子母车系统效率分析与验证

在子母车系统中,研究一台母车配合两台子车在同层进行复合作业的效率问题,提高系统作业效率计算的准确性,优化系统整体布局和物流设备的选择。首先分析一台母车配合两台子车在同层的循环复合作业过程;然后结合子母车的运动特性得到其作业效率计算模型;最后采用MATLAB工具计算效率模型分别在随机组合作业对和FEM9.851标准作业对的作业效率,通过对比验证,两种循环作业的效率绝对偏差符合工程实际。在工程实际中可以参照FEM9.851标准作业对代替随机组合作业对进行子母车系统的效率计算。     

Design and evaluation of a mobile smart home interactive system with elderly users in Brazil

Personal and Ubiquitous Computing - This article presents a study concerning the evaluation of a smart home control system for elderly people with a sample of 10 users in a city in the interior of...     

Metabolism of phospholipids in the yeast Schizosaccharomyces pombe

The fission yeast Schizosaccharomyces pombe is an important model organism for the study of fundamental questions in eukaryotic cell and molecular biology. A plethora of cellular processes are membrane associated and/or dependent on the proper functioning of cellular membranes. Phospholipids are not only the basic building blocks of cellular membranes; they also serve as precursors to numerous signaling molecules. In this review, we describe the biosynthetic pathways leading to major S. pombe phospholipids, how these pathways are regulated, and what is known about degradation and turnover of fission yeast phospholipids. This review also addresses the synthesis, regulation and the role of water-soluble phospholipid precursors. The last chapter of the review is devoted to the use of S. pombe for the biotechnological production of value-added lipid molecules.     

液压支架让缩性能试验特性分析与探讨

分析研究国家标准中液压支架让缩性能试验的技术要求,设计开发让缩性能试验系统,以双伸缩立柱液压支架为研究对象进行让缩性能试验分析与研究,为让缩性能试验的开展提供了试验条件,为液压支架国标的实施提供基础。     

Bioinformatic characterization of the extracellular lipases from Kluyveromyces marxianus

Lipases are hydrolytic enzymes that break the ester bonds of triglycerides, generating free fatty acids and glycerol. Extracellular lipase activity has been reported for the nonconventional yeast Kluyveromyces marxianus, grown in olive oil as a substrate, and the presence of at least eight putative lipases has been detected in its genome. However, to date, there is no experimental evidence on the physiological role of the putative lipases nor their structural and catalytic properties. In this study, a bioinformatic analysis of the genes of the putative lipases from K. marxianus L-2029 was performed, particularly identifying and characterizing the extracellular expected enzymes, due to their biotechnological relevance. The amino acid sequence of 10 putative lipases, obtained by in silico translation, ranged between 389 and 773 amino acids. Two of the analysed putative proteins showed a signal peptide, 25 and 33 amino acids long for KmYJR107Wp and KmLIP3p, and a molecular weight of 44.53 and 58.23 kDa, respectively. The amino acid alignment of KmLIP3p and KmYJR107Wp with the crystallized lipases from a patatin and the YlLip2 lipase from Yarrowia lipolytica, respectively, revealed the presence of the hydrolase characteristic motifs. From the 3D models of putative extracellular K. marxianus L-2029 lipases, the conserved pentapeptide of each was determined, being GTSMG for KmLIP3p and GHSLG for KmYJR107Wp; besides, the genes of these two enzymes (LIP3 and YJR107W) are apparently regulated by oleate response elements. The phylogenetic analysis of all K. marxianus lipases revealed evolutionary affinities with lipases from abH15.03, abH23.01, and abH23.02 families.