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A history of lameness is associated with reduced proportions of collagen type I relative to type III in the digital cushions of dairy cattle
(Elsevier B.V., 2025-12) Wilson JP; Green MJ; Randall LV; Huxley JN; Alibhai A; Ferguson HJ; Rutland CS
Hoof horn lesions (HHL) are a highly prevalent and recurrent causes of lameness in dairy cattle globally. The digital cushion is composed of 3 cylinders of adipose tissue embedded in a system of collagenous connective tissue, which are designed to reduce the risk of HHL onset. Previous research has identified that animals with a history of lameness and HHL are more likely to have a reduced digital cushion volume in their lateral digits, but the impact on the histological structure remains unknown. Collagen is an important fibril related to adipose tissue structure and function, but its role in the digital cushion is poorly understood. Our study aimed to examine the proportions of type I and type III collagen within the digital cushions of dairy cattle at cull, and to investigate associations with digital cushion volume, lameness, and HHL occurrence throughout the animal's life. This retrospective cohort study resulted in 599 digital cushions being dissected from the hind feet of 54 animals. Digital cushion tissue underwent picrosirius red staining, combined with systematic random sampling and collagen content analysis. The results described the relative proportions of type I and type III collagen. The proportion of type I collagen was used as the outcome variable in multivariable linear regression models. The median (minimum–maximum) proportion of collagen that was type I contained within the lateral and medial digits was 56.2% (23.6%–83.8%) and 59.6% (13.3%–92.7%) respectively. The proportion of type I collagen was lower in animals that had a history of HHL and lameness throughout their lives. Animals with a lower BCS at cull or that were culled at a later parity had less type I collagen in their lateral digits at cull. Animals with a higher digital cushion volume also had an increased proportion of type I collagen in their lateral digits at cull. Our results have highlighted the histological impact that HHL have on the structure of the digital cushion. We hypothesized that localized inflammation associated with HHL was associated with a remodeling of the adipose tissue within the digital cushion, which would predispose the individual to a future of lameness and HHL.
Insights into the pathogenesis of catastrophic spontaneous humeral fractures in first-lactation dairy cows
(CSIRO Publishing, Australia, 2025-05-06) Wehrle-Martinez AS; Lawrence KE; Back PJ; Rogers CW; Gibson MJ; Dittmer KE; Eastwood C
Spontaneous humeral fractures in first-lactation dairy cows have introduced significant challenges to the dairy industry in New Zealand, impacting animal welfare, farm economics, and veterinary practices. This review synthesizes current knowledge on the pathogenesis of these fractures and identifies potential key risk factors. The majority of bones from affected first-lactation dairy cows have osteoporosis, which is associated with inadequate bone formation and increased bone resorption. In addition, low total collagen content in bones from most affected dairy cows supports the hypothesis that inadequate bone formation is an important risk factor associated with humeral fractures in these cows. Spectroscopic analyses further confirmed a significant reduction in bone quality and strength. Novel findings suggest that low liver copper concentration in many of the affected cows' results from the mobilisation of copper to the bone. Although limited, the accumulated evidence suggests that to mitigate the incidence of catastrophic fractures, adequate nutrition (especially protein-energy) should be supplied during important growth periods. While significant progress has been made in understanding the cause of these fractures, many uncertainties and areas requiring further research remain.
Sous vide processing to tenderise meat : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Food Technology at Massey University, Palmerston North, New Zealand
(Massey University, 2024-12-03) Akmal, Noorul Faridatul
The development of meat tenderness during sous vide cooking is associated with the proteolysis of meat proteins by endogenous enzymes, such as cathepsins B and L, and collagen solubilisation. However, these two processes are optimal at different temperature regimes. The aim of this thesis was to evaluate the effect of combining both temperature regimes through two-stage sous vide cooking on meat tenderness and cooking loss, as well as its ability to reduce total cooking time compared to conventional single-temperature sous vide cooking. This thesis also aimed to determine the roles of cathepsin B and L, collagen denaturation, and collagen solubilisation in the development of meat tenderness. Data for this thesis were obtained using beef pectoralis profundus (brisket), which is a tough meat cut that has the potential to gain tenderness through sous vide cooking. In this thesis, the kinetics of cathepsin B and L activity during sous vide cooking of beef brisket were evaluated at the temperatures of 46 – 60 °C for up to 72 h. Their activity initially increased, then decreased with longer cooking time. These changes in cathepsin B and L activity were successfully modeled using consecutive reactions in series, which are activation (the release of cathepsin from lysosomes) followed by deactivation (thermal denaturation). The model allows for the calculation of the cumulative activity of cathepsins for a given temperature and time. It was found that a greater cumulative activity can be achieved by sous vide cooking at lower temperatures such as 46 °C for a prolonged time compared to a higher temperature such as 56 °C. To evaluate the effect of precooking at different cumulative cathepsin B and L activities on meat tenderness, cooking loss, and collagen solubilisation, beef brisket was precooked at the temperatures of 46 °C and 56 °C for up to 72 h, followed by cooking at 71 °C. No change in the shear force value of meat precooked at 46 °C was observed, while a decrease in the shear force value was noted in meat precooked at 56 °C with increasing cooking time. Meat precooked at 56 °C also showed higher collagen solubilisation than meat precooked at 46 °C, while no difference in cooking loss was observed between the two precooking temperatures. From this work it was concluded that higher cumulative cathepsin B and L activity did not result in tenderisation of meat indicating that cathepsin B and L do not contribute to the development of tenderness in tough meat cuts like brisket. On the other hand, meat tenderness appears to be correlated with collagen solubilisation. A further study using precooking at different cumulative activities (46 – 56 °C for 0 – 12 h), followed by cooking at 80 °C for 8 h, supports the result that cathepsins B and L do not contribute to meat tenderisation during sous vide cooking. In this study, beef brisket precooked at 46, 50, and 53 °C for 12 h and at 56 °C for 6 and 12 h had a lower shear force value than meat cooked directly at 80 °C for 8 h. Faster tenderisation was observed as early as 6 h with precooking at 56 °C. Sous vide cooking at 56 °C for 6 and 12 h was characterised by lower cumulative cathepsin B and L activity, a higher degree of collagen denaturation, and a marked decrease in final yield force compared to other temperature-time combinations. The kinetics of collagen denaturation in sous vide-cooked beef brisket were also determined in this thesis, using the enthalpy of denaturation (∆H) of the second peak (Peak 2) from the thermogram generated by differential scanning calorimetry (DSC). The change in the ∆H of Peak 2 was successfully modeled using a three-protein model. The simulation of collagen denaturation using kinetic parameters obtained from the model showed a marked increase in collagen denaturation at 56 °C. A further study using precooking at 56 °C for 6 h, followed by cooking at various second-stage temperature-time combinations (60, 70, 80, and 90 °C for 0 – 20 h), showed that two-stage sous vide cooking could not reduce the total cooking time to tenderise meat compared to conventional single-temperature sous vide cooking. Based on conventional single-temperature sous vide cooking, the time required for beef brisket to reach the shear force correlated with the consumer tenderness threshold (Liang et al., 2016) was determined. It was found that at 60, 70, 80, and 90 °C, the times required to achieve the consumer tenderness threshold were 20, 26, 12, and 8 h, respectively. Although shorter times were needed to achieve the consumer tenderness threshold at 80 and 90 °C, these temperatures resulted in significantly higher cooking loss compared to 60 °C.
Gelatin and Collagen from Sheepskin.
(MDPI (Basel, Switzerland), 2024-05-31) Matinong AME; Pickering KL; Waterland MR; Chisti Y; Haverkamp RG; Yu L; Popa M
Abattoirs dispose of sheepskins as solid waste due to low price and poor demand for sheepskin leather. In principle, as an alternative to being disposed of in landfill, sheepskins can serve as a source of the protein collagen or the hydrolysis product, gelatin. In this research, sheepskins collected from abattoirs were used as a source of collagen. Three extraction methods were compared: acid extraction, acid with enzymes, and alkali extraction. The extracted material was characterized using scanning electron microscopy (SEM) and Fourier-transform infrared spectroscopy (FTIR), small angle X-ray scattering (SAXS), and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The collagen and gelatin extraction yield ranged from 3.1% to 4.8% with the product purity determined by hydroxyproline, ranging from 7.8% for the alkali process to 59% and 68% for the acid and acid-enzyme processes. SDS PAGE showed that the acid process produced fragments with molecular weights in the range 100 to >250 kDa, while acid-enzyme resulted in smaller fragments, below 30 kDa. The FTIR region of the amide I band at 1800-1550 cm-1, which was used as an indicator of the collagen and gelatin content, showed that the gelatin dominated in the acid extracts, and the alkaline extract contained a large portion of keratin. SAXS was found to be a sensitive method for showing the presence of intact collagen fibrils in materials from all of the extraction methods, albeit at low concentrations. Herein, sheepskin is shown to be a useful source for collagen-gelatin material of varying molecular weights.
Impact of Gut Recolonization on Liver Regeneration: Hepatic Matrisome Gene Expression after Partial Hepatectomy in Mice.
(MDPI (Basel, Switzerland), 2023-06-28) Amin AR; Hairulhisyam NM; Aqilah RNF; Nur Fariha MM; Mallard BL; Shanahan F; Wheatley AM; Marlini M; Neuman M; Malnick S
The hepatic matrisome is involved in the remodeling phase of liver regeneration. As the gut microbiota has been implicated in liver regeneration, we investigated its role in liver regeneration focusing on gene expression of the hepatic matrisome after partial hepatectomy (PHx) in germ-free (GF) mice, and in GF mice reconstituted with normal gut microbiota (XGF). Liver mass restoration, hepatocyte proliferation, and immune response were assessed following 70% PHx. Hepatic matrisome and collagen gene expression were also analyzed. Reduced liver weight/body weight ratio, mitotic count, and hepatocyte proliferative index at 72 h post PHx in GF mice were preceded by reduced expression of cytokine receptor genes Tnfrsf1a and Il6ra, and Hgf gene at 3 h post PHx. In XGF mice, these indices were significantly higher than in GF mice, and similar to that of control mice, indicating normal liver regeneration. Differentially expressed genes (DEGs) of the matrisome were lower in GF compared to XGF mice at both 3 h and 72 h post PHx. GF mice also demonstrated lower collagen expression, with significantly lower expression of Col1a1, Col1a2, Col5a1, and Col6a2 compared to WT mice at 72 h post PHx. In conclusion, enhanced liver regeneration and matrisome expression in XGF mice suggests that interaction of the gut microbiota and matrisome may play a significant role in the regulation of hepatic remodeling during the regenerative process.
In Vitro Assessment of Hydrolysed Collagen Fermentation Using Domestic Cat (Felis catus) Faecal Inocula
(MDPI (Basel, Switzerland), 2022-02-17) Butowski CF; Thomas DG; Cave NJ; Bermingham EN; Rosendale DI; Hea S-Y; Stoklosinski HM; Young W; Ebani VV
The gastrointestinal microbiome has a range of roles in the host, including the production of beneficial fermentation end products such as butyrate, which are typically associated with fermentation of plant fibres. However, domestic cats are obligate carnivores and do not require carbohydrates. It has been hypothesised that in the wild, collagenous parts of prey-the so-called animal-derived fermentable substrates (ADFS) such as tendons and cartilage-may be fermented by the cat's gastrointestinal microbiome. However, little research has been conducted on ADFS in the domestic cat. Faecal inoculum was obtained from domestic cats either consuming a high carbohydrate (protein:fat:carbohydrate ratio of 35:20:28 (% dry matter basis)) or high protein (protein:fat:carbohydrate ratio of 75:19:1 (% dry matter basis)) diet. ADFS (hydrolysed collagen, cat hair, and cartilage) were used in a series of static in vitro digestions and fermentations. Concentrations of organic acids and ammonia were measured after 24 h of fermentation, and the culture community of microbes was characterised. The type of inoculum used affected the fermentation profile produced by the ADFS. Butyrate concentrations were highest when hydrolysed collagen was fermented with high protein inoculum (p < 0.05). In contrast, butyrate was not detectable when hydrolysed collagen was fermented in high carbohydrate inoculum (p < 0.05). The microbiome of the domestic cat may be able to ferment ADFS to provide beneficial concentrations of butyrate.
Novel collagen-based wafers as a drug delivery method for local analgesia in deer antlers : a thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Veterinary Sciences at Massey University, Manawatu, New Zealand
(Massey University, 2021) Sahebjam, Farzin
Introduction This study provided a practical and novel solution for post-operative pain mitigation and wound management after velvet antler removal in red deer (Cervus elaphus). Currently, there are no topical methods to mitigate pain for an extended period of time in deer following surgical removal of antlers. The current methods licensed in New Zealand provide only peri-operative analgesia with short-term effects and raise animal welfare concerns about whether animals are still in pain when the effect has worn off, especially in the deer industry in which a large number of animals are being managed. Materials and methods In vitro study: In vitro drug release test (IVDRT) was conducted using the Franz diffusion cell to assess the drug release rates of lidocaine and bupivacaine in two different phases of the pilot and main studies. The pilot in vitro study contained 9 treatment groups and 3 control groups (n=3), which were classified based on collagen extraction technique, whether modified with zinc oxide-polyvinylpyrrolidone (ZnO-PVP) nanoparticles and the difference in the order of adding local anaesthetics and ZnO-PVP nanoparticles. The main in vitro study was comprised of 4 treatment groups of 5%, 10%, and 25% ZnO-PVP nanoparticles (n=6) proportional to dry collagen weight and a control group. In both pilot and main in vitro studies, the samples were taken every 15 minutes in the first hour and every 2 hours up to 12 hours. LC-MS and HPLC were used for the quantification of the samples in the pilot and main in vitro studies, respectively. MNT validation study: Forty male deer (stags) were assigned for the MNT validation study on three alternative days. A handheld algometer (Wagner FPX50) was used for mechanical nociceptive threshold (MNT) assessment of four antler sites (cranial, medial, caudal, lateral) in both right and left antlers. Animal body weight (kg) and antler length (cm) were recorded to investigate the correlation with MNT. The MNT readings from three days were compared with each other. In addition, the MNT reading from all four antler sites and the right and left antlers were compared with each other. In vivo study: Eighteen stags sorted into three groups of 6 animals in each (2 treatment groups and 1 control group) for the pilot in vivo study, and forty yearling age stags assorted into four groups of 10 animals (three treatments and one control), were used in the main in vivo study. All animals had both antlers removed after administration of local anaesthesia. The control group in both pilot and main in vivo studies received a ring block of 4% articaine hydrochloride only, whilst the treatment groups received modified (with ZnO-PVP) or non-modified collagen composite wafers to the wound sites. The modified collagen composite wafers had 50% ZnO-PVP for the pilot in vivo study and had 0%, 5% or 25% ZnO-PVP proportional to dry collagen weight for the main in vivo study. A handheld algometer (Wagner FPX50), was used for mechanical nociceptive threshold (MNT) assessment at different time points (0, 4, 24, 72 hrs, 7 days and 14 days). Thermal imaging with a forward-looking infrared (FLIR) camera was performed for the detection of temperature differences between the groups. Digital photography of the wounds was performed for further quantitative wound healing analysis. Pharmacokinetic study: Blood samples were drawn from deer after the application of collagen composite wafers at time points t0, t1, t2, t4, t6, t8, t12, and t24 hours for the pilot study and at time points t0, t1, t2, t4, t6, t8, and t24 hours for the main in vivo study. The plasma was iv analysed with LC-MS to calculate pharmacokinetic parameters with the non-compartmental method such as Cmax, Tmax, AUC, AUMC, half-life, the volume of distribution and clearance. Statistical analysis: Higuchi model was mainly incorporated to calculate drug release rates for the in vitro studies. For in vivo studies, the statistical analyses were performed with a linear model for repeated measurements that accounted for the fixed effects of day, antler, location within antler or antler sites, antler length and weight of deer as covariates, and the random effect of animals. Results IVDRT did not show any statistically significant difference between the treatment groups; however, the treatment groups had significantly slower release compared to the control group in the pilot in vitro study. IVDRT in the main in vitro study showed the slowest release rate in the treatment group with 25% ZnO-PVP compared to the other groups for both lidocaine and bupivacaine. The control group had the most rapid drug release rates compared to the treatment groups, particularly for lidocaine. Furthermore, lidocaine showed a considerably slower release compared to bupivacaine when zinc oxide nanoparticles were incorporated, and the results significantly differed. MNT validation results showed that antler length (cm) and animal body weight (kg) are directly and positively correlated with the baseline MNT readings. The MNT readings from four sites of antlers, including cranial, medial, caudal and lateral aspects, did not have any significant difference from each other. In addition, the MNT readings from the right and left antlers did not show any significant difference from each other. In vivo results in the pilot study showed a lack of collagen composite wafer adherence for the non-modified wafers (PT2) and 50% adherence for the modified wafers (PT1) in the pilot study. As a result of the main in vivo study, 90%, 70%, and 45% were in group 25%NP (T1), 5%NP (T2), and 0%NP (T3) to the wounds, respectively. A significant difference was observed in the recovery rates of PT1 compared to the control group (P<0.0001) for the pilot study. For the main in vivo study, all three treatment groups also showed a significant difference compared to each other: T1 vs. T2 (P<0.01), T1 vs. T3 (P<0.05), and T2 vs. T3 (P<0.0001). In addition, the treatment groups showed a significantly slower recovery rate from analgesia compared to the control group (P<0.0001 for all). All the treatment groups in the main study demonstrated analgesia beyond 6 hrs and up to 10 hrs. The pharmacokinetics study showed significantly smaller Cmax for T1 and T2 compared to T3 only for bupivacaine. Tmax showed significantly smaller values for T1 compared to T2 for only bupivacaine. Both AUC (0-24), AUC (0-∞), and AUMC (0-∞) showed smaller values for T1 and T2 compared to T3. Conclusion The physically modified collagen composite wafer with zinc oxide-PVP nanoparticles, containing a short-acting (lidocaine) and a long-acting (bupivacaine) local anaesthetic, is a novel method to sustain drug delivery of local anaesthetics after the surgical removal of velvet antlers. Our suggested treatment can deliver analgesia to the wounded antler for up to 10 hours and is a safe and convenient method to use by farmers in the deer industry. Furthermore, the collagen wafer is very adhesive to the wound and can help facilitate wound healing of deer antlers.
Relative orientation of collagen molecules within a fibril: A homology model for homo sapiens type I collagen.
(Taylor & Francis, 30/01/2018) Collier TA; Nash A; Birch HL; de Leeuw NH
Type I collagen is an essential extracellular protein that plays an important structural role in tissues that require high tensile strength. However, owing to the molecule’s size, to date no experimental structural data are available for the Homo sapiens species. Therefore, there is a real need to develop a reliable homology model and a method to study the packing of the collagen molecules within the fibril. Through the use of the homology model and implementation of a novel simulation technique, we have ascertained the orientations of the collagen molecules within a fibril, which is currently below the resolution limit of experimental techniques. The longitudinal orientation of collagen molecules within a fibril has a significant effect on the mechanical and biological properties of the fibril, owing to the different amino acid side-chains available at the interface between the molecules.
Collagen Extraction from Animal Skin
(MDPI (Basel, Switzerland), 13/06/2022) Matinong AME; Chisti Y; Pickering KL; Haverkamp RG
Collagen is the most abundant structural protein in animals. It is the major component of skin. It finds uses in cosmetics, medicine, yarn production and packaging. This paper reviews the extraction of collagen from hides of most consumed animals for meat with the focus on literature published since 2000. The different pretreatment and extraction techniques that have been investigated for producing collagen from animal skins are reviewed. Pretreatment by enzymatic, acid or alkaline methods have been used. Extraction by chemical hydrolysis, salt solubilization, enzymatic hydrolysis, ultrasound assisted extraction and other methods are described. Post-extraction purification methods are also explained. This compilation will be useful for anyone wishing to use collagen as a resource and wanting to further improve the extraction and purification methods.
Novel Assessment of Collagen and Its Crosslink Content in the Humerus from Primiparous Dairy Cows with Spontaneous Humeral Fractures Due to Osteoporosis from New Zealand.
(23/09/2022) Wehrle-Martinez A; Naffa R; Back P; Rogers CW; Lawrence K; Loo T; Sutherland-Smith A; Dittmer K
Numerous cases of spontaneous humeral fracture in primiparous dairy cows from New Zealand have prompted the study of the condition to establish probable causes or risk factors associated with the condition. Previous studies identified inadequate protein-calorie malnutrition as an important contributory factor. Earlier case studies also reported that ~50% of cows have low liver and/or serum copper concentration at the time of humeral fracture. Because copper is so closely associated with the formation of collagen cross-links, the aim of this study was to compare collagen and collagen crosslink content in the humerus from primiparous cows with and without humeral fractures and to determine the role of copper in the occurrence of these fractures. Humeri were collected from cows with and without humeral fractures, ground, and the collagen and collagen cross-link content measured using high-performance liquid chromatography. Collagen content was significantly higher in the humeri of cows without humeral fractures, while total collagen crosslink content was significantly higher in the humerus of cows with humeral fractures. These results indicate other factor/s (e.g., protein-calorie undernutrition) might be more important than the copper status in the occurrence of humeral fractures in dairy cows in New Zealand.

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