Heat-induced changes in myofibrillar protein structures and myowater of two pork qualities. A combined FT-IR spectroscopy and low-field NMR relaxometry study

Low-field NMR T(2) and Fourier transform infrared (FT-IR) measurements were performed on meat samples of two qualities (normal and high ultimate pH) during cooking from 28 degrees C to 81 degrees C. Pronounced changes in both T(2) relaxation data and FT-IR spectroscopic data were observed during cooking, revealing severe changes in the water properties and structural organization of proteins. The FT-IR data revealed major changes in bands in the amide I region (1700-1600 cm(-)(1)), and a tentative assignment of these is discussed. Distributed NMR T(2) relaxation data and FT-IR spectra were compared by partial least-squares regression. This revealed a correlation between the FT-IR peaks reflecting beta-sheet and alpha-helix structures and the NMR relaxation populations reflecting hydration water (T(2B) approximately 0-10 ms), myofibrillar water (T(21) approximately 35-50 ms), and also expelled "bulk" water (T(2) relaxation times >1000 ms). Accordingly, the present study demonstrates that definite structural changes in proteins during cooking of meat are associated with simultaneous alterations in the chemical-physical properties of the water within the meat.     

Influence of aging and salting on protein secondary structures and water distribution in uncooked and cooked pork. A combined FT-IR microspectroscopy and 1H NMR relaxometry study

Fourier transform infrared (FT-IR) microspectroscopy and low-field (LF) proton NMR transverse relaxation measurements were used to study the changes in protein secondary structure and water distribution as a consequence of aging (1 day and 14 days) followed by salting (3%, 6%, and 9% NaCl) and cooking (65 degrees C). An enhanced water uptake and increased proton NMR relaxation times after salting were observed in aged meat (14 days) compared with nonaged meat (1 day). FT-IR bands revealed that salting induced an increase in native beta-sheet structure while aging triggered an increase in native alpha-helical structure before cooking, which could explain the effects of aging and salting on water distribution and water uptake. Moreover, the decrease in T2 relaxation times and loss of water upon cooking were attributed to an increase in aggregated beta-sheet structures and a simultaneous decrease in native protein structures. Finally, aging increased the cooking loss and subsequently decreased the final yield, which corresponded to a further decrease in T2 relaxation times in aged meat upon cooking. However, salting weakened the effect of aging on the final yield, which is consistent with the increased T2 relaxation times upon salting for aged meat after cooking and the weaker effect of aging on protein secondary structural changes for samples treated with high salt concentration. The present study reveals that changes in water distribution during aging, salting, and cooking are not only due to the accepted causal connection, i.e., proteolytic degradation of myofibrillar structures, change in electrostatic repulsion, and dissolution and denaturation of proteins, but also dynamic changes in specific protein secondary structures.     

Polymorphisms in the bovine HSP90AB1 gene are associated with heat tolerance in Thai indigenous cattle

Heat shock proteins act as molecular chaperones that have preferentially been transcribed in response to severe perturbations of the cellular homeostasis such as heat stress. Here the traits respiration rate (RR), rectal temperature (RT), pack cell volume (PCV) and the individual heat tolerance coefficient (HTC) were recorded as physiological responses on heat stress (environmental temperatures) in Bos taurus (crossbred Holstein Friesian; HF) and B. indicus (Thai native cattle: White Lamphun; WL and Mountain cattle; MT) animals (n = 47) in Thailand. Polymorphisms of the heat shock protein 90-kDa beta gene (HSP90AB1) were evaluated by comparative sequencing. Nine single nucleotide polymorphisms (SNP) were identified, i.e. three in exons 10 and 11, five in introns 8, 9, 10 and 11, and one in the 3′UTR. The exon 11 SNP g.5082C>T led to a missense mutation (alanine to valine). During the period of extreme heat (in the afternoon) RR and RT were elevated in each of the three breeds, whereas the PCV decreased. Mountain cattle and White Lamphun heifers recorded significantly better physiologic parameters (p < 0.05) in all traits considered, including or particularly HTC than Holstein Friesian heifers. The association analysis revealed that the T allele at SNP g.4338T>C within intron 3 improved the heat tolerance (p < 0.05). Allele T was exclusively found in White Lamphun animals and to 84% in Mountain cattle. Holstein Friesian heifers revealed an allele frequency of only 18%. Polymorphisms within HSP90AB1 were not causative for the physiological responses; however, we propose that they should at least be used as genetic markers to select appropriate breeds for hot climates.     

Evaluation of bitter masking flavanones from Herba Santa (Eriodictyon californicum (H. and A.) Torr., Hydrophyllaceae)

Products made from Herba Santa (Eriodictyon californicum (H. & A.) Torr.) have been used as bitter remedies for some pharmaceutical applications for many years, but they are actually too aromatic to be useful for many food or pharmaceutical applications. In sensory studies flavanones homoeriodictyol (1), its sodium salt (1-Na), sterubin (2), and eriodictyol (4) could significantly decrease the bitter taste of caffeine without exhibiting intrinsic strong flavors or taste characteristics. Further investigations on 1-Na elicited a broad masking activity between 10 and 40% toward different chemical classes of bitter molecules (e.g. salicin, amarogentin, paracetamol, quinine) but not toward bitter linoleic acid emulsions. For caffeine and amarogentin, dose-response studies were performed; the masking activity toward bitter taste for both compounds reached a plateau at higher concentrations of 1-Na. Due to these facts, homoeriodictyol sodium salt (1-Na) seems to be a very interesting new taste modifier for food applications and pharmaceuticals.     

Relationship between meat structure, water mobility, and distribution: a low-field nuclear magnetic resonance study

Nuclear magnetic resonance (NMR) measurements were carried out on pork longissimus muscle, which pre rigor had been manipulated to various muscle lengths, to investigate the relationship between the microstructure of meat and the NMR T(2) relaxation. Distributed exponential analysis of the NMR T(2) relaxation data revealed the existence of three distinct water populations: T(2b), T(21), and T(22). A high, significant correlation was found between the T(21) time constant and the sarcomere length (r = 0.84) and calculated ration of myofilament lattice volume in the I-band and A-band regions, respectively (r = 0.84), considering sigmoid relationships. The result implies that the T(21) time constant mainly is determined by the structure of the myofilament lattice and so strongly supports a previously proposed theory that the T(21) population corresponds to water located within a highly organized myofibrillar protein matrix including actin and myosin filament structures. A high correlation was also found between the T(22) population and the water-holding capacity (WHC) (r = 0.76), which suggests that the WHC is mainly determined by the amount of loosely bound extramyofibrillar water. However, the correlation between NMR T(2) parameters and WHC was further increased (r = 0.84) by including the T(21) time constant in the correlation analysis. This implies that the formation of drip loss is an ongoing process involving the transfer of water from myofibrils to the extracellular space and is affected by structural features at several levels of organization within the muscle tissue. This study demonstrates the advantages of NMR T(2) relaxation as an effective technique for obtaining further understanding of the relationship between the microstructure of meat, its WHC, water mobility, and water distribution.     

Foliar and tuber assessment of late blight (Phytophthora infestans (Mont.) de Bary) reaction in cultivated potato (Solanum tuberosum L.)

Summary Host plant resistance is an important component to the management of potato late blight,Phytophthora infestans (Mont.) de Bary. Assessment of potato lines (Solanum tuberosum L.) with various levels of resistance toP. infestans (US8, A2 genotype) were evaluated in field trials, greenhouse controlled environment chambers and inoculated tuber reactions. Five lines (AWN86514-2, B0692-4, B0718-3, Jacqueline Lee, and B0288-17) with strong foliar resistance to late blight were identified in these inoculated field trials. Greenhouse controlled environment chamber studies allowed resistant and susceptible lines to be distinguished, but the 1998 greenhouse results did not correlate well with field data. Four lines (A084275-3, Bzura, MSG007-1, and MSG297-4RD) evaluated by a digital image analysis technique demonstrated tuber resistance based upon average reflective index values in the inoculated tuber studies. Tuber resistance did not correlate with field foliar resistance. Based upon these results, field assessment of foliar reaction toP. infestans provides the best measure for assessing late blight resistance in potato. Tuber resistance to late blight can be identified among lines with varying levels of foliar resistance.     

Evidence for genetic linkage of Alzheimer's disease to chromosome 10q

Recent studies suggest that insulin-degrading enzyme (IDE) in neurons and microglia degrades Abeta, the principal component of beta-amyloid and one of the neuropathological hallmarks of Alzheimer's disease (AD). We performed parametric and nonparametric linkage analyses of seven genetic markers on chromosome 10q, six of which map near the IDE gene, in 435 multiplex AD families. These analyses revealed significant evidence of linkage for adjacent markers (D10S1671, D10S583, D10S1710, and D10S566), which was most pronounced in late-onset families. Furthermore, we found evidence for allele-specific association between the putative disease locus and marker D10S583, which has recently been located within 195 kilobases of the IDE gene.