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Titlebook: Extracellular Enzymes of Microorganisms; J. Chaloupka,Vladimir Krumphanzl (Corresponding Me Book 1987 Plenum Press, New York 1987 biochemi

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發(fā)表于 2025-3-21 19:47:12 | 只看該作者 |倒序瀏覽 |閱讀模式
書目名稱Extracellular Enzymes of Microorganisms
編輯J. Chaloupka,Vladimir Krumphanzl (Corresponding Me
視頻videohttp://file.papertrans.cn/320/319928/319928.mp4
圖書封面Titlebook: Extracellular Enzymes of Microorganisms;  J. Chaloupka,Vladimir Krumphanzl (Corresponding Me Book 1987 Plenum Press, New York 1987 biochemi
描述Czechoslovak Society for Microbiology and Institute of Microbiology of the Czechoslovak Academy of Sciences organized an international symposium "Extracellular enzymes of microorganisms" in September 1986. The symposium took place in a small South-Bohemian town Bechyne and this book includes the main contributions presented at the meeting. The study of microbial extracellular enzymes is a rapidly developing field of science, which is important both from practical and theoretical point of view. On one hand, microbial enzymes are nowadays broadly used in various branches of industry, medicine and agriculture, on the other hand, their study contributes substantially to our knowledge of problems of protein secretion, regulation of protein synthesis as related with growth and cytodifferentiation and - las,t but not least - it brings data important for the elucidation of evolutionary pathways. Microbial enzymology also represents a bordering area between different scientific disciplines such as microbiology, biochemistry, genetics, biotechnology and other and demonstrates that only their integration brings about a substantial progress in the development of our understanding of biological
出版日期Book 1987
關(guān)鍵詞biochemistry; enzymes; protein; protein synthesis; synthesis
版次1
doihttps://doi.org/10.1007/978-1-4684-1274-1
isbn_softcover978-1-4684-1276-5
isbn_ebook978-1-4684-1274-1
copyrightPlenum Press, New York 1987
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沙發(fā)
發(fā)表于 2025-3-21 20:47:26 | 只看該作者
sium "Extracellular enzymes of microorganisms" in September 1986. The symposium took place in a small South-Bohemian town Bechyne and this book includes the main contributions presented at the meeting. The study of microbial extracellular enzymes is a rapidly developing field of science, which is im
板凳
發(fā)表于 2025-3-22 00:47:52 | 只看該作者
https://doi.org/10.1007/978-981-32-9162-1han thermolabile is more versatile. In addition, α-amylase genes of barley [25], rats [18] as well as human beings [22], etc. [21] have been transferred to . by the use of either phage or vector plasmid.
地板
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5#
發(fā)表于 2025-3-22 09:50:11 | 只看該作者
A Society of Dignified Equals and Inequalityus transformation system, with a vector containing the . gene as a selectable marker. In the second system, a vector containing the hygromycin B resistance gene as a dominant selectable marker is used for transformation. This system is also applicable to ..
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發(fā)表于 2025-3-22 16:32:05 | 只看該作者
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發(fā)表于 2025-3-22 17:40:03 | 只看該作者
Conclusion: The Future of Comedy,rated by three amino acid residues. The mature enzyme is homologous with two other liquefying α-amylases from . and .. The enzyme is initially secreted into the periplasm of ., but when sufficient amount of α-amylase has accumulated in the stationary phase of growth, it is also found in the culture medium.
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發(fā)表于 2025-3-22 21:37:17 | 只看該作者
New Gene-Transfer Systems for ,us transformation system, with a vector containing the . gene as a selectable marker. In the second system, a vector containing the hygromycin B resistance gene as a dominant selectable marker is used for transformation. This system is also applicable to ..
9#
發(fā)表于 2025-3-23 04:12:00 | 只看該作者
Stimulation of a Proteinase Synthesis in , by Netropsinxtracellular metalloproteinase in Bacillus megaterium [4]. The antibiotic affected in a similar way the formation of the proteinase not only during sporulation but also during growth. The effect of the antibiotic on the proteinase regulation was further studied and the results are presented in this communication.
10#
發(fā)表于 2025-3-23 06:23:24 | 只看該作者
Thermostable Alpha Amylase of ,: Cloning, Expression, and Secretion by ,rated by three amino acid residues. The mature enzyme is homologous with two other liquefying α-amylases from . and .. The enzyme is initially secreted into the periplasm of ., but when sufficient amount of α-amylase has accumulated in the stationary phase of growth, it is also found in the culture medium.
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