Upload
others
View
30
Download
0
Embed Size (px)
Citation preview
Profa. dra. Édira Castello Branco de Andrade Gonçalves
http://www.unirio.br/analisedealimentos
Rigor mortis
http://www.unirio.br/analisedealimentos
http://faculty.southwest.tn.edu/rburkett/gb%201%20cell%20resp.htm
RESPIRATION
http://www.unirio.br/analisedealimentos
http://ib.bioninja.com.au/standard-level/topic-2-molecular-biology/28-cell-respiration/anaerobic-respiration.html
RESPIRATION
http://www.unirio.br/analisedealimentos
FERMENTATION
Myosin
http://physiologyonline.physiology.org/content/15/1/26
https://www.slideshare.net/suknamgoong/cell-bio7
MUSCLE CONTRACTION
http://www.unirio.br/analisedealimentos
MUSCLE CONTRACTION
higheredbcs.wiley.com
http://www.unirio.br/analisedealimentos
Regnier & Cheng 2016
http://www.unirio.br/analisedealimentos
Rigor Mortis as a Function of Meat Chemistry and Time The timing of
the stages of rigor mortis varies between species. Poultry is often in rigor
within 1-2 hours, pork within 4 to 6 hours, beef and lamb within 7 to 15
hours after exsanguination.
http://qpc.adm.slu.se/6_Fundamentals_of_WHC/page_16.htm
http://www.unirio.br/analisedealimentos
Compound Color Name
-CN Red Cyanmetmyoglobin
-OH Brown Metmyoglobin
-SH Green Sulfmyoglobin
-H2O2 Green Choleglobin
Compound Color Name
:H2O Purple Reduced myoglobin
or deoxymyoglobin
:O2 Red Oxymyoglobin
:NO Cured pink Nitric oxide
myoglobin
:CO Red Carboxymyoglobin
Chemical state of myoglobin
(covalent bonds)
Chemical state of myoglobin
(ionic bonds)
http://meat.tamu.edu/ansc-307-honors/meat-color/
http://www.unirio.br/analisedealimentos
Four Categories of Pork Quality
RFN
Red, Firm, Non-exudative.
Minolta L* less than 50; pH
between 5.5 – 6.1
RSE
Red, Soft, Exudative.
Minolta L* less than 50; pH less
than 5.6
PSE
Pale, Soft, Exudative. Minolta L*
greater than 50; pH less than 5.5
DFD
Dark, Firm, Dry. Minolta L* less
than 38; pH greater than 6.1
http://www.thepigsite.com/articles/5341/pork-meat-quality-understanding-industry-
measurements-and-guidelines/
http://www.unirio.br/analisedealimentos
Water Holding Capacity (WHC) of Meat
http://qpc.adm.slu.se/6_Fundamentals_of_WHC/page_21.htm
http://www.unirio.br/analisedealimentos
Effect of seasonality and storage temperature on rigor mortis in the
adductor muscle of lion's paw scallop Nodipecten subnodosus
The effect of season and storage at three temperatures (0, 5 and 10 °C) was
evaluated on the main metabolites and parameters related to rigor mortis.
Adenosine 5′-triphosphate (ATP), lactic acid, octopine, pH and sarcomere length
in the adductor muscle of lion's paw scallop Nodipecten subnodosus were
determined. Seasonality influenced the initial values of ATP, octopine and pH, however, no effect was noticed during storage, since a similar effect for the three
temperatures evaluated in the four seasons was observed. A lower ATP
concentration was found during storage at 0 °C than that found in muscle stored
at 5 and 10 °C. According to the analyses of lactic acid, octopine and pH, the
muscle acidification during rigor mortis was independent of lactic acid production. The greater sarcomere lengths for all seasons were in agreement
with the highest ATP concentrations, corresponding to the samples stored at 5
and 10 °C. Therefore, according to the level of myofibrillar contraction, rigor
mortis was lower at 5 and 10 °C storage in the four seasons. Hence, it is
concluded that the seasonality did not show a significant impact on metabolite and parameter values related to rigor mortis during storage, and that 5 °C is the
best storage temperature for the adductor muscles during the initial stage
of rigor mortis and then reduce it to 0 °C, if it is focused to the fresh market.
Jiménez-Ruiz et al. 2013
http://www.unirio.br/analisedealimentos
ATP concentration in the
adductor muscle of lion's paw
scallop N.
subnodosus harvested at
distinct seasons and stored at different temperatures. a)
Spring, b) summer, c)
autumn, and d) winter.
Lactic acid concentration
in the adductor muscle of
lion's paw scallop N.
subnodosusharvested at
distinct seasons and stored at different
temperatures. a) Spring, b)
summer, c) autumn, and d)
winter.
Jiménez-Ruiz et al. 2013
http://www.unirio.br/analisedealimentos
pH values in the adductor
muscle of lion's paw
scallop N.
subnodosus harvested at
distinct seasons and stored at different temperatures. a)
Spring, b) summer, c)
autumn, and d) winter.
octopine is considered
as one of the possible
final metabolites of
anaerobic glycolysis
for certain invertebrates
Jiménez-Ruiz et al. 2013
http://www.unirio.br/analisedealimentos
Comparative profiling of sarcoplasmic phosphoproteins
in ovine muscle with different color stability
The phosphorylation of sarcoplasmic proteins in postmortem muscles was
investigated in relationship to color stability in the present study. Although no
difference was observed in the global phosphorylation level of sarcoplasmic
proteins, difference was determined in the phosphorylation levels of individual
protein bands from muscles with different color stability. Correlation analysis and liquid chromatography – tandem mass spectrometry (LC-MS/MS)
identification of phosphoproteins showed that most of the color stability-related
proteins were glycolytic enzymes. Interestingly, the phosphorylation level of
myoglobin was inversely related to meat color stability. As the phosphorylation
of myoglobin increased, color stability based on a∗ value decreased and metMb content increased. In summary, the study revealed that protein
phosphorylation might play a role in the regulation of meat color stability
probably by regulating glycolysis and the redox stability of myoglobin, which
might be affected by the phosphorylation of myoglobin.
Li et al. 2017
http://www.unirio.br/analisedealimentos
Gel-base analysis of
sarcoplasmic protein phosphorylation Li et al. 2017
http://www.unirio.br/analisedealimentos
Underlying connections between the redox system imbalance, protein oxidation
and impaired quality traits in pale, soft and exudative (PSE) poultry meat
The connections between the redox imbalance in post-mortem muscle, early protein
oxidation and the onset of pale, soft and exudative (PSE) condition in chicken breast
are studied. PSE was induced by incubation of post-mortem chicken carcasses at
37 °C for 200 min. PSE-induced muscle consistently had faster pH decline and
lower pH at 200 min (5.84 vs. 6.59) and 24 h (5.69 vs. 5.96), higher L∗ (54.4 vs. 57.3), and lower texture and water holding capacity (WHC) than normal meat. The
activities of catalase, glutathione peroxidase and superoxide dismutase were
significantly lower in PSE-induced samples than in the normal counterparts. PSE
was more susceptible to proteolysis and protein oxidation than normal meat during
succeeding chilled storage with more intense tryptophan and thiols depletion, higher protein carbonylation and more intense formation of protein cross-links. We provide
plausible explanations to support the role of protein oxidation in the impaired quality PSE chicken.
Carvalho et al. 2017
http://www.unirio.br/analisedealimentos
Evolution of pH in normal and
PSE-induced breast broiler meat during
24 h following slaughter.
Tryptophan (mg NATA/g protein) (A) and free
thiols (μmol thiols/mg sample) (B) depletion
during chilled storage of normal and PSE-induced
breast broiler meat.
Carvalho et al. 2017
http://www.unirio.br/analisedealimentos
Carvalho et al. 2017
Formation of oxidation products: protein carbonyls (nmol carbonyls/mg protein)
(A) TBA-RS (mg MDA/kg muscle) (B), Schiff bases (fluorescence intensity) (C) and
disulphide bonds (μmol thiols/mg sample) (D) during chilled storage at 4 °C of normal
and PSE-induced breast broiler meat.
http://www.unirio.br/analisedealimentos
Applications of high pressure to pre-rigor rabbit muscles
affect the water characteristics of myosin gels
Myosin was extracted immediately after high-pressure treatment (HP,
100–300 MPa for 15 or 180 s) to pre-rigor rabbit muscles (PRRMs) for
evaluating the influences of HP-treatment on gel properties, using
untreated muscles as Controls. Assessment of myosin yields, water-
holding capacity (WHC), water mobility and distribution demonstrated that HP modified myosin before its extraction. Myosin gels subjected to
HP at 100 MPa 180 s and 200 MPa 15 s had enhanced WHC
compared with Controls. Also, the highest proportion of immobile-water
was observed in myosin gels treated at 200 MPa for 15 s. HP-
treatment of PRRMs affected their physicochemical properties as evidenced by alterations in tertiary, secondary conformations and
rheological properties during subsequent heating. These modifications
appear to induce various degrees of exposure of hydrophobic and
sulfhydryl groups, resulting in different gelation rates. These alterations
partly explain the various gel qualities obtained and indicate the potential of HP for pre-rigor muscles.
Xue et al. 2017
http://www.unirio.br/analisedealimentos
Yields of myosin extracted from PRRMs
following various HP
treatments. Note: Means with different
superscripts (a–e)
Water holding capacity (WHC) of
myosin gels. Xue et al. 2017
http://www.unirio.br/analisedealimentos
Changes in the hydrophobicity of various myosin
samples when heated from 25 to 85 °C.
The Surface hydrophobicity (H0) is an important
indicator of protein
conformation changes,
and the exposure of buried hydrophobic
residues has been
considered as a
prerequisite for the aggregation of myosin
Xue et al. 2017
http://www.unirio.br/analisedealimentos
Changes in the sulfhydryl contents of of various
myosin samples when heated from 25-85°C
The tertiary changes of
myosin are mainly
related to those based
on non-covalent
interactions and the breaking of some non-
covalent bonds which
are beneficial for the
exposure of buried
amino groups, such as hydrophobic groups
and sulfhydryl groups
Xue et al. 2017
http://www.unirio.br/analisedealimentos
Storage modulus (G′) of various myosin solutions
The gelling process of meat
proteins usually occurs in three
stages: 1) an initial increase in
G′, ascribed to the denaturation
and aggregation of the head and hinge components of
myosin; 2) followed by a
reduction of G′ induced by the
denaturation of myosin tails,
which may disrupt the weak gel network, leading to the
enhancement of fluidity; 3)
finally, where the denatured
myosin is aggregated and
bound to form an organized gel network.
http://www.unirio.br/analisedealimentos
Effect of sodium alginate with three molecular weight forms
on the water holding capacity of chicken breast myosin gel
The effect of 0.1–0.5% (w/w) sodium-alginate (SA) with three
molecular-weights (2660, 3890 and 4640 kDa) on the water-holding
capacity (WHC) of chicken-breast myosin gels was investigated. The
results showed that 0.1–0.5% SA of three molecular-weights
increased the WHC of myosin-SA gels, and the heavier SA induced a higher WHC. Electrostatic-interactions and hydrogen-bonding
contributed to the intermolecular aggregation in the myosin-SA system
and enhanced its intermolecular interactions by overcoming the steric
hindrance effect of SA with heavier molecules. This aggregation
induced the increased turbidity, transition temperature and the decreased surface hydrophobicity of myosin-SA solutions and the
formation of an inhomogeneous network with large cavities for
entrapping water. The combined effects of stronger intermolecular
interactions and the network induced a higher WHC of the gel with
heavier SA. It is interesting to understand the gelling mechanism for the protein-polysaccharide system and to efficiently select SA for
developing low-fat meat products in industry.
Yao et al. 2018
http://www.unirio.br/analisedealimentos
Effects of L-SA, M-SA and H-SA on
the WHC of myosin gels
Effects of L-SA, M-SA and H-SA
on the turbidity (A) and the surface
hydrophobicity (B) of myosin gels.
Yao et al. 2018
http://www.unirio.br/analisedealimentos
WHC of myosin with 0.3% SA (A) and 0.5% SA
(B) gels as affected by chemical reagents
Treatment Tpeak1 (°C) Tpeak2 (°C)
Myosin 53.87 ± 0.39a 65.14 ± 0.30a
Myosin + 0.5% L-SA 54.54 ± 0.47a 65.85 ± 0.40ab
Myosin + 0.5% M-SA 54.14 ± 0.22a 66.87 ± 0.23b
Myosin + 0.5% H-SA 54.83 ± 0.36a 67.31 ± 0.00c
Transition temperature (Tpeak) of myosin,
myosin + L-SA, myosin + M-SA and
myosin + H-SA.*
Yao et al. 2018
Carvalho, R.H. et al., 2017. Underlying connections between the redox system imbalance, protein oxidation and impaired qualit y traits in pale, soft
and exudative (PSE) poultry meat. Food Chemistry, 215, pp.129–137. Available at: http://ac-els-cdn-
com.ez39.periodicos.capes.gov.br/S0308814616312158/1-s2.0-S0308814616312158-main.pdf?_tid=179fa19c-8100-11e7-b1a1-
00000aab0f27&acdnat=1502722485_0a16a67a574f320f9b3a5d988ac24c4c [Acedido Agosto 14, 2017].
Damodaran, S., Parkin, K.L. & Fennema, O.R., 2010. Quimica de Alimentos de Fennema 4.a ed. Artmed, ed., Porto Alegre.
Édira Castelo Branco de Andrade, 2015. Análise de alimentos - uma visão química da Nutrição Varela, ed., São Paulo.
Ertbjerg, P. & Puolanne, E., 2017. Muscle structure, sarcomere length and influences on meat quality: A review. Meat Science. Available at:
www.elsevier.com/locate/meatsci [Acedido Agosto 12, 2017].
Jiménez-Ruiz, E.I. et al., 2013. Effect of seasonality and storage temperature on rigor mortis in the adductor muscle of lion’s paw scallop Nodipecten
subnodosus. Aquaculture, 388–391(1), pp.35–41. Available at: http://ac-els-cdn-com.ez1.periodicos.capes.gov.br/S0044848613000100/1-s2.0-
S0044848613000100-main.pdf?_tid=7449c7ae-7f1d-11e7-9029-00000aacb362&acdnat=1502515194_48a39a774413a426b1a9234c1e1ac9fd
[Acedido Agosto 12, 2017].
Li, M. et al., 2017. Comparative profiling of sarcoplasmic phosphoproteins in ovine muscle with different color stability. Available at: http://ac-els-
cdn-com.ez1.periodicos.capes.gov.br/S0308814617312505/1-s2.0-S0308814617312505-main.pdf?_tid=d3d91754-7f1f-11e7-be88-
00000aacb35f&acdnat=1502516213_fa74b09f994691a3aea7deb562850619 [Acedido Agosto 12, 2017].
Regnier, M. & Cheng, Y., 2016. Finally, We Can Relax: A New Generation of Muscle Models that Incorporate Sarcomere Compliance . Biophysical
Journal, 110(3), pp.521–522.
Xue, S. et al., 2017. Applications of high pressure to pre-rigor rabbit muscles affect the functional properties associated with heat-induced gelation.
Meat Science, 129, pp.176–184. Available at: www.elsevier.com/locate/foodchem [Acedido Agosto 14, 2017].
Yao, J. et al., 2018. Effect of sodium alginate with three molecular weight forms on the water holding capacity of chicken breast myosin gel. , 239,
pp.1134–1142. Available at: http://ac-els-cdn-com.ez39.periodicos.capes.gov.br/S030881461731172X/1-s2.0-S030881461731172X-
main.pdf?_tid=c988e93a-8106-11e7-bd8e-00000aacb362&acdnat=1502725361_67348016d5d4cb463dc2bd773ed71a98 [Acedido Agosto 14,
2017].
Yildiz, F., 2010. Advances in food biochemistry, CRC Press.
References