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Dive into the research topics where Per Ertbjerg is active.

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Featured researches published by Per Ertbjerg.


Food Quality and Preference | 2003

Cooking loss and juiciness of pork in relation to raw meat quality and cooking procedure

Margit Dall Aaslyng; Camilla Bejerholm; Per Ertbjerg; Hanne Christine Bertram; Henrik J. Andersen

The study comprised two experiments with the aim to investigate the influence of raw meat quality and cooking procedure on cooking loss and juiciness of pork. The first experiment determined the cooking loss at 60, 70 and 80 °C centre temperature of 10 raw meat qualities (defined according to ultimate pH, drip loss, breed and rearing conditions) when cooked as steaks on a pan or as a roast in oven at a oven temperature of 90 or 190 °C. The differences in cooking loss between the raw meat qualities and the cooking procedures did decrease as the centre temperature increased and were almost negligble at 80 °C. Low water holding capacity (WHC) and low pH resulted in high cooking loss while no difference in cooking loss was observed between meat having medium or high WHC and pH. In the second experiment four raw meat qualities (standard, Duroc, low pH and heavy carcass weight) chosen from the first experiment to ensure a wide variation in cooking loss, were cooked in oven at 90 or 190 °C oven temperature. Juiciness was assessed three times during the chewing process. The results suggested that juiciness experienced initially in the chewing process depended only on the water content of the meat, whereas juiciness experienced later in the chewing process was determined by a combination of the water and intramuscular fat contents and the saliva production during chewing.


Animal Science | 2000

Long-term changes in performance and meat quality of Danish Landrace pigs: a study on a current compared with an unimproved genotype.

Niels Oksbjerg; J. S. Petersen; I. L. Sørensen; P. Henckel; Mogens Vestergaard; Per Ertbjerg; A. J. Møller; C. Bejerholm; S. Støier

An experiment was conducted in 1995 in order to examine muscle growth, muscle histochemical properties, muscle metabolism and meat quality of two types of Danish Landrace pigs representing the growth potential of years 1976 and 1995, respectively. Danish Landrace pigs representing 1976 (slow-growing, SG) originated from a breeding station where the population was maintained without being selected for production traits such as daily gain, food conversion ratio and meat content. Pigs representing Danish Landrace of 1995 (fast-growing, FG) were bought from certified Danish pig breeders. The pigs were simultaneously tested for performance from 40 to 95 kg live weight. The daily gain, food conversion ratio and meat content of the carcass were improved proportionately by 0·43, 0·24 and 0·03 in FG pigs compared with SG pigs. In m. longissimus dorsi (LD), the cross-sectional area of muscle fibres was smaller in FG pigs compared with SG pigs indicating increased muscle fibre number. Data further suggest increased satellite cell proliferation in muscles of FG pigs. Serum from FG pigs stimulated the proliferation of C2C12 muscle cells to a greater extent than serum from SG pigs, although the serum level of insulin-like growth factor 1 did not differ between pig types. The effect of serum on protein turn-over of C2C12 myotubes did not depend on pig type. The glycogen concentration in the LD did not differ significantly between pig types, while the activity of citrate synthase, 3-OH-acyl-CoA-dehydrogenase, and lactate dehydrogenase were higher in the LD of SG pigs compared with FG pigs. Pork chop colour of FG pigs was proportionately 0·09 lighter (L ⋆ ) and 0·13 less red (a ⋆ ) than pork chops of SG pigs. The total muscle pigment concentration in the LD, m. biceps femoris and m. vastus intermedius was proportionately reduced by 0·17, 0·19 and 0·11, respectively, in FG pigs compared with SG pigs. In the LD, the concentration of myoglobin was proportionately reduced by 0·17 in FG pigs. The chemical composition of the LD differed between pig types such that the water content was higher and protein content lower in LD from FG pigs compared with SG pigs. The pH of the LD measured 45 min and 24 h post mortem, drip loss and thawing loss were similar for both pig types. Meat tenderness of conditioned pork chops of FG pigs was slightly reduced in accordance with a decreased intensity of the 31 kDa peptide band and increased cooking loss. The present study suggests that increased muscle fibre number and rate of muscle DNA deposition (satellite cell proliferation) have contributed to the increased muscle growth as a result of selection for performance in pigs under Danish conditions. However, the increase in growth performance was accompanied by deterioration in muscle colour and slightly reduced tenderness.


Meat Science | 2011

Relationship between collagen characteristics, lipid content and raw and cooked texture of meat from young bulls of fifteen European breeds.

Mette Christensen; Per Ertbjerg; Sebastiana Failla; C. Sañudo; R. Ian Richardson; Geoff R. Nute; J.L. Olleta; B. Panea; P. Albertí; M. Juárez; Jean-François Hocquette; John L. Williams

Variations in texture were determined for 10 day aged raw and cooked Longissimus thoracis (LT) muscle from 436 bulls of 15 European cattle breeds slaughtered at an age of 13-16 months. Variations in texture were related to differences in pH 24 h post-mortem, sarcomere length, collagen characteristics and lipid content. The shear force of cooked meat samples varied from 43.8 to 67.4 N/cm². Simmental, Highland and Marchigiana cattle had the highest shear force values and Avileña-Negra Ibérica, Charolais, Casina and Pirenaica cattle had the lowest values. Cooked meat toughness showed a weak negative correlation to lipid content (P<0.001) but no correlation to collagen characteristics. Raw meat texture measured by compression correlated positively (P<0.001) with total and insoluble collagen. In conclusion, collagen characteristics showed correlation to raw meat texture but not to cooked meat toughness of LT muscle in European young bulls.


Animal Science | 2002

Compensatory growth response in pigs, muscle protein turn-over and meat texture: effects of restriction/realimentation period

Margrethe Therkildsen; B. Riis; Anders Karlsson; Lars Kristensen; Per Ertbjerg; P. P. Purslow; M. Dall Aaslyng; Niels Oksbjerg

The present experiment was designed to evaluate the effect of different time spans of ad libitum feeding of pigs prior to slaughter after a period of restricted feeding on performance and texture characteristics of the meat. Te n litters of five pigs (Duroc ✕ Landrace ✕ Large White crosses) were allocated to five feeding treatments (AA, R28A42, R43A27, R52A18 and R60A10) at the age of 70 days. AA-pigs were given ad libitum a concentrate diet from day 70 to slaughter at day 140 (approx. 100 kg live weight). R28A42, R43A27, R52A18 and R60A10 pigs were given food at a restricted level (0·6 of ad libitum) for 28, 43, 52 and 60 days, respectively, followed by ad libitum feeding for 42, 27, 18 and 10 days, respectively, until slaughter at day 140. All pigs that had been given food at a restricted level for a period (R28A42, R43A27, R52A18 and R60A10) showed a compensatory growth response in the subsequent ad libitum period. However, only pigs on ad libitum for a minimum of 27 days prior to slaughter (R28A42 and R43A27) had carcass weights and muscle mass similar to that of the control pigs (AA) at slaughter. The restricted feeding increased meat proportion, whereas the feeding strategies had no effect on technological meat quality traits (pH24, drip loss and CIE-colour traits: L*, a* and b*). During compensatory growth, protein turn-over was increased and positively related to the length of the ad libitum period as indicated by the concentration of elongation factor-2 (eEF-2) (P


Meat Science | 2008

In vitro study to evaluate the degradation of bovine muscle proteins post-mortem by proteasome and μ-calpain.

Malene Bergh Houbak; Per Ertbjerg; Margrethe Therkildsen

The degradation of bovine muscle proteins by proteasome and ubiquitous calpains was explored via 2D gel proteome analysis by inhibition of the physiological level of the proteases by specific inhibitors. The inhibition of the proteasome chymotrypsin- and trypsin-like activity results in the lack of degradation of several fragments of structural proteins such as actin, troponin T, myosin light chain and nebulin. In addition the degradation of several sarcoplasmatic proteins was eliminated when proteasome was inhibited. The inhibition of the ubiquitous calpain only resulted in minor changes in the degradation pattern, which might indicate that p94, which is not inhibited by calpastatin, is involved in the degradation post-mortem. The results of the present study indicate a sequential degradation of the structural proteins post-mortem, where calpain initiates the disruption and destabilisation of the myofibrillar structure, and thereby allows the proteasome to act.


Meat Science | 2011

Investigation on CAST, CAPN1 and CAPN3 porcine gene polymorphisms and expression in relation to post-mortem calpain activity in muscle and meat quality

Gabriele Gandolfi; Luigi Pomponio; Per Ertbjerg; Anders Karlsson; L. Nanni Costa; René Lametsch; V. Russo; R. Davoli

This study aimed to detect variability in CAST, CAPN1 and CAPN3 porcine genes and to investigate the effect of CAST and CAPN1 polymorphisms on the activity of native and autolyzed μ-calpain and m-calpain, measured from 1 to 72 h post-mortem in Longissimus dorsi (LD) muscle of 30 pigs. Effects of polymorphisms on meat quality parameter such as pH, color and drip loss were also evaluated. Samples carrying CAST EU137105:g.76,872AA genotype showed higher autolyzed μ-calpain activity 24 and 72 h post-mortem, as well as lower drip loss values. Expression of CAST, CAPN1 and CAPN3 was assessed in LD muscles divergent for shear force. Higher CAST and CAPN3 expression was found in LD with high shear force (P<0.2), confirming a direct role for calpastatin but not for calpain 3 in meat tenderization. In conclusion, CAST gene affected post-mortem activation time of calpain and drip loss.


Meat Science | 2011

Effect of prolonged heat treatment from 48°C to 63°C on toughness, cooking loss and color of pork

Line Christensen; Per Ertbjerg; Margit Dall Aaslyng; Mette Christensen

The effect of low temperature long time (LTLT) heat treatment at 48 °C, 53 °C, 58 °C, and 63 °C for T(c) (time to reach a core temperature equal to the water bath), T(c)+5h holding time, and T(c)+17h holding time was studied in Longissimus dorsi and Semitendinosus muscles from slaughter pigs and sows. Meat toughness (Warner-Bratzler Shear Force), cooking loss and color (Minolta L*a*b*-values) was measured and in the cooking loss the amount of heat-soluble collagen and activity of cathepsin B+L was determined. Decreasing shear force and increasing cooking loss during LTLT treatment was observed between 53 °C and 58 °C. Furthermore, increasing temperature from 53 °C to 58 °C and increasing time from T(c) to T(c)+17h increased the solubility of collagen. Residual activity of cathepsin B+L in LTLT treated pork was mainly affected by temperature, showing the highest activity at 58 °C and 63 °C.


Meat Science | 2010

Ageing of large cuts of beef loin in vacuum or high oxygen modified atmosphere--effect on shear force, calpain activity, desmin degradation and protein oxidation.

Gunilla Lindahl; Åsa Lagerstedt; Per Ertbjerg; Sabine Sampels; Kerstin Lundström

The aim was to investigate the effect of ageing large beef cuts directly in high oxygen modified atmosphere (MA) and how ageing time in vacuum influence meat quality when followed by retail packaging in high oxygen MA. Large cuts (10 cm long) of beef loin (LD) were aged for up to 25 days postmortem in different ageing systems at 4 degrees C. Ageing solely in high oxygen modified atmosphere (MA, 80% O(2)+20% CO(2)) for 5 or 10 days and ageing in vacuum for 5 or 15 days followed by high oxygen MA for 5 or 10 days were compared with ageing in vacuum for 5, 15 and 25 days. Warner-Bratzler shear force, purge and cooking losses, calpain activity and desmin and carbonyl contents were measured. Shear force decreased to the same level when ageing this large beef cut solely in high oxygen MA for 5 or 10 days as when ageing in vacuum. The activity of mu-calpain disappeared, the activity of m-calpain decreased and purge loss increased between 5 and 10 days, but cooking loss and the contents of desmin and carbonyls were unaffected. The ageing time in vacuum before packaging of this large beef cut in high oxygen MA did not affect the ultimate shear force. The m-calpain activity decreased and the content of carbonyls increased compared with solely in vacuum after 15 days of total ageing, but there was no difference in the content of desmin or cooking loss between these ageing systems at the same ageing time.


Meat Science | 2008

Evidence for post-mortem m-calpain autolysis in porcine muscle

Luigi Pomponio; René Lametsch; Anders Karlsson; Leonardo Nanni Costa; Alberto Grossi; Per Ertbjerg

The objective of the present work was to characterize changes in calpain activity in pork post-mortem. Samples from pig M. longissimus dorsi and M. semimembranosus were collected three days post-mortem from 75 animals and analyzed with casein zymography. The results indicated post-mortem autolysis of m-calpain as two m-calpain bands were observed on the zymogram gel. Use of M. longissimus dorsi from three pigs collected at different times during storage further confirmed post-mortem autolysis of m-calpain. The activity of the autolyzed form of m-calpain was detectable at day 3 and further increased at day 6. The results also showed a decrease in the non-autolyzed m-calpain activity during post-mortem storage. Collectively, these results suggest that m-calpain is active post-mortem in porcine muscles.


Meat Science | 2010

Influence of early pH decline on calpain activity in porcine muscle

Luigi Pomponio; Per Ertbjerg; Anders Karlsson; Leonardo Nanni Costa; René Lametsch

This study investigated the influence of post-mortem pH decline on calpain activity and myofibrillar degradation. From 80 pigs, 30 Longissimus dorsi (LD) muscles were selected on the basis of pH values at 3h post-mortem and classified into groups of 10 as fast, intermediate and slow pH decline. The rate of pH decline early post-mortem differed between the three groups, but the ultimate pH values were similar at 24h. Calpain activity and autolysis from 1 to 72h post-mortem were determined using casein zymography and studied in relation to myofibrillar fragmentation. Colour and drip loss were measured. A faster decrease in pH resulted in reduced level of mu-calpain activity and increased autolysis of the enzyme, and hence an earlier loss of activity due to activation of mu-calpain in muscles with a fast pH decline. Paralleling the mu-calpain activation in muscles with a fast pH decline a higher myofibril fragmentation at 24h post-mortem was observed, which was no longer evident in the later phase of the tenderization process. In conclusion, the rate of early pH decline influenced mu-calpain activity and the rate but not the extent of myofibrillar degradation, suggesting an early effect of proteolysis on myofibril fragmentation that is reduced during ageing due to an earlier exhaustion of mu-calpain activity.

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René Lametsch

University of Copenhagen

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Luigi Pomponio

University of Copenhagen

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Jean-François Hocquette

Institut national de la recherche agronomique

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C. Sañudo

University of Zaragoza

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P. Albertí

University of Zaragoza

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B. Panea

University of Zaragoza

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