Relevant bibliographies by topics / Enzymes; Peptidase; Protein thermostability

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  2. Dissertations / Theses
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Academic literature on the topic 'Enzymes; Peptidase; Protein thermostability'

Author: Grafiati
Published: 4 June 2021
Last updated: 5 February 2022

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Journal articles on the topic "Enzymes; Peptidase; Protein thermostability"

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Purwani, Ni Nyoman, Caterina Martin, Simone Savino, and Marco W. Fraaije. "Modular Assembly of Phosphite Dehydrogenase and Phenylacetone Monooxygenase for Tuning Cofactor Regeneration." Biomolecules 11, no. 6 (2021): 905. http://dx.doi.org/10.3390/biom11060905.

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The use of multienzyme complexes can facilitate biocatalytic cascade reactions by employing fusion enzymes or protein tags. In this study, we explored the use of recently developed peptide tags that promote complex formation of the targeted proteins: the dimerization-docking and anchoring domain (RIDD–RIAD) system. These peptides allow self-assembly based on specific protein–protein interactions between both peptides and allow tuning of the ratio of the targeted enzymes as the RIAD peptide binds to two RIDD peptides. Each of these tags were added to the C-terminus of a NADPH-dependent Baeyer–V
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Chen, Zhiguo, Yi Fu, Wenbo Xu, and Ming Li. "Molecular Dynamics Simulation of Barnase: Contribution of Noncovalent Intramolecular Interaction to Thermostability." Mathematical Problems in Engineering 2013 (2013): 1–12. http://dx.doi.org/10.1155/2013/504183.

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Bacillus amyloliquefaciensribonuclease Barnase (RNase Ba) is a 12 kD (kilodalton) small extracellular ribonuclease. It has broad application prospects in agriculture, clinical medicine, pharmaceutical, and so forth. In this work, the thermal stability of Barnase has been studied using molecular dynamics simulation at different temperatures. The present study focuses on the contribution of noncovalent intramolecular interaction to protein stability and how they affect the thermal stability of the enzyme. Profiles of root mean square deviation and root mean square fluctuation identify thermostab
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Xu, Zhen, Yunqing Liu, Yunliu Yang, Weihong Jiang, Eddy Arnold, and Jianping Ding. "Crystal Structure of d-Hydantoinase from Burkholderia pickettii at a Resolution of 2.7 Angstroms: Insights into the Molecular Basis of Enzyme Thermostability." Journal of Bacteriology 185, no. 14 (2003): 4038–49. http://dx.doi.org/10.1128/jb.185.14.4038-4049.2003.

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ABSTRACT d-Hydantoinase (d-HYD) is an industrial enzyme that is widely used in the production of d-amino acids which are precursors for semisynthesis of antibiotics, peptides, and pesticides. This report describes the crystal structure of d-hydantoinase from Burkholderia pickettii (HYDBp) at a 2.7-Å resolution. The structure of HYDBp consists of a core (α/β)8 triose phosphate isomerase barrel fold and a β-sheet domain, and the catalytic active site consists of two metal ions and six highly conserved amino acid residues. Although HYDBp shares only moderate sequence similarity with d-HYDs from
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Suleimanova, Aliya, Daria Bulmakova, and Margarita Sharipova. "Heterologous Expression of Histidine Acid Phytase From Pantoea sp. 3.5.1 in Methylotrophic Yeast Pichia Pastoris." Open Microbiology Journal 14, no. 1 (2020): 179–89. http://dx.doi.org/10.2174/1874285802014010179.

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Background and Objective: The major storage form of phosphorus in plant-derived feed is presented by phytates and not digested by animals. Phytases are able to hydrolyze phytates and successfully used as feed additives. Nevertheless, nowadays, there is a constant search of new phytases and expression systems for better production of these enzymes. In this study, we describe cloning and expression of gene encoding histidine acid phytase from Pantoea sp. 3.5.1 using methylotrophic yeast Pichia pastoris as the host. Methods: The phytase gene was placed under the control of the methanol-inducible
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Camarero, S., I. Pardo, A. I. Cañas, et al. "Engineering Platforms for Directed Evolution of Laccase from Pycnoporus cinnabarinus." Applied and Environmental Microbiology 78, no. 5 (2011): 1370–84. http://dx.doi.org/10.1128/aem.07530-11.

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ABSTRACTWhile thePycnoporus cinnabarinuslaccase (PcL) is one of the most promising high-redox-potential enzymes for environmental biocatalysis, its practical use has to date remained limited due to the lack of directed evolution platforms with which to improve its features. Here, we describe the construction of a PcL fusion gene and the optimization of conditions to induce its functional expression inSaccharomyces cerevisiae, facilitating its directed evolution and semirational engineering. The native PcL signal peptide was replaced by the α-factor preproleader, and this construct was subjecte
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Tuan, Le Quang Anh. "Rational protein design for enhancing thermal stability of industrial enzymes." ENGINEERING AND TECHNOLOGY 8, no. 1 (2020): 3–17. http://dx.doi.org/10.46223/hcmcoujs.tech.en.8.1.340.2018.

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Enzymes possessing many excellent properties such as high selectivity, consuming less energy, and producing less side products or waste have been widely applied as biocatalysts in pharmaceutical production and many industries such as biofuel, biomaterials, biosensor, food, and environmental treatment. Although enzymes have shown its potential as biocatalysts for many industrial applications, natural enzymes were not originated for manufacturing process which requires harsh reaction conditions such as high temperature, alkaline pH, and organics solvents. It was reported that reduction of final
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Goodenough, Peter W., and John A. Jenkins. "Protein engineering to change thermal stability for food enzymes." Biochemical Society Transactions 19, no. 3 (1991): 655–62. http://dx.doi.org/10.1042/bst0190655.

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Summary In this review we have briefly indicated how the present state of knowledge allows proteins to be mutated to increase or decrease stability. We have discussed experiments on both model proteins and those of relevance to the food industry, and show how hydrophobic forces are a major driving force for folding as well as having a major role in thermostability. We have also indicated the large contribution that hydrogen bonding, electrostatic interactions and, in a less well predicted way, disulphide bridges make to thermostability.
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Palomeque-Messia, P., V. Quittre, M. Leyh-Bouille, et al. "Secretion by overexpression and purification of the water-soluble Streptomyces K15 dd-transpeptidase/penicillin-binding protein." Biochemical Journal 288, no. 1 (1992): 87–91. http://dx.doi.org/10.1042/bj2880087.

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Though synthesized with a cleavable signal peptide and devoid of membrane anchors, the 262-amino-acid-residue Streptomyces K15 DD-transpeptidase/penicillin-binding protein is membrane-bound. Overexpression in Streptomyces lividans resulted in the export of an appreciable amount of the synthesized protein (4 mg/litre of culture supernatant). The water-soluble enzyme was purified close to protein homogeneity with a yield of 75%. It requires the presence of 0.5 M-NaCl to remain soluble. It is indistinguishable from the detergent-extract wild-type enzyme with respect to molecular mass, thermostabi
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Nakabayashi, Makoto, Saori Kamachi, Dominggus Malle, et al. "Construction of thermostable cellobiohydrolase I from the fungus Talaromyces cellulolyticus by protein engineering." Protein Engineering, Design and Selection 32, no. 1 (2019): 33–40. http://dx.doi.org/10.1093/protein/gzz001.

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Abstract Fungus-derived GH-7 family cellobiohydrolase I (CBHI, EC 3.2.1.91) is one of the most important industrial enzymes for cellulosic biomass saccharification. Talaromyces cellulolyticus is well known as a mesophilic fungus producing a high amount of CBHI. Thermostability enhances the economic value of enzymes by making them more robust. However, CBHI has proven difficult to engineer, a fact that stems in part from its low expression in heterozygous hosts and its complex structure. Here, we report the successful improvement of the thermostability of CBHI from T. cellulolyticus using our h
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Konno, Naotake, Kiyohiko Igarashi, Naoto Habu, Masahiro Samejima, and Akira Isogai. "Cloning of the Trichoderma reesei cDNA Encoding a Glucuronan Lyase Belonging to a Novel Polysaccharide Lyase Family." Applied and Environmental Microbiology 75, no. 1 (2008): 101–7. http://dx.doi.org/10.1128/aem.01749-08.

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ABSTRACT The filamentous fungus Trichoderma reesei produces glucuronan lyase (TrGL) when it is grown on β-(1→4)-polyglucuronate (cellouronate) as a sole carbon source. The cDNA encoding TrGL was cloned, and the recombinant enzyme was heterologously expressed in Pichia pastoris. The cDNA of TrGL includes a 777-bp open reading frame encoding a 20-amino-acid signal peptide and the 238-amino-acid mature protein. The amino acid sequence showed no similarity to the amino acid sequences of previously described functional proteins, indicating that the enzyme should be classified in a novel polysacchar
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Dissertations / Theses on the topic "Enzymes; Peptidase; Protein thermostability"

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Singleton, Martin Robert. "Studies on pyrrolidone carboxyl peptidase from the archaeon Thermococcus litoralis." Thesis, University of Exeter, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.245927.

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Stewart, Richard John. "Increasing the thermostability of barley (1->3,1->4)-B-glucanases /." Title page, abstract and contents only, 1999. http://web4.library.adelaide.edu.au/theses/09APSP/09apsps851.pdf.

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Burrows, Camilla S. "Protein engineering of thermostability in the cysteine proteinase caricain." Thesis, University of Kent, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.365248.

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Muir, Jacqueline M. "Citrate synthase from the hyperthermophilic archaeon, Pyrococcus furiosus." Thesis, University of Bath, 1995. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260247.

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"Effect of protein thermostability on the cooperative function of split enzymes." Thesis, 2010. http://hdl.handle.net/1911/61965.

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Although the effects of mutational events on protein function cannot yet be predicted a priori, molecular evolution studies have shown that the tolerance of protein structure and function to random mutation is positively correlated with the thermostability of the protein mutated. To test whether thermostability also influences protein function upon random fission, I have characterized the function of split Bacillus subtilis and Thermotoga neapolitana adenylate kinases (AK Bs and AKTn, respectively), enzymes that are required to maintain adenine energy charge. Using libraries of split AKBs and
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Pillay, Sarveshni. "Improvement of thermostability of a fungal xylanase using error-prone polymerase chain reaction (EpPCR)." Thesis, 2007. http://hdl.handle.net/10321/310.

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Thesis (M.Tech.: Biotechnology)-Dept. of Biotechnology, Durban University of Technology, 2007 vi, 92 leaves<br>Interest in xylanases from different microbial sources has increased markedly in the past decade, in part because of the application of these enzymes in a number of industries, the main area being the pulp and paper industry. While conventional methods will continue to be applied to enzyme production from micro-organisms, the application of recombinant DNA techniques is beginning to reveal important information on the molecular basis and this knowledge is now being applied both in the
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Larasati, Rezka, and Rezka Larasati. "Inhibition Potencies Of Guava Leaf Extracts And Synthetic Triazole Compounds On Protein Tyrosine Phosphatase 1B (PTP1B) And Dipeptidyl Peptidase-IV (DPP-IV) Enzymes." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/13930302262140466112.

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碩士<br>亞洲大學<br>保健營養生技學系碩士班<br>99<br>Diabetes mellitus (DM) is a chronic disease that is characteristic of hyperglycemia with various etiologies. The rising prevalence of diabetes mellitus has fueled an intensified search for new therapeutic treatments. Dipeptidyl peptidase IV (DPP-IV) and protein tyrosine phosphatase 1b (PTP1B) are two major enzymes that have recently emerged as biological targets for anti-diabetic compound development. The validation of specific inhibitor to PTP1B and DPP-IV is required for treating diabetes. Guava leaf has been used as a folk medicine traditionally because of
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Polatová, Daniela. "Příprava a biochemická charakterizace proteasového inhibitoru equistatinu." Master's thesis, 2017. http://www.nusl.cz/ntk/nusl-348911.

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Equistatin from the sea anemone Actinia equina contains a protein domain Eqd2 which inhibits aspartic peptidases and has not been characterized in detail. Recombinant Eqd2 was produced in the yeast expression system, and a protocol for its chromatographic purification was designed. The inhibitory specificity of Eqd2 was determined using a fluorescence inhibition assay, showing that Eqd2 is a highly selective inhibitor of cathepsin D-like and pepsin-like aspartic peptidases of family A1. Furthermore, size exclusion chromatography was used to analyze the Eqd2-peptidase complex and Eqd2 oligomeri
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Rybáriková, Renata. "Rekombinantní exprese a funkční charakterizace rostlinných Kunitzových inhibitorů." Master's thesis, 2021. http://www.nusl.cz/ntk/nusl-449050.

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PDI ("potato cathepsin D inhibitor ") and NID ("novel inhibitor of cathepsin D ") from potato (Solanum tuberosum) belong to the protein family of Kunitz inhibitors (I3 family, Merops database). These 20 kDa isoinhibitors with the typical β-trefoil architecture inhibit aspartic and serine peptidases. In this thesis, the constructs for recombinant expression of PDI and NID in the yeast Pichia pastoris system were prepared and high-producing colonies were selected. Both proteins were identified in the cultivation media by mass spectrometry and N-terminal sequencing. A purification protocol for PD
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Book chapters on the topic "Enzymes; Peptidase; Protein thermostability"

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Dore, Timothy M., and Walter K. Schmidt. "Isoprenylated Protein Peptidase Rce1p." In Handbook of Proteolytic Enzymes. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00398-7.

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Diruggiero, Jocelyne, and Frank T. Robb. "Enzymes of Central Nitrogen Metabolism from Hyperthermophiles: Characterization, Thermostability, and Genetics." In Advances in Protein Chemistry. Elsevier, 1996. http://dx.doi.org/10.1016/s0065-3233(08)60365-4.

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Yadav, Durgavati, Vivek Pandey, Shivani Srivastava, and Yamini Bhusan Tripathi. "New Herbal Approaches for the Treatment of Diabetic Kidney Diseases and Its Therapeutic Implications." In Food Science and Nutrition. IGI Global, 2018. http://dx.doi.org/10.4018/978-1-5225-5207-9.ch015.

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Diabetic Kidney Diseases (DKD) is a very serious complication of diabetes. There is recent steep rise in the prevalence of metabolic syndrome and DKD worldwide. Factors responsible for intraglomerular hypertension include activation of various vasoactive systems, polyol pathway, oxidative stress, inflammation and protein kinase C. Sodium-Dependent Glucose Co-Transporter (SGLT-2) inhibitors, DPP-IV (Dipeptidyl peptidase-4) inhibitors are being develop to manage the hyperglycemia and oxidative stress induced inflammatory cascade. Herbal drugs have gained increasing popularity; are complex mixtures of polyphenols and phytochemicals from any raw or processed part of a plant, including leaves. Herbal drugs in this modern era are preferred due to its lesser side effects. Various preparations are presently used for ameliorating the effect of DKD. Since, medicinal plants have been reported to affect various metabolic receptors, enzymes and signaling cascade. Above book chapter explains the involvement of different phytochemicals in biological pathway associated with the kidney damage.
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Gunathilaka, Thilina, Lakshika Rangee Keertihirathna, and Dinithi Peiris. "Advanced Pharmacological Uses of Marine Algae as an Anti-Diabetic Therapy." In Pharmacognosy - Medicinal Plants [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96807.

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Marine seaweeds are a promising source of bioactive secondary metabolites that can be utilized in drug development and nutraceuticals. Diabetes mellitus is a leading non-communicable disease, and it is the third leading cause of death worldwide. Among the types of diabetes, type 2 became the major health problem as it is associated with severe health complications. Since available oral hypoglycemic drugs cause several adverse effects, it is worth searching for a natural cure with fewer or no side effects that may benefit patients with type 2 diabetes. Among the marine seaweeds, brown and red seaweeds are extensively studied for the anti-diabetic activity compared to the green seaweeds. Bioactive compounds present in marine seaweeds possess anti-diabetic potential through diverse mechanisms, mainly by reducing postprandial hyperglycemia and associated complication. Most of the studies emphasized that the marine seaweeds control the hyperglycemic condition by inhibiting carbohydrate hydrolyzing α-amylase,α glucosidase enzymes, and the inhibitory effect of dipeptide peptidase-4 that are involved in the degradation of incretins. Similarly, bioactive compounds in marine seaweeds can reduce diabetes complications by inhibiting angiotensin-converting enzymes, aldose reductase, protein tyrosine phosphatase 1B enzyme. This chapter focuses on the anti-diabetic potential of marine brown, green, and red seaweeds through different mechanisms.
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Journal articles
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