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Search Results: 1 - 10 of 8212 matches for " Weilan Shao "
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Image Mathematics—Mathematical Intervening Principle Based on “Yin Yang Wu Xing” Theory in Traditional Chinese Mathematics (I)  [PDF]
Yingshan Zhang, Weilan Shao
Applied Mathematics (AM) , 2012, DOI: 10.4236/am.2012.36096
Abstract: By using mathematical reasoning, this paper demonstrates the mathematical intervening principle: “Virtual disease is to fill his mother but real disease is to rush down his son” (虚则补其母, 实则泄其子) and “Strong inhibition of the same time, support the weak” (抑强扶弱) based on “Yin Yang Wu Xing” Theory in image mathematics of Traditional Chinese Mathematics (TCMath). We defined generalized relations and generalized reasoning, introduced the concept of steady multilateral systems with two non-compatibility relations, and discussed its energy properties. Later based on the intervention principle in image mathematics of TCMath and treated the research object of the image mathematics as a steady multilateral system, it has been proved that the mathematical intervening principle is true. The kernel of this paper is the existence and reasoning of the non-compatibility relations in steady multilateral systems, and it accords with the oriental thinking model.
An Approach to the Production of Soluble Protein from a Fungal Gene Encoding an Aggregation-Prone Xylanase in Escherichia coli
Yilin Le,Jingjing Peng,Huawei Wu,Jianzhong Sun,Weilan Shao
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0018489
Abstract: The development of new procedures and protocols that allow researchers to obtain recombinant proteins is of fundamental importance in the biotechnology field. A strategy was explored to overcome inclusion-body formation observed when expressing an aggregation-prone fungal xylanase in Escherichia coli. pHsh is an expression plasmid that uses a synthetic heat-shock (Hsh) promoter, in which gene expression is regulated by an alternative sigma factor (σ32). A derivative of pHsh was constructed by fusing a signal peptide to xynA2 gene to facilitate export of the recombinant protein to the periplasm. The xylanase was produced in a soluble form. Three factors were essential to achieving such soluble expression of the xylanase: 1) the target gene was under the control of the Hsh promoter, 2) the gene product was exported into the periplasm, and 3) gene expression was induced by a temperature upshift. For the first time we report the expression of periplasmic proteins under the control of an Hsh promoter regulated by σ32. One unique feature of this approach was that over 200 copies of the Hsh promoter in an E. coli cell significantly increased the concentration of σ32. The growth inhibition of the recombinant cells corresponded to an increase in the levels of soluble periplasmic protein. Therefore, an alternative protocol was designed to induce gene expression from pHsh-ex to obtain high levels of active soluble enzymes.
Advances in and challenges for thermophilic fermentation of cellulosic ethanol
纤维素乙醇高温发酵的研究进展与展望

Yilin Le,Weilan Shao,
乐易林
,邵蔚蓝

生物工程学报 , 2013,
Abstract: Thermophiles can produce cellulosic ethanol at a high temperature where ethanol is directly distillated from fermentation, and biodegradation of lignocellulose can be simultaneously achieved when these thermophiles carry and express cellulase and hemicellulase genes. The simultaneous biodegradation, fermentation and distillation, a three-in-one process, can result in low production costs of cellulosic ethanol. We reviewed the advances and challenges in the approach to the three-in-one process, which refer to lignocellulases, regulation mechanisms, and genetic transfer systems.
Application of GFAT as a Novel Selection Marker to Mediate Gene Expression
Guogan Wu,Yu Sun,Wei Qu,Ying Huang,Ling Lu,Lun Li,Weilan Shao
PLOS ONE , 2012, DOI: 10.1371/journal.pone.0017082
Abstract: The enzyme glutamine: fructose-6-phosphate aminotransferase (GFAT), also known as glucosamine synthase (GlmS), catalyzes the formation of glucosamine-6-phosphate from fructose-6-phosphate and is the first and rate-limiting enzyme of the hexosamine biosynthetic pathway. For the first time, the GFAT gene was proven to possess a function as an effective selection marker for genetically modified (GM) microorganisms. This was shown by construction and analysis of two GFAT deficient strains, E. coli ΔglmS and S. pombe Δgfa1, and the ability of the GFAT encoding gene to mediate plasmid selection. The gfa1 gene of the fission yeast Schizosaccharomyces pombe was deleted by KanMX6-mediated gene disruption and the Cre-loxP marker removal system, and the glmS gene of Escherichia coli was deleted by using λ-Red mediated recombinase system. Both E. coli ΔglmS and S. pombe Δgfa1 could not grow normally in the media without addition of glucosamine. However, the deficiency was complemented by transforming the plasmids that expressed GFAT genes. The xylanase encoding gene, xynA2 from Thermomyces lanuginosus was successfully expressed and secreted by using GFAT as selection marker in S. pombe. Optimal glucosamine concentration for E. coli ΔglmS and S. pombe Δgfa1 growth was determined respectively. These findings provide an effective technique for the construction of GM bacteria without an antibiotic resistant marker, and the construction of GM yeasts to be applied to complex media.
Expression, purification and characterization of a thermostable pectate lyase from Thermotoga maritima
海栖热袍杆菌来源的极耐热碱性果胶裂解酶的表达、纯化及定性

Ping Li,Qingqing Jing,Weilan Shao,
李平
,景庆庆,邵蔚蓝

生物工程学报 , 2009,
Abstract: The structure gene pelA from Thermotoga maritima MSB8 encoding pectate lyase was amplified and ligated into pHsh, resulting pHsh-pelA. Through structural optimization on pHsh-pelA, the ultimate plasmid, pHsh-pelC, which possessed the most appropriate structure and free energy of mRNA, was obtained. Pectate lyase C (PelC) was obtained after expressing pHsh-pelC in Escherichia coli JM109. The optimum activity of PelC was determined at pH 8.5 at 90oC, with a half-life for almost 2 h at 95oC. PelC was stable at the pH range of 8.2-9.8, and was dependent on Ca2+ for activity and stability. The enzyme kept stable for a long time and possessed a high level of activity at 60oC. The kinetic assay using polygalacturonic acid (PGA) as substrate gave Km and Vmax of 0.11 mmol/L and 327 U per mg of protein. SDS-PAGE analysis showed that the molecular mass of the expressed recombinant PelC was about 43 kD, which was exactly the size predicted. The expression vector system of the heat shock plasmid pHsh owned such advantages as high expression level and cheap induction. Moreover, the superior stability of the recombinant enzyme laid the base for large-scale fermentation application.
Expression, Characterization and Application of Thermostable b-glucuronidase from Thermotoga maritima
极耐热性b-葡萄糖醛酸酶的高效表达和酶学性质及其 应用

Zhuo Wang,Jianjun Pei,Huazhong Li,Weilan Shao,
王卓
,裴建军,李华钟,邵蔚蓝

生物工程学报 , 2008,
Abstract: The gene of b-glucuronidase from Thermotoga maritima was cloned into the plasmid pHsh, and expressed in Escherichia coli JM109. The recombinant protein was purified to homogeneity by a simple step, heat treatment. The recombinant enzyme had a molecular mass of 65.9 kD. The optimal activity of b-glucuronidase was found at pH 5.0 and 80oC. The purified enzyme was stable over a pH range from 5.8 to 8.2 and had a half life of 2 h at 80oC. The kinetic experiments at 80oC with p-nitrophenyl-b- glucuronide as substrate gave a Km and Vmax of 0.18 mmol/L and 312 u per mg of protein. The purified enzyme could transform glycyrrhizin to glycyrrhetinic acid.
Detecting Dementia-Related Wandering Locomotion of Elders by Leveraging Active Infrared Sensors  [PDF]
Qiang Lin, Weichao Zhao, Weilan Wang
Journal of Computer and Communications (JCC) , 2018, DOI: 10.4236/jcc.2018.65008
Abstract: For elders with dementia, wandering is among the most problematic, frequent and dangerous behavior. Managing wandering behavior has become increasingly imperative due to its high prevalence, negative outcomes and burden on caregivers. We study to propose an active infrared-based method to identify wandering locomotion by monitoring rhythmical repetition of an elder’s indoor motion events. Specifically, we utilize our customized active infrared sensors to collect human indoor motions that will be converted into motion events by using hardware redundancy technique. Each motion event is a directed motion obtained via introducing temporal and dimensions into the spatial motion data. Based on the most cited spatial-temporal patterns of wandering locomotion, a spatiotemporal model is then proposed to identify wandering locomotion from an ongoing sequence of motion events. Experimental evaluation on eight individuals’ real-world motion datasets has shown that our proposed method is able to effectively identify wandering locomotion from repetitive events collected from active infrared sensors with a value over 98% for both accuracy and precision based on properly chosen parameters. Wandering in elders with dementia that follow specific spatiotemporal patterns can be reliably identified by analyzing repetitive motion events collected from active infrared sensors based on the well-known spatiotemporal patterns of wandering locomotion.
Study of System Model of Image Inpainting Combining Subjective Estimation and Impersonal Estimation
Weilan Wang,Huaming Liu
Lecture Notes in Engineering and Computer Science , 2009,
Abstract:
A Fast Input Method for Tibetan Based on Word in Unicode
Weilan Wang,Lingwang Kun
Lecture Notes in Engineering and Computer Science , 2008,
Abstract:
Purification and Properties of Thermostable Catalase in Engineered E. coli
重组大肠杆菌热稳定性过氧化氢酶的纯化及性质研究

Wang Fanqing Wang Zhengxiang Shao Weilan Liu Jiquan Xu Chengyong Zhuge Jian,
王凡强
,王正祥,邵蔚蓝,刘吉泉,徐成勇,诸葛健

微生物学报 , 2002,
Abstract: A thermostable catalase in engineered bacterium E. coli was purified to electrophoretic homogenenity by heat treatment, ammonium sulfate fractionation precipitation, DEAE-A50 ion exchange chromatography, HiPrep 16/10 Phenyl hydrophobic interaction chromatography and Superdex200 HR 10/30 size exclusion chromatography with 187.2-fold purification and 9.8% recovery. The optimum reaction temperature and pH of this recombinant catalase were 70 degrees C and 7.0 respectively. The catalase is stable below 60 degrees C and at pH range 3-8. The residual activity of the catalase was about 60% after treated at 70 degrees C for 60 minutes and 80 degrees C for 10 minutes. The apprant Km and Vmax value of the catalase were 7.75 mmol/L and 27.8 mmol.min-1.mg-1 respectively. The affects of some metal ions and compounds on this enzyme were shown. Zn2+, Ba2+, Mn2+ of 1 mmol/L could completely inactivate the enzyme, EDTA of 50 mmol/L had no affect on activity.
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