黑米色素的提取和稳定性的初步研究

黑米含有大量的天然黑（紫）色素，该文主要研究了该色素的提取方法及酸度、温度、光照等因素对其稳定性的影响。     

非凸粘性守恒律退化激波的稳定性

本文利用加权函数的方法研究初值问题的退化粘性激波ｕ（ｘ－ｓｔ）（ｓ＝３ｕ）的大时间稳定性态，证明在一定条件下上述初值问题存在唯一整体解，且退化激波ｕ（ｘ－ｓｔ）具有大时间稳定性。     

埃及扁圆红甜菜色素的提取及其稳定性研究

提取埃及扁圆红甜菜中的色素，研究了酸度、热、光等对该色素稳定性的影响。结果表明：红甜菜色素水溶性好，对热、光的稳定性较好，适于弱酸性条件下使用。     

汽－液相变中成核的热力学理论

对现有汽－液相变过程有关文献中关于汽泡形成过程的分析提出了不同看法，并利用热力学理论从亚稳平衡态的特性出发对汽泡形成的热力学机制作出了分析，对系统从液态转变到汽－液共存状态的各阶段作出了说明。     

土坡稳定分析变分法的应用

本文应用土压力变分法理论解决土坡滑裂面型式及稳定安全系数 K 等问题,并可减少试算工作量.该法证明曲线及折线滑裂面是统一的,在一定条件下能相互转化.通过算例初步表明所得结果是可取的.     

时变线性系统的稳定性

本文研究了一般时变线性系统的渐近稳定性。利用构造二次型李雅普诺夫函数的思想,引进一个新的讨论时变线性系统稳定性的方法,得到了较宽和较实用的结果.     

水分对头孢唑林钠药效的影响初探

用平衡湿度法测定了头孢唑林钠的临界相对湿度，在２０℃时约为６７％。同时，通过破坏性实验考察了水分对其药效的影响，初步结果表明，水分每增加１％，效价降低约０．５％。据此，提出了分装操作的若干注意事项。     

多重特征值处分岐解的稳定性

本文讨论形如这类运动方程的平衡态分歧解(即M(x,λ)=0的分歧解)的线性化稳定性问题。本文采用一个算子的K谱概念,考察广义的算子演算,推广了线性泛函中的预解式,进而推广泛函分析中关于谱摄动的某些结果,在半单特征值以及K在KN(L(0))上存在广义逆和由M(x,λ)=0导出的分歧方程为F(u,λ)=0的条件假设下,得到关于平衡态分歧解的线性化稳定性可由关于平衡态分歧解的线性化稳定性确定的结论,将Sattinger,D.H.的结果作为定理3.9当K=I时的特例。     

Elucidation of the relationship between enzyme activity and internal motion using a lysozyme stabilized by cavity-filling mutations

We investigated the activity and the internal motions of a stabilized mutant hen lysozyme (HEL) in which the residues M12 and L56 were mutated to L and F, respectively (LF mutant HEL). The result of the activity measurements against glycol chitin at various temperatures suggested that the temperature dependence of the activity of LF mutant HEL shifted to the high-temperature side compared with that of wild-type HEL. The detailed internal motions of LF mutant HEL in the absence and presence of a substrate analogue, (NAG)₃, were examined by model-free analysis at 35°C. The results showed that the internal motions of LF mutant HEL in the presence of (NAG)₃ were drastically restricted compared with those in wild-type HEL. Our findings thus suggested that the mutation to the stabilized lysozyme restricted internal motions required for the enzymatic reaction.Received 8 February 2005; accepted 10 March 2005Y. Yoshida and T. Ohkuri contributed equally to this work.     

Structural and dynamical features contributing to thermostability in α-amylases

In recent years an increasing number of studies on thermophilic and hyperthermophilic proteins aiming to elucidate determinants of protein thermostability have yielded valuable insights about the relevant mechanisms. In particular, comparison of homologous enzymes with different thermostabilities (isolated from psychrophilic, mesophilic, thermophilic and hyperthermophilic organsims) offers a unique opportunity to determine the strategies of thermal adaptation. In this respect, the medium-sized amylolytic enzyme α-amylase is a well-established representative. Various studies on α-amylases with very different thermostabilities (melting temperature T_m = 40–110°C) report structural and dynamical features as well as thermodynamical properties which are supposed to play key roles in thermal adaptation. Here, results from selected homologous α-amylases are presented and discussed with respect to some new and recently proposed strategies to achieve thermostability.Received 28 February 2005; received after revision 29 April 2005; accepted 19 May 2005