نتایج جستجو برای: thermostable
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© 2013 Fossi and Tavea, licensee InTech. This is an open access chapter distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Application of Amylolytic Lactobacillus fermentum 04BBA19 in Fermentation for Simul...
Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM(-1) s(-1). Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5 degrees C.
Crystallization and preliminary X-ray analysis of the highly thermostable sweet protein Mabinlin II.
Mabinlin II is a thermostable sweet protein isolated from the mature seeds of Capparis masaikai Levl. grown in the subtropical region of the South of China. The Mabinlin II has been crystallized and diffraction data were collected to 1.7 A resolution. The crystal belongs to space group C2 with unit cell parameters a = 80.11 A, b = 51.08 A, c = 47.34 A, beta = 122.77 degrees.
We determined the transcriptional start site of the thermostable direct hemolysin-related hemolysin gene (trh) of Vibrio parahaemolyticus by using a PCR-based method and identified the promoter. Mutagenic analysis indicated that the promoter-bearing region rather than its downstream inverted repeat sequence was responsible for the low-revel of trh transcription.
Spores of Bacillus subtilis are significantly more resistant to wet heat than are their vegetative cell counterparts. Analysis of the effects of mutations in and the expression of fusions of a coding gene for a thermostable beta-galactosidase to a number of heat shock genes has shown that heat shock proteins play no significant role in the wet heat resistance of B. subtilis spores.
Heat-treated Escherichia coli producing Thermus polyphosphate kinase regenerated ATP by using exogenous polyphosphate. This recombinant could be used as a platform to produce valuable compounds in combination with thermostable phosphorylating or energy-requiring enzymes. In this work, we demonstrated the production of fructose 1,6-diphosphate from fructose and polyphosphate.
BACKGROUND Screening is a routine procedure for isolation of microorganisms which are able to produce special metabolites. Purified thermostable α-amylase from bacterial sources is widely used in different industries. In this study we analyzed samples collected from three different hot springs in Iran to detect any strains capable of producing thermostable α-amylase. MATERIALS AND METHODS Hot...
Molecular dynamics simulations were employed to study how protein solution structure and dynamics are affected by adaptation to high temperature. Simulations were carried out on a para-nitrobenzyl esterase (484 residues) and two thermostable variants that were generated by laboratory evolution. Although these variants display much higher melting temperatures than wild-type (up to 18 degrees C h...
Proteins in thermophilic organisms remain stable and function optimally at high temperatures. Owing to their important applicability in many industrial processes, such thermostable proteins have been studied extensively, and several structural factors attributed to their enhanced stability. How these factors render the emergent property of thermostability to proteins, even in situations where n...
Cytochrome P450 BM-3 is a soluble fatty acid hydroxylase composed of a heme domain and a reductase domain on a single polypeptide chain. We recently described a laboratoryevolved variant of the P450 BM-3 heme domain which functions as an H2O2-driven hydroxylase (TMperoxygenase∫) and does not require NADPH, O2, or the reductase. This variant, which we named 21B3, allows us to carry out cytochrom...
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