16
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: found
      • Article: not found

      Tenderization of Bovine Longissimus Dorsi Muscle using Aqueous Extract from Sarcodon aspratus

      research-article

      Read this article at

      ScienceOpenPublisherPMC
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Abstract

          The aim of this study was to investigate the effects of aqueous extract from Sarcodon aspratus on tenderization of the bovine longissimus dorsi muscles in comparison with commercial proteolytic enzymes. Furthermore, meat quality and muscle protein degradation were examined. We marinated meat with 2% Sarcodon aspratus extract, 2% kiwi extract, and 0.2% papain. Beef chunks (3×3×3 cm 3) were marinated with distilled water (control), Sarcodon aspratus extract (T1), kiwi extract (T2) or papain (T3) for 48 h at 4℃. There were no significant differences in muscle pH and lightness between control and treated samples. T1 had the lowest redness ( p<0.01), and higher cooking loss and water holding capacity than control and T2 ( p<0.05). T1 and T3 exhibited lower shear force values than control ( p<0.05). Total protein solubility did not differ significantly between T1 and control, but T1 had less myofibrillar protein solubility than control and T2 ( p<0.001). The degradation of myosin heavy chain in T1 and T3 was observed. This degradation of myofibrillar protein suggests that Sarcodon aspratus extract could influence tenderization. These results show that aqueous extract of Sarcodon aspratus extract actively affect the tenderness of the bovine longissimus dorsi muscle.

          Related collections

          Most cited references30

          • Record: found
          • Abstract: not found
          • Article: not found

          Determination of serum proteins by means of the biuret reaction.

            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            The relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity in porcine longissimus muscle.

            In order to investigate the relationship of sarcoplasmic and myofibrillar protein solubility to colour and water-holding capacity (WHC) in pork, 60 loins were selected to represent the quality classes: PSE (pale, soft, exudative), RSE (reddish-pink, soft, exudative), RFN (reddish-pink, firm, non-exudative) and DFD (dark, firm, dry). PSE samples exhibited lower (p<0.05) protein solubility (sarcoplasmic, myofibrillar and total) compared to the other quality classes. RSE samples exhibited lower (p<0.05) sarcoplasmic protein solubility compared to DFD samples. RSE, RFN and DFD samples had similar myofibrillar and total protein solubilities. Sarcoplasmic protein solubility explained 71% of the variation in lightness with a linear decrease in L* value. Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) gels of the sarcoplasmic and myofibrillar samples distinctly showed the association of some sarcoplasmic proteins with the myofibrillar protein fractions in PSE and RSE samples. The sarcoplasmic proteins which precipitated were phosphorylase, creatine kinase, triose phosphate isomerase and myokinase for PSE and phosphorylase for RSE samples. Pork colour is highly correlated with precipitation of sarcoplasmic proteins while WHC is affected by denaturation of myofibrillar proteins (PSE samples) and lower ultimate pH (PSE and RSE samples).
              Bookmark
              • Record: found
              • Abstract: found
              • Article: not found

              Correlations among selected pork quality traits.

              Establishing relationships among specific quality traits is important if significant progress toward developing improved pork quality is to be realized. As part of a study to examine the individual effects of genes on meat quality traits in pigs, a three-generation resource family was developed. Two Berkshire sires and nine Yorkshire dams were used to produce nine F1 litters. Sixty-five matings were made from the F1 litters to produce four sets of F2 offspring, for a total of 525 F2 animals used in the study. These F2 animals were slaughtered at a commercial facility upon reaching approximately 110 kg. Carcass composition traits, pH measurements, and subjective quality scores were made at 24 h postmortem. Loin samples (n = 525) were collected at 48 h postmortem, and meat quality traits were evaluated. These traits included pH (48 h), Hunter L-values, drip loss, glycolytic potential, ratio of type IIa/IIb myosin heavy chains (IIa/IIb), total lipid, instrumental measures of tenderness using the Star Probe attachment of the Instron, cook loss measurements, and sensory evaluations. Significant phenotypic correlations were found between many carcass, instrumental, and biochemical measurements, and sensory quality traits. Star Probe measurements were significantly correlated with drip loss (0.29), glycolytic potential (0.30), pH (-0.29), total lipid (-0.14), and Hunter L-values (0.28). Drip loss was significantly correlated with glycolytic potential (0.36), pH (-0.28), IIa/IIb (-0.10), and Hunter L-values (0.33). Hunter L-values were also significantly correlated with total lipid (0.33) and IIa/ IIb (-0.11). Sensory tenderness, flavor, and off-flavor scores were significantly correlated with drip loss, pH, and glycolytic potential measurements. Marbling score, total lipid, and drip loss were not significantly correlated with sensory juiciness scores, but cooking loss was. Marbling and total lipid were significantly correlated with firmness scores (0.37 and 0.31, respectively). Taken together, the data in this study suggest that changes in some meat quality traits can affect many other meat quality attributes. The correlations yield information that could aid in directing future studies aimed at understanding the underlying biological mechanisms behind the development of many quality traits.
                Bookmark

                Author and article information

                Journal
                Korean J Food Sci Anim Resour
                Korean J Food Sci Anim Resour
                ksfsar
                Korean Journal for Food Science of Animal Resources
                Korean Society for Food Science of Animal Resources
                1225-8563
                2234-246X
                2015
                31 August 2015
                : 35
                : 4
                : 533-540
                Affiliations
                [1] Division of Biotechnology, College of Applied Life Sciences, Jeju National University, Jeju 690-756, Korea
                [1 ] Department of Culinary & Food Service Management, Sejong University, Seoul 143-747, Korea
                [2 ] Department of Nutritional Science and Food Management, College of Health Science, Ewha Womans University, Seoul 120-750, Korea
                Author notes
                []These authors contributed equally to this work.
                [* ]Corresponding author: Youn-Chul Ryu, Department of Biotechnology, Jeju National University, Jeju 690-756, Korea. Tel: +82-64-754-3332, Fax: +82-64-725-2403, E-mail: ycryu@ 123456jejunu.ac.kr
                Article
                kosfa-35-533
                10.5851/kosfa.2015.35.4.533
                4662137
                f6067db4-95fc-4de3-8446-b73f53440f9a
                Copyright © 2015, Korean Society for Food Science of Animal Resources

                This is an open access article distributed under the terms of the Creative Commons Attribution Non-Commercial License ( http://creativecommons.org/licences/by-nc/4.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                : 06 May 2015
                : 23 July 2015
                : 23 July 2015
                Categories
                Article

                sarcodon aspratus,proteolytic enzymes,beef,tenderization

                Comments

                Comment on this article