scholarly journals Rational mutagenesis by engineering disulphide bonds improves Kluyveromyces lactis beta-galactosidase for high-temperature industrial applications

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Agustín Rico-Díaz ◽  
María-Efigenia Álvarez-Cao ◽  
Juan-José Escuder-Rodríguez ◽  
María-Isabel González-Siso ◽  
M. Esperanza Cerdán ◽  
...  
Keyword(s):  
High Temperature ◽  
Kluyveromyces Lactis ◽  
Industrial Applications ◽  
Disulphide Bonds ◽  
Rational Mutagenesis ◽  
Beta Galactosidase

Electron energy loss near edge structures of intermetallic alloys and grain boundaries in NiAl

1996 ◽  
Vol 54 ◽  
pp. 522-523
Author(s):  
G.A. Botton ◽  
C.J. Humphreys
Keyword(s):  
High Temperature ◽  
Transition Metal ◽  
Energy Loss ◽  
Grain Boundaries ◽  
Industrial Applications ◽  
Edge Structure ◽  
Structural Applications ◽  
Yield Behaviour ◽  
Late Transition ◽  
Metal Aluminides

Transition metal aluminides are of great potential interest for high temperature structural applications. Although these materials exhibit good mechanical properties at high temperature, their use in industrial applications is often limited by their intrinsic room temperature brittleness. Whilst this particular yield behaviour is directly related to the defect structure, the properties of the defects (in particular the mobility of dislocations and the slip system on which these dislocations move) are ultimately determined by the electronic structure and bonding in these materials. The lack of ductility has been attributed, at least in part, to the mixed bonding character (metallic and covalent) as inferred from ab-initio calculations. In this work, we analyse energy loss spectra and discuss the features of the near edge structure in terms of the relevant electronic states in order to compare the predictions on bonding directly with spectroscopic experiments. In this process, we compare spectra of late transition metal (TM) to early TM aluminides (FeAl and TiAl) to assess whether differences in bonding can also be detected. This information is then discussed in terms of bonding changes at grain boundaries in NiAl.

ALUMINUM 1100

Alloy Digest ◽  
1974 ◽  
Vol 23 (2) ◽  
Keyword(s):  
Corrosion Resistance ◽  
Shear Strength ◽  
High Temperature ◽  
Physical Properties ◽  
Tensile Properties ◽  
Pure Aluminum ◽  
Heat Treating ◽  
Industrial Applications ◽  
Temperature Performance ◽  
Commercially Pure

Abstract ALUMINUM 1100 is commercially pure aluminum and is characterized by its excellent ability to be drawn, spun, stamped or forged. It has good weldability, excellent resistance to corrosion and many home, architectural and industrial applications. This datasheet provides information on composition, physical properties, hardness, elasticity, tensile properties, and shear strength as well as fatigue. It also includes information on low and high temperature performance, and corrosion resistance as well as forming, heat treating, machining, and joining. Filing Code: Al-44. Producer or source: Various aluminum companies. Originally published October 1956, revised February 1974.

PLATINUM

Alloy Digest ◽  
1970 ◽  
Vol 19 (11) ◽  
Keyword(s):  
Corrosion Resistance ◽  
High Temperature ◽  
Heat Treating ◽  
Industrial Applications ◽  
High Melting ◽  
High Melting Point ◽  
White Metal ◽  
Temperature Performance ◽  
Wide Range ◽  
Corrosion And Oxidation

Abstract PLATINUM is a soft, ductile, white metal which can be readily worked either hot or cold. It has a wide range of industrial applications because of its excellent corrosion and oxidation resistance and its high melting point. This datasheet provides information on composition, physical properties, hardness, elasticity, and tensile properties. It also includes information on high temperature performance and corrosion resistance as well as forming, heat treating, machining, and joining. Filing Code: Pt-1. Producer or source: Matthey Bishop Inc..

KUBOTA HK40 and HK50

Alloy Digest ◽  
2007 ◽  
Vol 56 (10) ◽  
Keyword(s):  
High Temperature ◽  
Physical Properties ◽  
Carbon Content ◽  
Tensile Properties ◽  
Oxidation Resistance ◽  
Heat Treating ◽  
Industrial Applications ◽  
High Temperature Strength ◽  
Ni Alloys ◽  
Moderately High Temperature

Abstract Kubota alloys HK40 and HK50 are austenitic Fe-Cr-Ni alloys that have been standard heat-resistant materials for more than four decades. With moderately high temperature strength, oxidation resistance, and carburization resistance the alloys are used in a wide variety of industrial applications. HK 50 has slightly higher carbon content. This datasheet provides information on composition, physical properties, and tensile properties as well as creep. It also includes information on casting, heat treating, machining, and joining. Filing Code: SS-998. Producer or source: Kubota Metal Corporation, Fahramet Division.

Oxa-Michael polyaddition of vinylsulfonylethanol for aliphatic polyethersulfones

2021 ◽  
Author(s):  
Nicole Ziegenbalg ◽  
Ruth Lohwasser ◽  
Giovanni D’Andola ◽  
Torben Adermann ◽  
Johannes Christopher Brendel
Keyword(s):  
Refractive Index ◽  
High Temperature ◽  
Flame Retardant ◽  
Chemical Resistance ◽  
High Refractive Index ◽  
Industrial Applications ◽  
Interesting Class ◽  
The Common ◽  
Flame Retardant Properties

Polyethersulfones are an interesting class of polymers for industrial applications due to their unusual properties such as a high refractive index, flame-retardant properties, high temperature and chemical resistance. The common...

scholarly journals Functional homology between the yeast regulatory proteins GAL4 and LAC9: LAC9-mediated transcriptional activation in Kluyveromyces lactis involves protein binding to a regulatory sequence homologous to the GAL4 protein-binding site.

1987 ◽  
Vol 7 (12) ◽  
pp. 4400-4406 ◽  
Author(s):  
K D Breunig ◽  
P Kuger
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Transcriptional Activation ◽  
Kluyveromyces Lactis ◽  
Regulatory Protein ◽  
Binding Activity ◽  
Protein Binding Site ◽  
Regulatory Sequence ◽  
Functional Homology ◽  
Beta Galactosidase

As shown previously, the beta-galactosidase gene of Kluyveromyces lactis is transcriptionally regulated via an upstream activation site (UASL) which contains a sequence homologous to the GAL4 protein-binding site in Saccharomyces cerevisiae (M. Ruzzi, K.D. Breunig, A.G. Ficca, and C.P. Hollenberg, Mol. Cell. Biol. 7:991-997, 1987). Here we demonstrate that the region of homology specifically binds a K. lactis regulatory protein. The binding activity was detectable in protein extracts from wild-type cells enriched for DNA-binding proteins by heparin affinity chromatography. These extracts could be used directly for DNase I and exonuclease III protection experiments. A lac9 deletion strain, which fails to induce the beta-galactosidase gene, did not contain the binding factor. The homology of LAC9 protein with GAL4 (J.M. Salmeron and S. A. Johnston, Nucleic Acids Res. 14:7767-7781, 1986) strongly suggests that LAC9 protein binds directly to UASL and plays a role similar to that of GAL4 in regulating transcription.

scholarly journals Insights into the Maturation of Pernisine, a Subtilisin-Like Protease from the Hyperthermophilic Archaeon Aeropyrum pernix

2020 ◽  
Vol 86 (17) ◽  
Author(s):  
Miha Bahun ◽  
Marko Šnajder ◽  
Dušan Turk ◽  
Nataša Poklar Ulrih
Keyword(s):  
High Temperature ◽  
High Temperatures ◽  
Catalytic Domain ◽  
Industrial Applications ◽  
Binding Motif ◽  
Content Type ◽  
Hyperthermophilic Archaeon ◽  
Aeropyrum Pernix ◽  
Autocatalytic Process ◽  
Exceptional Stability

ABSTRACT Pernisine is a subtilisin-like protease that was originally identified in the hyperthermophilic archaeon Aeropyrum pernix, which lives in extreme marine environments. Pernisine shows exceptional stability and activity due to the high-temperature conditions experienced by A. pernix. Pernisine is of interest for industrial purposes, as it is one of the few proteases that has demonstrated prion-degrading activity. Like other extracellular subtilisins, pernisine is synthesized in its inactive pro-form (pro-pernisine), which needs to undergo maturation to become proteolytically active. The maturation processes of mesophilic subtilisins have been investigated in detail; however, less is known about the maturation of their thermophilic homologs, such as pernisine. Here, we show that the structure of pro-pernisine is disordered in the absence of Ca2+ ions. In contrast to the mesophilic subtilisins, pro-pernisine requires Ca2+ ions to adopt the conformation suitable for its subsequent maturation. In addition to several Ca2+-binding sites that have been conserved from the thermostable Tk-subtilisin, pernisine has an additional insertion sequence with a Ca2+-binding motif. We demonstrate the importance of this insertion for efficient folding and stabilization of pernisine during its maturation. Moreover, analysis of the pernisine propeptide explains the high-temperature requirement for pro-pernisine maturation. Of note, the propeptide inhibits the pernisine catalytic domain more potently at high temperatures. After dissociation, the propeptide is destabilized at high temperatures only, which leads to its degradation and finally to pernisine activation. Our data provide new insights into and understanding of the thermostable subtilisin autoactivation mechanism. IMPORTANCE Enzymes from thermophilic organisms are of particular importance for use in industrial applications, due to their exceptional stability and activity. Pernisine, from the hyperthermophilic archaeon Aeropyrum pernix, is a proteolytic enzyme that can degrade infective prion proteins and thus has a potential use for disinfection of prion-contaminated surfaces. Like other subtilisin-like proteases, pernisine needs to mature through an autocatalytic process to become an active protease. In the present study, we address the maturation of pernisine and show that the process is regulated specifically at high temperatures by the propeptide. Furthermore, we demonstrate the importance of a unique Ca2+-binding insertion for stabilization of mature pernisine. Our results provide a novel understanding of thermostable subtilisin autoactivation, which might advance the development of these enzymes for commercial use.

scholarly journals Rational protein design for enhancing thermal stability of industrial enzymes

2020 ◽  
Vol 8 (1) ◽  
pp. 3-17
Author(s):  
Le Quang Anh Tuan
Keyword(s):  
High Temperature ◽  
Protein Engineering ◽  
Protein Design ◽  
Disulfide Bonds ◽  
Industrial Applications ◽  
Enzymatic Reactions ◽  
Industrial Enzymes ◽  
Effective Strategies ◽  
Environmental Treatment ◽  
Pharmaceutical Production

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 conversion of several enzymatic reactions was declined at high temperature. Protein engineering to improve the enzymes’ thermostability is crucial to extend the use of the industrial enzymes and maximize effectiveness of the enzyme-based procesess. Various industrial enzymes with improved thermostability were produced through rational protein engineering using different strategies. This review is not aimed to cover all successful rational protein engineering studies. The review focuses on some effective strategies which have widely used to increase the thermostability of several industrial enzymes through introduction of disulfide bonds and introduction of proline.

scholarly journals Screening For Yeast Phytase Leads to the Identification of a New Cell-Bound and Secreted Activity in Cyberlindnera jadinii CJ2

2021 ◽  
Vol 9 ◽  
Author(s):  
Claudia Capusoni ◽  
Immacolata Serra ◽  
Silvia Donzella ◽  
Concetta Compagno
Keyword(s):  
High Temperature ◽  
Phytic Acid ◽  
Convenient Method ◽  
Kluyveromyces Marxianus ◽  
Food Industry ◽  
Yeast Species ◽  
Industrial Applications ◽  
Industrial Processes ◽  
Acidic Ph ◽  
Initial Screening

Phytic acid is an anti-nutritional compound able to chelate proteins and ions. For this reason, the food industry is looking for a convenient method which allows its degradation. Phytases are a class of enzymes that catalyze the degradation of phytic acid and are used as additives in feed-related industrial processes. Due to their industrial importance, our goal was to identify new activities that exhibit best performances in terms of tolerance to high temperature and acidic pH. As a result of an initial screening on 21 yeast species, we focused our attention on phytases found in Cyberlindnera jadinii, Kluyveromyces marxianus, and Torulaspora delbrueckeii. In particular, C. jadinii showed the highest secreted and cell-bound activity, with optimum of temperature and pH at 50°C and 4.5, respectively. These characteristics suggest that this enzyme could be successfully used for feed as well as for food-related industrial applications.

Optimization of Acidic Labneh Whey Lactose Hydrolysis with Immobilized Beta-Galactosidase Enzyme from Kluyveromyces lactis

2011 ◽  
Vol 10 (7) ◽  
pp. 675-679 ◽  
Author(s):  
Wail- Alomari ◽  
Malik Hadadin ◽  
Ali K. Alsaed ◽  
Khalid Al-Ismail
Keyword(s):  
Kluyveromyces Lactis ◽  
Lactose Hydrolysis ◽  
Beta Galactosidase
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