胶原蛋白对发酵乳品质的影响

通过测定不同胶原蛋白添加量下发酵乳的卜羟脯氨酸的含量、黏度、酸度、乳清析出量和感官品质指标的变化情况,得出胶原蛋白对发酵乳品质的影响．结果表明：胶原蛋白的加入能够提高发酵乳中-L羟脯氨酸的含量,提高发酵乳的黏度和保水性,减少乳清析出,改善发酵乳的口感．     

兔皮Ⅰ型胶原的提取、改性与性能研究

采用酸溶、酶溶相结合的方法,从兔皮中提取了胶原蛋白.通过SDS-PAGE对其进行定性分析,利用FT-IR及TG/DTG表征其理化性能.结果表明,所提胶原为I型胶原,保持了完整的三股螺旋结构;热处理过程中,在100℃之前,200～450℃之间和450℃以后有3次明显失重.经戊二醛交联改性后,该胶原的含水量为(78.7±1.3)%,酶降解率从(88.65±0.11)%降为(6.03±0.38)%(p0.01).采用细胞生长抑制法测定了改性胶原对小鼠胚胎成纤维细胞(MEF-WT)的细胞毒性.结果表明,改性胶原对MEF-WT细胞无明显毒性,毒性评价为0级或1级.该胶原可用于组织工程.     

TGase对海地瓜胶原蛋白凝胶强度的影响

为了研究海地瓜胶原蛋白的凝胶特性,提高其凝胶强度,探讨了谷氨酰胺转氨酶(TGase)对海地瓜胶原蛋白凝胶特性的影响,在单因素的基础上采用响应面设计对影响凝胶特性的3个显著因素（TGase添加量、作用时间、作用温度）进行优化.结果显示:单因素实验时,海地瓜胶原蛋白的凝胶强度在TGase添加量18.0 U/g、作用时间5.0 h、作用温度40.0 ℃时达到最大;通过响应面优化,得到海地瓜胶原蛋白凝胶强度在TGase添加量18.00 U/g、作用时间5.13 h和作用温度40.30 ℃时达到最大,为6473.98 g·mm,是未优化前凝胶强度5511.50 g·mm的1.17倍,是未添加TGase前凝胶强度1118.88 g·mm的5.79倍,即TGase能够促进蛋白质之间的交联作用,显著提高海地瓜胶原蛋白凝胶强度.经过验证性试验,得到该条件下海地瓜胶原蛋白凝胶强度为6428.36 g·mm,与理论值相比,误差仅为0.70%.     

Early results of transcutaneous injection laryngoplasty with micronized acellular dermis versus type-I thyroplasty for glottic incompetence dysphonia due to unilateral vocal fold paralysis

Medialization thyroplasty (type I) has become the gold standard to improve glottic closure due to unilateral vocal fold paralysis. A newer injection method utilizing homologous collagen from cadaveric human tissue has been described as an attractive alternative as no donor site is required, there is a very low risk of hypersensitivity, and the intact, acellular collagen fibers may suffer a reduced long-term reabsorption rate. Preliminary results on eight patients comparing presurgical and postsurgical parameters (perceptual, stroboscopic, acoustic, and aerodynamic) revealed comparable results when compared with a control group of individuals, age- and sex-matched, that had undergone standard medialization thyroplasty (type I). Further study is needed to assess the long-term results with this minimally invasive method of vocal fold medialization.     

胶原蛋白的研究进展

综述了胶原蛋白在烧伤,创伤,美容,矫形,创面止血等方面的临床应用及与其相关性疾病的研究进展。     

应用bFGF胶原缓释海绵修复髓室底穿孔的疗效

目的:观察碱性成纤维细胞生长因子(bFGF)胶原缓释海绵消除髓室底炎症及修复髓室底穿孔的疗效。方法:实验组5 2例(5 7颗患牙)应用bFGF胶原缓释海绵作为内屏障材料充填穿孔周围,避免穿孔周围修补材料超充填,对照组4 0例(42颗患牙)使用聚梭酸锌粘固粉。对临床症状和X片随访观察6个月,结果进行统计学处理,评价bFGF胶原缓释海绵的治疗效果。结果:当穿孔大于3mm以上及有临床症状时,bFGF组成功率为80 % ,失败率为2 0 % ,两组差异有统计学意义(P <0 0 5 )。结论:bFGF胶原缓释海绵在消除髓室底炎症修复髓室底穿孔具有显著的疗效,是一种新型内屏障材料     

Antibacterial and Miscibility Properties of Chitosan/Collagen Blends

The miscibility, bioactivity, and antibacterial properties of chitosan/collagen specimens were systematically studied. The specimens were prepared by blending collagen and chitosan with varying deacetylation degrees in solutions; the collagen molecules had been extracted from pigskins using the acid swelling-pepsin digestion method. To understand the miscibility properties of collagen and chitosan molecules, the intrinsic viscosity and differential scanning calorimetry analysis of collagen, chitosan, and collagen/chitosan specimens were performed. The instrinsic viscosity measurements suggested that chitosan and collagen molecules with varying deacetylation degrees were miscible at molecular level for all compositions and degrees of deacetylation of chitosan/collagen mixture solutions prepared in this study. Fourier transform infrared analyses suggested that the percentage of preserved triple helix structures present in collagen molecules in collagen/chitosan specimens decreased with increasing chitosan contents, since the ratios of peak absorbance at 1239 cm^?1 of amide III and 1455 cm^?1 of C?H bending of collagen/chitosan specimens decreased significantly with increase in their chitosan contents. Abnormally high denaturation temperatures (T_d) were observed as the chitosan contents of collagen/chitosan specimens reached 40 wt%, at which T_d of collagen molecules was even higher than that of the corresponding pure chitosan molecules with varying deacetylation degrees. The antibacterial activity of collagen/chitosan blends increased consistently with increasing deacetylation degrees and concentrations of chitosan molecules in collagen/chitosan solutions. Possible explanations for these interesting thermal denaturation, antibacterial, and miscibility properties of chitosan/collagen specimens are reported.     

Effect of Immobilization on Insoluble Collagen Concentration and Type I and Type III Collagen Isoforms of Rat Soleus Muscle

Immobilization is often associated with decreased muscle elasticity. This condition is known as muscle contracture; however, the mechanism remains unclear. The purpose of this study was to clarify the mechanism governing muscle contracture in rat soleus muscle by identifying changes in ankle joint mobility, insoluble collagen concentration and type I and type III collagen isoforms following 1- and 3-week immobilizations. Following a 1-week immobilization, range of motion (ROM) of dorsiflexion declined to 90% of the control value; additionally, ROM dropped to 67.5% of the control value after a 3-week immobilization. This finding suggested that ankle joint mobility decreases in conjunction with extended periods of immobilization. Insoluble collagen concentration in soleus muscles, which was unchanged after 1 week of immobilization, increased 3 weeks after immobilization. These results may be indicative of collagen fibers with strong intermolecular cross-links contained in the muscle was made increased relatively by 3 weeks of immobilization. Therefore, the change in intermolecular cross-links may be significant in terms of progress of muscle contracture with longer periods of immobilization. On the other hand, the ratio of type III to type I collagen isoforms in muscular tissue increased following a 1-week immobilization; moreover, this ratio remained constant after 3 weeks of immobilization. These data suggested that muscle immobilization may induce type III collagen isoform expression. The increase in the ratio of type III to type I collagen isoforms do not change in parallel with the increase in the limitation in ROM; however, this phenomenon probably is not closely related to the progress of muscle contracture. The change of collagen isoform in immobilized muscle may be involved in the mechanism governing the progression of muscle fibrosis.     

二维红外相关光谱法研究温度对交联胶原结构的影响

采用傅里叶红外光谱和二维相关分析研究了改性前后胶原在升温(25～115℃)过程中结构的变化。结果显示,改性前后胶原的特征吸收峰强度降低,峰值向低波数移动,其中酰胺II带的变化最明显,降低了～10cm-1,表明维系胶原三股螺旋结构稳定的氢键被破坏,结构发生改变。在1 515cm-1处自相关峰强度最强,说明温度对酰胺II带的影响最大。与未改性胶原相比,改性胶原的相关程度更弱,表明改性胶原结构受温度影响要小,交联提高了胶原的热稳定性;改性后胶原结构变化的顺序也不一样。由此可见,二维红外相关分析法能提供由温度引起的胶原结构动态变化的微观信息,对进一步研究改性胶原结构和功能之间的关系有一定的意义。