Titin-mediated thick filament activation stabilizes myofibrils on the descending limb of their force-length relationship

Purpose:The aim of this study was to extend current half-sarcomere models by involving a recently found force-mediated activation of the thick filament and analyze the effect of this mechanosensing regulation on the length stability of half-sarcomeres arranged in series.Methods:We included a super-relaxed state of myosin motors and its force-dependent activation in a conventional cross-bridge model.We simulated active stretches of a sarcomere consisting of 2 non-uniform half-sarcomeres on the descending limb of the force-length relationship.Results:The mechanosensing model predicts that,in a passive sarcomere on the descending limb of the force-length relationship,the longer half-sarcomere has a higher fraction of myosin motors in the on-state than the shorter half-sarcomere.The difference in the number of myosin motors in the on-state ensures that upon calcium-mediated thin filament activation,the force-dependent thick filament activation keeps differences in active force within 20%during an active stretch.In the classical cross-bridge model,the corresponding difference exceeds 80%,leading to great length instabilities.Conclusion:Our simulations suggest that,in contrast to the classical cross-bridge model,the mechanosensing regulation is able to stabilize a system of non-uniform half-sarcomeres arranged in series on the descending limb of the force-length relationship.

煮制时间对鹅肉蛋白结构的影响

为了探究煮制对鹅肉蛋白的影响,本文通过测定不同煮制时间(0、30、60、90、120 min)下鹅肉的蒸煮损失率、剪切力、蛋白电泳、肌原纤维小片化指数(myofibril fragmentation index,MFI)、游离氨基酸(free amino acid,FAA)构成及微观结构研究了煮制时间对鹅肉蛋白结构特性的影响。结果表明:蒸煮损失率随着煮制时间的延长而升高,由0 min处的27.5%升高到120 min处的39.0%;剪切力值则是随着煮制时间的延长而呈现先上升再下降的趋势,且在90 min时出现最低值;十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE)图谱显示,随着煮制时间的延长35~55 kDa处的条带逐渐变浅变细,10~15 kDa处条带随煮制时间延长颜色变深;MFI值随着煮制时间的延长显著增加(P<0.05),煮制120 min时的MFI值约为处理0 min时的2倍;共检出三种呈味氨基酸,从总量看,苦味氨基酸的含量最多,甜味氨基酸含量次之,鲜味氨基酸含量最少。煮制过程中,这三类氨基酸总含量总体表现为随煮制时间的延长而增加的趋势(甜味氨基酸的总含量约增加了2.5倍,苦味氨基酸的总含量约增加了3.1倍,鲜味氨基酸的总含量约增加了3.4倍),而甲硫氨酸和半胱氨酸这两者的含量随煮制时间的延长而减少;扫描电镜(scanning electron microscope,SEM)图中发现肌纤维之间的空隙表现出先变大后减小到粘成一块。同时,肌纤维和肌束膜结构的完整程度随着煮制时间的延长逐步破坏,最终导致部分肌纤维束发生崩塌使它们相互黏成一块。因此,鹅肉在蒸煮过程中,其蛋白组成和含量、MFI值、游离氨基酸组成及微观结构会因时间变化而发生改变,从而影响了鹅肉蛋白结构的变化。研究表明,90 min为鹅肉的最佳煮制时间。

Effect of xanthan gum on the quality of low sodium salted beef and property of myofibril proteins

The effects of xanthan gum (0 % and 0.3 %) on the quality of low sodium (2.0 %, 2.4 %, 2.8 %, 3.2 %, 3.6 % and 4.0 %) salted beef and property of myofibril proteins (MP) extracted from salted beef were researched. Changes in the salting absorptivity, cooking loss, shear force, color and sensory analysis showed that xanthan gum had a positive effect on the quality of salted beef with low salinity (2.0 %, 2.4 % and 2.8 %). MP of salted beef treated with xanthan gum had higher solubility, lower hydrogen bond than that without it (P < 0.05). The decrease of surface hydrophobicity and intrinsic fluorescence intensity indicated that the chromophore of protein was brought into a hydrophobic environment in the presence of xanthan gum. The electrophoresis showed that xanthan gum could improve the concentration of myosin heavy chain, paramyosin and actin after tumble-salting. The data suggested that salted beef and its MP treated with xanthan gum and 2.8 % salt (XS3) had the best properties. Together, xanthan gum could be considered as a sodium salt substitute for the development of low sodium meat products.

Phosphorylation of sarcoplasmic and myofibrillar proteins in three ovine muscles during postmortem ageing

This study aimed to examine changes in phosphorylation of sarcoplasmic and myofibrillar proteins from longissimus lumborum,semitendinosus,and psoas major muscles during postmortem ageing for 5 d.These sarcoplasmic and myofibrillar proteins were separated using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and stained with phosphorous and protein specific stains.Myofibril fragmentation index,pH,the content of lactic acid and the relative activity of μ-calpain in three ovine muscles were measured.These results showed that the relative phosphorylation level of sarcoplasmic and myofibrillar proteins of psoas major muscle were lower compared with longissimus lumborum and semitendinosus muscles(P<0.05).The pH of psoas major muscle was the lowest at 0.5 h postmortem,and the highest after 12 h postmortem(P<0.05).In addition,the relative activity of μ-calpain was higher within 5 d postmortem and myofibril fragmentation index was higher after 1 d postmortem in psoas major muscle than those of longissimus lumborum and semitendinosus muscles(P<0.05).The sarcoplasmic protein phosphorylation may regulate the rate of pH decline to influence the μ-calpain activity and then proteolysis of proteins consequently.This study gives a new perspective of the mechanism of postmortem meat tenderization.

The Relationships between Rheological Properties and Structural Changes of Chilled Abalone Meat

The quantitative correlation between rheological properties and structural characteristic values of chilled abalone meat was studied. Structural changes were observed, and these values were enumerated using image processing and analysis technique. Structural changes in the myofibrils and collagen fibrils were the greatest in chilling for 24 h. After chilling for 48h, similar structures of vertical and cross sections were observed. For chilling from 0h to 72h, the instantaneous modulus E0 of the both section meat decreases gradually with time, but no significant differences were observed after chilling for 48h. The relaxation time and viscosity of both sections attained the same values for the same chilling time, but increased gradually with increasing chilling time. Meanwhile, a negative correlation between the structural characteristic values (Dm, Am, Rvm), and rheological properties (E1, τ1 , η1) clearly exists. Some logarithmic expressions have been obtained for these negative correlations. These results suggest that the difference in rheological properties between the cross and vertical sections was mainly due to the structural changes of myofibrils and collagen fibrils, and rheological properties are influenced quantitatively by the structural characteristic values for chilling from 0h to 72h.

Structural Changes and Rheological Properties of Dry Abalone Meat (Haliotis diversicolor) During the Process of Water Restoration

Changes in tissue structure, rheological property and water content of dry abalone meat in the process of water restora- tion were studied. The weight and volume of dry abalone meat increased with water restoration. When observed under a light micro- scope, structural change in myofibrils was obvious and a distinct network was found. When water restoration time increased from 24 h to 72 h, the instantaneous modulus E0 and viscosity η1 increased, whereas the rupture strength and relaxation time (τ1) were re- duced. There were no significant changes of rheological parameters (E0, η1, τ1, rupture strength) from 72 h to 96 h of water restoration. Therefore, the dry abalone meat was swollen enough at the time of 72 h. The rheological parameters were obviously influenced by the structural changes.