BIOCHEMICAL CHARACTERIZATION OF LEG AND BREAST MUSCLE OF QUAIL

dc.contributor.advisorPrasad, R. L. Prasad
dc.contributor.authorThakur, Raman Kumar
dc.date.accessioned2017-08-19T11:12:32Z
dc.date.available2017-08-19T11:12:32Z
dc.date.issued2006
dc.descriptionBIOCHEMICAL CHARACTERIZATION OF LEG AND BREAST MUSCLE OF QUAILen_US
dc.description.abstractQuail being a new species introduced into meat industries, the physicochemical characteristics and biochemical constituents of muscle with view to study molecular characteristics, besides tenderness of meat were undertaken. Leg and breast muscle were selected during the present investigation. Among the physicochemical characteristics, pH of meat play important role in maintaining the quality of meat which is influenced by glycogen content. The pH of meat decreases with increase in the age. The female had higher pH value as compared to male. The leg and breast muscle of quail also had significant difference in pH value. All these findings are in close association with tenderness of muscle which suggests that as the pH of meat falls, tenderness decreases. Glycogen content and amount of lactic acid of the muscle is also in agreement with the finding of pH. Glycogen content was lower in female as compared to male while lactic acid increased with advancement of age. Lactic acid was higher for breast muscle than leg muscle. The water holding capacity significantly decreased with increase in the age of the quail. Breast muscle always had higher WHC as compared to leg muscle in both male and female. This finding is in positive correlation with the finding on sensory Abstract 2 parameters of meat (juiciness) which decreased with age and was higher for breast muscle. The muscle fiber diameter appears to be increased from 5 week to 8 week and it was almost constant after 8 week of age. Male had slight higher MFD than female. The leg muscle had always higher MFD than breast muscle in both male and female at all ages. Hydroxyproline content of the muscle increased with advancement in the age. It was higher in leg muscle as compared to breast muscle. Amount of hydroxyproline increased with the age of the quail which is in correlation with decreased tenderness of the muscle with age. Breast muscle also had lower hydroxyproline content and higher tenderness value as compared to leg muscle. The amount of total protein remained almost constant in leg and breast muscle in both male and female at all ages. High total protein content observed in quail as compared to other species viz. poultry. Organolaptic evaluation revealed slight detoriation in colour, flavour, tenderness, juiciness and overall acceptability with advancement of age. Broiler quail (5 week) had higher overall acceptability indicating suitable for marketing and in meat industries. Breast muscle had higher score for tenderness, juiciness and overall acceptability as compared to leg muscle. Abstract 3 The resolution of sarcoplasmic protein into subunit components on SDS-PAGE showed the presence of enzymes and metalloproteins. Band 1 and 2 from top of gel with molecular weight 178 kDa and 116 kDa remained unidentified. Band 3 with molecular weight 92 kDa was identified as phosphorylase B. Phosphorylase B kinase was identified in Band 4 with molecular weight 78 kDa. Band 5 was identified as AMP deaminase and phosphoglucoisomerase with molecular weight 63 kDa. Band 6 was identified as pyruvate kinase with molecular weight 50 kDa. Phosphoglycerate kinase with molecular weight 44 kDa was identified in Band 7. Band 8 was identified as enolase with molecular weight 41 kDa. Band 9 was identified as creatin phosphokinase and aldolase with molecular weight 37 kDa. Band 10 had molecular weight 32 kDa and it was identified as lactic dehydrogenase and glyceraldehydes phosphate dehydrogenase. Band 11 and 12 with molecular weight 29 kDa and 25 kDa were identified as triosephosphate isomerase and phosphoglycerate mutase. Band 13 with molecular weight 19 kDa was identified as myoglobin. The resolution of myofibrillar protein on SDS slab gel PAGE revealed the presence of myosin heavy chain and M-protein with molecular weight 178 kDa in Band 1. Band 2 was identified as Cprotein with molecular weight 115 kDa. Band 3 and 4 with molecular weight 86 kDa and 81 kDa were identified as α-actinin. Band 5 with Abstract 4 molecular weight of 48 kDa remained unidentified. Band 6 was identified as actin with molecular weight 38 kDa. Troponin-T and tropomyosin was identified in Band 7 with molecular weight 34 kDa. Band 8 with molecular weight 27 kDa was identified as troponin-I and myosin light chain I. Band 9 with molecular weight 21 kDa remained unidentified. Band 10 was identified troponin-C and myosin light chain II while Band 11 was identified as myosin light chain III with molecular weight 14 kDa. Quail meat is suitable for marketing for human consumption from 5 weeks onwards up to 8 weeks. There is slight detoriation in the quality of meat at 20 weeks of age due to increase in connective tissue which decrease the tenderness of meat, but it can be overcome by properly processing (tenderization) it. Quail meat having higher total protein content is superior to other species viz. poultry. The overall quality of breast meat was better than leg muscle in both male and female at all ages. Further work on lipid profile of quail muscle/meat is suggesteden_US
dc.identifier.urihttp://krishikosh.egranth.ac.in/handle/1/5810029139
dc.keywordsBIOCHEMICAL CHARACTERIZATION OF LEG AND BREAST MUSCLE OF QUAILen_US
dc.language.isoen_USen_US
dc.pages89en_US
dc.publisherBirsa Agricultural University, Kanke, Ranchi, Jharkhanden_US
dc.subVeterinary Biochemistry
dc.subjectnullen_US
dc.themeBIOCHEMICAL CHARACTERIZATION OF LEG AND BREAST MUSCLE OF QUAILen_US
dc.these.typeM.V.Sc.
dc.titleBIOCHEMICAL CHARACTERIZATION OF LEG AND BREAST MUSCLE OF QUAILen_US
dc.typeThesisen_US
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