality, Collagen, Fatty Acids, and Ribonucleotides of Native Thai Cattle Longissimus Muscle

Chaosap

Lukkananukool

Polyorach

et al. 2022

Foods

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This study investigated the effects of dietary energy density in rice straw and cassava pulp fermented total mixed ration on pH, cooking loss, Warner–Bratzler shear force (WBSF), and collagen content of 2- or 14-d-aged native Thai cattle (NTC) Longissimus thoracic (LT) muscles and fatty acids and ribonucleotides of 2-d-aged LT. Eighteen yearling NTC (Bos indicus) were randomly divided into three dietary treatments (T1 = 8.9, T2 = 9.7, and T3 = 10.5 MJ ME/kg), with six bulls per treatment. The results showed that T1 had the highest WBSF (p < 0.05). However, T2 had similar WBSF to T3 (p > 0.05). With aging, cooking loss increased (p < 0.01), while WBSF decreased (p < 0.01). Insoluble and total collagen decreased with aging (p < 0.05). Dietary energy density had no effect (p > 0.05) on collagen content, ribonucleotides and most fatty acids. However, T1 had more (p < 0.05) decanoic (C10:0), vaccenic (C18:1n9t), trans-linolelaidic (C18:2n6t), eicosatrienoic (C20:3n6), and docosadienoic (C22:2) acids than T2 and T3. In terms of lowest feed cost with comparable tenderness to T2 and highest energy density, T3 may be well suited for feeding NTC. Aging for 14 days improves LT tenderness, but its cooking loss may affect yield and juiciness.

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“…Hydroxyproline (Hyp) was measured using the colorimetric procedure 21 . Samples (10 g) were hydrolyzed with eightfold the volume of 3 mol L −1 H 2 SO 4 at 105 °C for 14 h and neutralized with 5.0 mol L −1 NaOH.…”

Section: Methodsmentioning

confidence: 99%

Assessment of gelatinolytic proteinases in chilled grass carp (Ctenopharyngodon idellus) fillets: characterization and contribution to texture softening

et al. 2021

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BACKGROUND Texture softening is always a problem during chilling of grass carp fillets. To solve this problem and provide for better quality of flesh, understanding the mechanism of softening is necessary. Gelatinolytic proteinases are suspected to play an essential role in the disintegration of collagen in softening of fish flesh. In the present study, the types and contribution of gelatinolytic proteinases in chilled fillets were investigated. RESULTS Four active bands (G1, 250 kDa; G2, 68 kDa; G3, 66 kDa; G4, 29 kDa) of gelatinolytic proteinases were identified in grass carp fillets by gelatin zymography. The effect of inhibitors and metal ions revealed that G1 was possibly a serine proteinase, G2 and G3 were calcium‐dependent metalloproteinases and G4 was a cysteine proteinase. The effect of the inhibitors phenylmethanesulfonyl fluoride (PMSF), l‐3‐carboxy‐trans‐2,3‐epoxy‐propionyl‐l‐leucine‐4‐guanidinobutylamide (E‐64) and 1,10‐phenanthroline (Phen) on chilled fillets revealed that gelatinolytic proteinase activities were significantly suppressed. Collagen solubility indicated that metalloproteinase and serine proteinase played critical roles in collagen breakdown during the first 3 days, and cysteine proteinase revealed its effect after 3 days. Meanwhile, during chilled storage for 11 days, the final values of shear force increased 19.68% and 24.33% in PMSF and E‐64 treatments when compared to control fillets respectively, whereas the increase after Phen treatment was 49.89%. CONCLUSION Our study concluded that the disintegration of collagen in post‐mortem softening of grass carp fillets was mainly mediated by metalloproteinase and to a lesser extent by serine proteinase and cysteine proteinase. © 2021 Society of Chemical Industry.

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An analysis of the influence of various tenderising treatments on the tenderness of meat from Polish Holstein-Friesian bulls and the course of changes in collagen

Cited by 15 publications

References 47 publications

Collagen characteristics affect the texture of pork Longissimus and Biceps femoris

Collagen characteristics affect the texture of pork Longissimus and Biceps femoris

Effects of Dietary Energy Density in a Fermented Total Mixed Ration Formulated with Different Ratios of Rice Straw and Cassava Pulp on 2- or 14-Day-Aged Meat Quality, Collagen, Fatty Acids, and Ribonucleotides of Native Thai Cattle Longissimus Muscle

Assessment of gelatinolytic proteinases in chilled grass carp (Ctenopharyngodon idellus) fillets: characterization and contribution to texture softening

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