BIOCHEMICAL CHARACTERIZATION OF LEG AND BREAST MUSCLE OF QUAIL
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Date
2006
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Birsa Agricultural University, Kanke, Ranchi, Jharkhand
Abstract
Quail 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
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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.
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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
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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 suggested
Description
BIOCHEMICAL CHARACTERIZATION OF LEG AND BREAST MUSCLE OF QUAIL
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