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11 articles for “Thermostable Enzyme”
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Review ArticleOpen accessEvery word in the titleA Review: Biodegradation and Applications of Keratin Degrading Microorganisms and Keratinolytic Enzymes, Focusing on Thermophiles and Thermostable Serine ProteasesWirojne Kanoksilapatham, Weeranut IntagunKeratins are hard-degrading fibrous proteins, insoluble in water and organic solvents, often accumulated in nature and major components in feathers, skins, hair, horn, nail, hoof etc., Keratin-degrading microorganisms such as bacteria, archaea, actinomycetes and fungi employ keratinases to attack keratin. Keratinases belonging to subtilisin-like serine proteases were classified based on similarity of amino acid sequences. Keratinolytic thermophilic or hyperthermophilic bacteria … …American Journal of Applied Sciences, Vol. 14, Issue 11 · 10 Nov 2017 · 9,981 accessesView PDFCite
Research ArticleOpen accessIn the keywordsOptimization and Molecular Identification of Protease-Producing Thermophilic Bacterial Isolate TUA-26Anthoni Agustien, Mufidhatul Muqarramah, Feskaharny AlamsjahProtease enzymes are used as biocatalysts that can accelerate a reaction. Thermostable enzymes produced by thermophilic bacteria are needed in the industrial field because of their ability to withstand high temperatures. The thermophilic bacterial isolate TUA-26 that produces protease was to analyze the optimum conditions of temperature, pH, agitation, trace elements, carbon sources, and nitrogen sources; the stability of protease … …OnLine Journal of Biological Sciences, Vol. 24, Issue 3 · 6 Apr 2024 · 4,935 accessesView PDFCite
Research ArticleOpen accessIn the abstractEnhancement of Geobacillus thermodenitrificans Lipase Activity and Binding Affinity by Acetone Treatment: Kinetic and in silico InvestigationsAmmar Khazaal Kadhim Almansoori, Alyaa Abdulhussein Alsaedi et al.Lipase Geobacillus thermodenitrificans (LipGt) is a thermostable enzyme that has an optimal activity temperature of 65°C. It can tolerate various organic solvents and has an improved activity, especially in the presence of acetone. In this study, in-vitro and in-silico studies were carried out to investigate the effect of acetone in enhancing the kinetic and binding affinity of LipGt. The LipGt … …American Journal of Biochemistry and Biotechnology, Vol. 20, Issue 4 · 10 Oct 2024 · 4,817 accessesView PDFCite
Research ArticleOpen accessIn the abstractDiscovery of a New Thermostable Chitinase from Streptomyces No. 6Xiaowen Que, Yonghong Bao, Qing Liu et al.Chitinases are a class of hydrolases that hydrolyze the β-1, 4-glycosidic bonds between N-acetyl-D-glucosamine (GlcNAc) in chitin. Among chitinases, thermophilic chitinases and thermostable chitinases have received extensive attention in recent years due to their ability to tolerate higher temperatures and maintain enzyme stability for a longer period of time. However, it has previously been observed that not all chitinases are … …American Journal of Biochemistry and Biotechnology, Vol. 20, Issue 3 · 1 Aug 2024 · 5,115 accessesView PDFCite
Research ArticleOpen accessIn the abstractIn-silico Rational Protein Engineering and Design Approach to Improve Thermostability of a Haloalkane Dehalogenase EnzymeRaghunath Satpathy, V. Badireenath Konkimalla, Jagnyeswar RathaThermostability of enzymes is a major prerequisite for use in industrial enzymology. There are as such no simple general principles for achieving thermostability in case of enzymes as many factors are required to fulfil for different enzymes. The present study describes computational methods to design thermostable haloalkane dehalogenase enzyme using the crystal structure available Protein Data Bank (PDB ID: 1EDE). … …Current Research in Bioinformatics, Vol. 4, Issue 2 · 13 Oct 2015 · 8,279 accessesView PDFCite
Research ArticleOpen accessIn the abstractScreening of Yeast Strains for Pectinolytic Activity: Effects of Different Carbon and Nitrogen Sources in Submerged FermentationsMustafa Oskay, Hüsniye Tansel YalçinTwenty yeast strains were screened for pectinolytic activity, among the strains, only nine were positive for pectinase production. The best strain was Kluyveromyces marxianus NRRL-Y-1109 which gave high quantities of pectinase activity, by submerged fermentation. Different parameters such as incubation time, pH (3.5-7), temperature (20-45°C), nitrogen and carbon source, were optimized. The optimal incubation time, temperature and pH for pectinase … …OnLine Journal of Biological Sciences, Vol. 15, Issue 3 · 22 Jun 2015 · 7,812 accessesView PDFCite
Research ArticleOpen accessIn the abstractHeterologous Expression and Characterization of Thermostable Levansucrase (BsSacB) from Bacillus subtilis BB03Viniti Vaidya, Gajjeraman Prabu, D. Theertha PrasadThermostable levansucrase encoding gene (sacB) with its promoter was isolated from Bacillus subtilis BB03. BsSacB is composed of 1419 bp, encoding 473 amino acid residues and with promoter regions TTGCAA (-35) and TAGAAT (-10). The amino acid sequence analysis of BsSacB showed conserved motifs of microbial fructosyltransferase belonging to Glycoside Hydrolase family 68 (GH68). Comparative analysis of the protein structure … …OnLine Journal of Biological Sciences, Vol. 15, Issue 1 · 25 Mar 2015 · 7,371 accessesView PDFCite
Research ArticleOpen accessIn the abstractUse of a Mixture of Thermophilic Enzymes Produced by the Fungus Thermoascus aurantiacus to Enhance the Enzymatic Hydrolysis of the Sugarcane Bagasse CelluloseJ. R. Monte, W. Carvalho, A. M. F. MilagresProblem statement: The production of hydrolytic enzymes by T. aurantiacus has been performed under solid-state fermentations using lignocellulosic materials. The influences of the inoculum size and of the fermentation medium on the production of hemicellulases and cellulases were studied. Filtrates from the cultures were used to hydrolyze a pulp of sugarcane bagasse and the produced enzymes were shown to be … …American Journal of Agricultural and Biological Sciences, Vol. 5, Issue 4 · 13 Dec 2010 · 9,212 accessesView PDFCite
Research ArticleOpen accessIn the abstractCharacteristics of a Novel Highly Thermostable and Extremely Thermophilic Alkalitolerant Amylase from Hyperthermophilic Bacillus Strain HUTBS71Farouk Al-Quadan, Hazem Akel, Rasha NatshiProblem statement: This study reported the purification and characterization of a novel highly thermostable alkaline amylase from a newly isolated Bacillus strain HUTBS71. Approach: The enzyme was purified using ammonium sulfate precipitation, ion exchange and gel filtration chromatography. Results: Maximum amylase activity (72 U mL-1) was obtained at 100°C after 10 min of incubation. The enzyme was purified 24 fold … …OnLine Journal of Biological Sciences, Vol. 9, Issue 3 · 30 Sep 2009 · 7,400 accessesView PDFCite
Research ArticleOpen accessIn the abstractA Thermostable α-Amylase Producing Natural Variant of Bacillus spp. Isolated From Soil in IranIraj Rasooli, Shakiba D. A. Astaneh, Hojjat Borna, Kamal A. BarchiniThermophilic processes appear more stable, rapid and less expensive and facilitate reactant activity and product recovery. Amylases have a quarter of the world enzyme market and thermostable a-amylases possess extensive commercial applications. Since little work has been done on strain isolation, growth and enzyme yield optimization, the level of thermophilic enzyme production remains relatively low. Therefore, large scale exploitation of … …American Journal of Agricultural and Biological Sciences, Vol. 3, Issue 3 · 30 Sep 2008 · 8,902 accessesView PDFCite