Calculation of the molecular masses of two newly synthesized thermostable enzymes isolated from thermophilic microorganisms

1995 ◽  
Vol 666 (1) ◽  
pp. 188-193 ◽  
Author(s):  
M.H. Gey ◽  
K.K. Unger
Keyword(s):  
Thermostable Enzymes ◽  
Thermophilic Microorganisms ◽  
Molecular Masses

scholarly journals ISOLATION OF THERMOPHILIC LIPASE PRODUCING BACTERIUM FROM HOT SPRINGS AT THE EAST COAST OF PENINSULAR MALAYSIA

2021 ◽  
Vol 11 (1) ◽  
pp. 1-10
Author(s):  
Tengku Hamid ◽  
◽  
Nur Abidin ◽  
Nurmusfirah Hasan ◽  
◽  
...  
Keyword(s):  
Hot Springs ◽  
East Coast ◽  
Hot Spring ◽  
Thermophilic Bacteria ◽  
Natural Habitat ◽  
Primary Source ◽  
Industrial Applications ◽  
Peninsular Malaysia ◽  
Thermostable Enzymes ◽  
Thermophilic Microorganisms

Hot spring is a natural habitat for thermophilic bacteria and the primary source of thermostable enzymes useful in industrial applications. In Malaysia, the search for thermophilic organisms has been focused on hot springs, especially on the peninsular West coast. In this work, lipase or esterase producing thermophilic microorganisms were isolated from East coast hot springs in Pahang and Terengganu's states. Morphological and biochemical analysis were carried out on Isolates LH1, LH2, LH3, LH4, LH5, B2B2 and S1B4, which showed that they are gram positive, aerobic, spore forming, and motile organisms. All of the seven isolates showed the ability to grow at 45°C and formed hydrolysis zones on tributyrin agar plates. However, only isolate B2B2 and S1B4 were able to thrive at higher temperatures of up to 65°C. The genotypic characterisation was carried out using 16S rRNA sequencing. Bacillus and Geobacillus species were found to be the dominant bacteria isolated from these hot springs. From La hot spring, isolate LH1 (MT 645486), Isolates LH2 (MT645483), LH3 (MT645484), LH4 (MT 645485) and LH5 (MT 645487) were all closely related to Bacillus sp. (at 97.3-97.9%). Meanwhile, from Bentong and Sungai Lembing hot springs, isolates B2B2 (MT668631) and S1B4 (MT668632) were near related to either Geobacillus kaustophilus or Geobacillus thermoleovorans; each at 98.5% and 97.9% similarity, respectively. These strains from Geobacillus sp. were able to thrive at higher temperature and their thermostable esterases or lipases have properties useful for biotechnological applications.

scholarly journals Thermostable Cellulases / Xylanases From Thermophilic and Hyperthermophilic Microorganisms: Current Perspective

2021 ◽  
Vol 9 ◽  
Author(s):  
Samaila Boyi Ajeje ◽  
Yun Hu ◽  
Guojie Song ◽  
Sunday Bulus Peter ◽  
Richmond Godwin Afful ◽  
...  
Keyword(s):  
Value Added ◽  
High Yield ◽  
Industrial Enzymes ◽  
Efficient Technology ◽  
Thermostable Enzymes ◽  
Thermophilic Microorganisms ◽  
Economic Production ◽  
Current Perspective ◽  
Low Energy Consumption ◽  
Enzymatic Depolymerization

The bioconversion of lignocellulose into monosaccharides is critical for ensuring the continual manufacturing of biofuels and value-added bioproducts. Enzymatic degradation, which has a high yield, low energy consumption, and enhanced selectivity, could be the most efficient and environmentally friendly technique for converting complex lignocellulose polymers to fermentable monosaccharides, and it is expected to make cellulases and xylanases the most demanded industrial enzymes. The widespread nature of thermophilic microorganisms allows them to proliferate on a variety of substrates and release substantial quantities of cellulases and xylanases, which makes them a great source of thermostable enzymes. The most significant breakthrough of lignocellulolytic enzymes lies in lignocellulose-deconstruction by enzymatic depolymerization of holocellulose into simple monosaccharides. However, commercially valuable thermostable cellulases and xylanases are challenging to produce in high enough quantities. Thus, the present review aims at giving an overview of the most recent thermostable cellulases and xylanases isolated from thermophilic and hyperthermophilic microbes. The emphasis is on recent advancements in manufacturing these enzymes in other mesophilic host and enhancement of catalytic activity as well as thermostability of thermophilic cellulases and xylanases, using genetic engineering as a promising and efficient technology for its economic production. Additionally, the biotechnological applications of thermostable cellulases and xylanases of thermophiles were also discussed.

New thermophilic prokaryotes with hydrolytic activities

2018 ◽  
Vol 39 (3) ◽  
pp. 122
Author(s):  
Elizaveta Bonch-Osmolovskaya ◽  
Alexander Elcheninov ◽  
Ksenia Zayulina ◽  
Ilya Kublanov
Keyword(s):  
Textile Industry ◽  
Thermophilic Bacteria ◽  
Hydrolytic Enzymes ◽  
Natural Environments ◽  
Thermostable Enzymes ◽  
Thermophilic Microorganisms ◽  
Hydrolytic Activities ◽  
Polymeric Substrates ◽  
Thermophilic Organisms ◽  
Industrial Demand

Thermophilic microorganisms are capable of growing on polymeric substrates and have been intensively studied for their enzymes, thermostable hydrolases (glycosidases, proteinases, lipases), which have important applications in many fields of bioindustry: production of detergents, food processing, paper and textile industry, biofuel formation from organic wastes, etc.1. The advantages of thermostable enzymes application are in their higher stability not only against temperature, but also against high or low pH, presence of detergents, etc. High temperature increases solubility of substrates2, thus making them more available, and significantly decreases the contamination risks. Many highly stable hydrolases, produced by thermophilic bacteria and archaea have been discovered3–6; however, due to continuous industrial demand and our knowledge that natural environments are a significant reservoir of genetic and hence functional diversity7, new thermophilic organisms producing hydrolytic enzymes are still of high interest. Here we present our achievements in isolation of novel thermophilic bacteria and archaea with various hydrolytic activities.

scholarly journals Proteases from Canavalia ensiformis: Active and Thermostable Enzymes with Potential of Application in Biotechnology

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Rayane Natshe Gonçalves ◽  
Suellen Duarte Gozzini Barbosa ◽  
Raquel Elisa da Silva-López
Keyword(s):  
Divalent Cations ◽  
Peptidase Activity ◽  
Leaf Extracts ◽  
Thermostable Enzymes ◽  
Biotechnological Potential ◽  
Good Thermal Stability ◽  
Sds Page ◽  
Molecular Masses ◽  
Triton X ◽  
Different Levels

Extracts of leaves, seeds, roots, and stem from a tropical legume, C. ensiformis, were prepared employing buffers and detergent in aqueous solution. Leaf extracts had the highest protein content and the most pronounced peptidase activity with optimal pH in the neutral to alkaline range. All extracts exhibited peaks of activity at various pH values, suggesting the presence of distinctive classes of proteases. N-α-Tosyl-L-arginine methyl ester hydrolysis was maximal at 30°C to 60°C and peptidase activity from all extracts presented very good thermal stability after 24 h incubation at 70°C. C. ensiformis proteases exhibited molecular masses of about 200–57, 40–37, and 20–15 kDa by SDS-PAGE analysis. These enzymes cleaved hemoglobin, bovine serum albumin, casein, and gelatin at different levels. Serine and metalloproteases are the major proteases in C. ensiformis extracts, modulated by divalent cations, stable at 1% of surfactant Triton X-100 and at different concentrations of the reducing agent β-mercaptoethanol. Thus, C. ensiformis expresses a particular set of proteases in distinctive organs with high activity and stability, making this legume an important source of proteases with biotechnological potential.

Biotechnological Eminence of Chitinases: A Focus on Thermophilic Enzyme Sources, Production Strategies and Prominent Applications.

2021 ◽  
Vol 28 ◽  
Author(s):  
Fatima Akram ◽  
Rabia Akram ◽  
Ikram ul Haq ◽  
Ali Nawaz ◽  
Zuriat Jabbar ◽  
...  
Keyword(s):  
Specific Activity ◽  
High Specific Activity ◽  
Industrial Applications ◽  
Thermostable Enzyme ◽  
Raw Material ◽  
Thermostable Enzymes ◽  
Thermophilic Microorganisms ◽  
Industrial Processing ◽  
Glycosidic Bonds ◽  
Renewable Raw Material

Background: Chitin, the second most abundant polysaccharide in nature, is a constantly valuable and renewable raw material after cellulose. Due to advancement in technology, industrial interest has grown to take advantage of the chitin. Objective: Now, biomass is being treated with diverse microbial enzymes or cells for the production of desired products under best industrial conditions. Glycosidic bonds in chitin structure are degraded by chitinase enzymes, which are characterized into number of glycoside hydrolase (GHs) families. Methods: Thermophilic microorganisms are remarkable sources of industrially important thermostable enzymes, having ability to survive harsh industrial processing conditions. Thermostable chitinases have an edge over mesophilic chitinases as they can hydrolyse the substrate at relatively high temperatures and exhibit decreased viscosity, significantly reduced contamination risk, thermal and chemical stability and increased solubility. Various methods are employed to purify the enzyme and increase its yield by optimizing various parameters such as temperature, pH, agitation, and by investigating the effect of different chemicals and metal ions etc. Results: Thermostable chitinase enzymes show high specific activity at elevated temperature which distinguish them from mesophiles. Genetic engineering can be used for further improvement of natural chitinases, and unlimited potential for the production of thermophilic chitinases has been highlighted due to advancement in synthetic biological techniques. Thermostable chitinases are then used in different fields such as bioremediation, medicine, agriculture and pharmaceuticals. Conclusion: This review will provide information about chitinases, biotechnological potential of thermostable enzyme and the methods by which they are being produced and optimized for several industrial applications. Some of the applications of thermostable chitinases have also been briefly described.

Characterization of dissolved material during the initial phase of softwood kraft pulping

TAPPI Journal ◽  
2013 ◽  
Vol 12 (1) ◽  
pp. 37-43 ◽  
Author(s):  
HANNU PAKKANEN ◽  
TEEMU PALOHEIMO ◽  
RAIMO ALÉN
Keyword(s):  
Mass Transfer ◽  
Molecular Mass ◽  
Initial Phase ◽  
Degradation Products ◽  
Kraft Pulping ◽  
Reaction Products ◽  
Cooking Temperature ◽  
Molecular Masses ◽  
Aliphatic Carboxylic Acids

The influence of various cooking parameters, such as effective alkali, cooking temperature, and cooking time on the formation of high molecular mass lignin-derived and low molecular mass carbohydrates-derived (aliphatic carboxylic acids) degradation products, mainly during the initial phase of softwood kraft pulping was studied. In addition, the mass transfer of all of these degradation products was clarified based on their concentrations in the cooking liquor inside and outside of the chips. The results indicated that the degradation of the major hemicellulose component, galactoglucomannan, typically was dependent on temperature, and the maximum degradation amount was about 60%. In addition, about 60 min at 284°F (140°C) was needed for leveling off the concentrations of the characteristic reaction products (3,4-dideoxy-pentonic and glucoisosaccharinic acids) between these cooking liquors. Compared with low molecular mass aliphatic acids, the mass transfer of soluble lignin fragments with much higher molecular masses was clearly slower.

Diversity of Thermophilic Microorganisms on Fermented Leaves of Flue-cured Tobacco

2012 ◽  
Vol 18 (3) ◽  
pp. 471
Author(s):  
Fang WANG ◽  
Yonghong LAI ◽  
Jing MI ◽  
Guosong WEN ◽  
Hongmei BAI ◽  
...  
Keyword(s):  
Thermophilic Microorganisms

scholarly journals Synthetic lipopeptide Pam3CysSer(Lys)4 is an effective activator of human platelets

1994 ◽  
Vol 266 (6) ◽  
pp. C1684-C1691 ◽  
Author(s):  
M. Berg ◽  
S. Offermanns ◽  
R. Seifert ◽  
G. Schultz
Keyword(s):  
Calcium Concentration ◽  
Cytosolic Calcium ◽  
Human Platelets ◽  
Cellular Effects ◽  
Prostacyclin Receptor ◽  
Serotonin Secretion ◽  
Peptide Moiety ◽  
Lipid Moiety ◽  
Molecular Masses ◽  
Aggregation Of Platelets

Lipopeptide analogues of the NH2-terminus of bacterial lipoprotein are known to induce activation of macrophages, neutrophils, and lymphocytes. We studied the effect of the lipopeptide N-palmitoyl-S-[2,3-bis(palmitoyloxy)-(2RS)-propyl]-(R)-cysteinyl-( S)-seryl-(S)-lysyl-(S)-lysyl-(S)-lysyl-(S)-lysine [Pam3CysSer(Lys)4] on several functions of human platelets. Pam3CysSer(Lys)4 led to the aggregation of platelets and induced the secretion of serotonin with an effectiveness similar to thrombin. These cellular effects of Pam3CysSer(Lys)4 were concentration dependent, being half maximal at 2-3 microM and maximal at 10-30 microM. Another lipopeptide also induced platelet aggregation and serotonin secretion but was less potent and less effective than Pam3CysSer(Lys)4. The lipid moiety and the peptide moiety of Pam3CysSer(Lys)4 alone were without any effect. Lipopeptides also stimulated tyrosine phosphorylation of several proteins with molecular masses similar to those found to be tyrosine phosphorylated in response to thrombin, and Pam3CysSer(Lys)4 led to an increase in the cytosolic calcium concentration. All studied responses of platelets to lipopeptides were inhibited by the prostacyclin receptor agonist cicaprost. Taken together, our data show that lipopeptides are effective activators of human platelets and that this activation is susceptible to the action of physiological platelet inhibitors.

scholarly journals Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA

1997 ◽  
Vol 325 (3) ◽  
pp. 761-769 ◽  
Author(s):  
Isabelle GARCIA ◽  
Matthew RODGERS ◽  
Catherine LENNE ◽  
Anne ROLLAND ◽  
Alain SAILLAND ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Gel Filtration ◽  
Peptide Sequence ◽  
Amino Acid Residues ◽  
Carrot Cells ◽  
Expression Studies ◽  
Sds Page ◽  
Molecular Masses ◽  
The Difference ◽  
Dioxygenase Activity

p-Hydroxyphenylpyruvate dioxygenase catalyses the transformation of p-hydroxyphenylpyruvate into homogentisate. In plants this enzyme has a crucial role because homogentisate is the aromatic precursor of all prenylquinones. Furthermore this enzyme was recently identified as the molecular target for new families of potent herbicides. In this study we examine precisely the localization of p-hydroxyphenylpyruvate dioxygenase activity within carrot cells. Our results provide evidence that, in cultured carrot cells, p-hydroxyphenylpyruvate dioxygenase is associated with the cytosol. Purification and SDS/PAGE analysis of this enzyme revealed that its activity is associated with a polypeptide of 45–46 kDa. This protein specifically cross-reacts with an antiserum raised against the p-hydroxyphenylpyruvate dioxygenase of Pseudomonas fluorescens. Gel-filtration chromatography indicates that the enzyme behaves as a homodimer. We also report the isolation and nucleotide sequence of a cDNA encoding a carrot p-hydroxyphenylpyruvate dioxygenase. The nucleotide sequence (1684 bp) encodes a protein of 442 amino acid residues with a molecular mass of 48094 Da and shows specific C-terminal regions of similarity with other p-hydroxyphenylpyruvate dioxygenases. This cDNA encodes a functional p-hydroxyphenylpyruvate dioxygenase, as evidenced by expression studies with transformed Escherichia coli cells. Comparison of the N-terminal sequence of the 45–46 kDa polypeptide purified from carrot cells with the deduced peptide sequence of the cDNA confirms that this polypeptide supports p-hydroxyphenylpyruvate dioxygenase activity. Immunodetection studies of the native enzyme in carrot cellular extracts reveal that N-terminal proteolysis occurs during the process of purification. This proteolysis explains the difference in molecular masses between the purified protein and the deduced polypeptide.

scholarly journals Applicability of the Cox-Merz Rule to High-Density Polyethylene Materials with Various Molecular Masses

Polymers ◽  
2021 ◽  
Vol 13 (8) ◽  
pp. 1218
Author(s):  
Raffael Rathner ◽  
Wolfgang Roland ◽  
Hanny Albrecht ◽  
Franz Ruemer ◽  
Jürgen Miethlinger
Keyword(s):  
Molecular Weight ◽  
Pressure Drop ◽  
High Molecular Weight ◽  
High Density Polyethylene ◽  
Parallel Plate ◽  
Empirical Relationship ◽  
Polymer Processing ◽  
High Density ◽  
Viscosity Data ◽  
Molecular Masses

The Cox-Merz rule is an empirical relationship that is commonly used in science and industry to determine shear viscosity on the basis of an oscillatory rheometry test. However, it does not apply to all polymer melts. Rheological data are of major importance in the design and dimensioning of polymer-processing equipment. In this work, we investigated whether the Cox-Merz rule is suitable for determining the shear-rate-dependent viscosity of several commercially available high-density polyethylene (HDPE) pipe grades with various molecular masses. We compared the results of parallel-plate oscillatory shear rheometry using the Cox-Merz empirical relation with those of high-pressure capillary and extrusion rheometry. To assess the validity of these techniques, we used the shear viscosities obtained by these methods to numerically simulate the pressure drop of a pipe head and compared the results to experimental measurements. We found that, for the HDPE grades tested, the viscosity data based on capillary pressure flow of the high molecular weight HDPE describes the pressure drop inside the pipe head significantly better than do data based on parallel-plate rheometry applying the Cox-Merz rule. For the lower molecular weight HDPE, both measurement techniques are in good accordance. Hence, we conclude that, while the Cox-Merz relationship is applicable to lower-molecular HDPE grades, it does not apply to certain HDPE grades with high molecular weight.

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