scholarly journals Thermostable Cellulases from the Yeast Trichosporon sp.

2019 ◽  
Vol 2019 ◽  
pp. 1-6 ◽  
Author(s):  
Hanane Touijer ◽  
Najoua Benchemsi ◽  
Mohamed Ettayebi ◽  
Abdellatif Janati Idrissi ◽  
Bouchra Chaouni ◽  
...  
Keyword(s):  
Elevated Temperatures ◽  
Cellulose Fiber ◽  
Cellulosic Biomass ◽  
Measured Temperature ◽  
Cellulolytic Microorganisms ◽  
Lignocellulosic Substrates ◽  
Wide Ph Range ◽  
Ph Range ◽  
Hydrolysis Of ◽  
Optimal Ph

Objectives. Identification of cellulolytic microorganisms is of great interest to the hydrolysis of cellulosic biomass. This study focuses on the identification of cellulolytic yeasts and the optimization of cellulase activities produced by the best performing isolate. Results. 30 cellulolytic yeast isolates were selected. Enzymes produced by an isolate from the Trichosporon genus showed the property to hydrolyze different substrates: carboxymethyl cellulose (CMC), cellulose fiber, and filter paper (FP). The optimum measured temperature was 55°C for CMCase and 60°C for FPase. The optimal pH was 5 for CMCase and 4 to 6 for FPase. The effect of the substrates concentration showed that the best activities were obtained at 100 mg/mL CMC or FP. The highest activities were 0.52 for the CMCase and 0.56 for the cellulase fiber at 10 min incubation, 0.44 IU/mL at 15 min incubation, and 24 h FPase preincubation. Conclusion. Cellulases produced by the studied yeast are capable of hydrolyzing soluble and insoluble substrates at elevated temperatures and at a wide pH range. They are considerable interest in the production of fermentable sugars from lignocellulosic substrates.

scholarly journals Purification and properties of three (1→3)-β-d-glucanase isoenzymes from young leaves of barley (Hordeum vulgare)

1993 ◽  
Vol 289 (2) ◽  
pp. 453-461 ◽  
Author(s):  
M Hrmova ◽  
G B Fincher
Keyword(s):  
Hordeum Vulgare ◽  
Elevated Temperatures ◽  
Gel Filtration ◽  
Degree Of Polymerization ◽  
Exchange Chromatography ◽  
Purification And Properties ◽  
Young Leaves ◽  
Monomeric Proteins ◽  
Ph Range ◽  
Hydrolysis Of

Three (1->3)-beta-D-glucan glucanohydrolase (EC 3.2.1.39) isoenzymes GI, GII and GIII were purified from young leaves of barley (Hordeum vulgare) using (NH4)2SO4 fractional precipitation, ion-exchange chromatography, chromatofocusing and gel-filtration chromatography. The three (1->3)-beta-D-glucanases are monomeric proteins of apparent M(r)32,000 with pI values in the range 8.8-10.3. N-terminal amino-acid-sequence analyses confirmed that the three isoenzymes represent the products of separate genes. Isoenzymes GI and GII are less stable at elevated temperatures and are active over a narrower pH range than is isoenzyme GIII, which is a glycoprotein containing 20-30 mol of hexose equivalents/mol of enzyme. The preferred substrate for the enzymes is laminarin from the brown alga Laminaria digitata, an essentially linear (1->3)-beta-D-glucan with a low degree of glucosyl substitution at 0-6 and a degree of polymerization of approx. 25. The three enzymes are classified as endohydrolases, because they yield (1->3)-beta-D-oligoglucosides with degrees of polymerization of 3-8 in the initial stages of hydrolysis of laminarin. Kinetic analyses indicate apparent Km values in the range 172-208 microM, kcat. constants of 36-155 s-1 and pH optima of 4.8. Substrate specificity studies show that the three isoenzymes hydrolyse substituted (1->3)-beta-D-glucans with degrees of polymerization of 25-31 and various high-M(r), substituted and side-branched fungal (1->3;1->6)-beta-D-glucans. However, the isoenzymes differ in their rates of hydrolysis of a (1->3;1->6)-beta-D-glucan from baker's yeast and their specific activities against laminarin vary significantly. The enzymes do not hydrolyse (1->3;1->4)-beta-D-glucans, (1->6)-beta-D-glucan, CM-cellulose, insoluble (1->3)-beta-D-glucans or aryl beta-D-glycosides.

2´-carboxy-3-keto-D-arabinitol 1,5-bisphosphate, the six-carbon intermediate of the ribulose bisphosphate carboxylase reaction

1986 ◽  
Vol 313 (1162) ◽  
pp. 397-407 ◽  
Keyword(s):  
Metal Ion ◽  
Ribulose Bisphosphate Carboxylase ◽  
Ribulose Bisphosphate ◽  
Bisphosphate Carboxylase ◽  
Wide Ph Range ◽  
Alkaline Conditions ◽  
Divalent Metal Ion ◽  
Ph Range ◽  
Short Time ◽  
Hydrolysis Of

The six-carbon intermediate of the ribulose 1,5-bisphosphate (RuBP) carboxylase reaction, 2'-carboxy-3-keto-D-arabinitol 1,5-bisphosphate (CKABP), was prepared enzymatically by quenching the reaction with acid after a short time ( ca 12 ms). Over a wide pH range (4-11), GKABP undergoes a slow ( t 1/2 = 1 h), pH-independent decarboxylation. No detectable decomposition of CKABP occurs over a six-week period at — 80 °C. The decarboxylation of CKABP is acid-catalysed and is also catalysed by deactivated enzyme lacking the activator carbamate-divalent metal ion complex. Decarboxylation is accompanied by β-elimination of the C-1 phosphate from the 2,3-enediolate. Under alkaline conditions (pH >11) CKABP undergoes hydrolysis. Non-enzymatic hydrolysis of the intermediate is also accompanied by β-elimination of the C-1 phosphate (presumably from the aci-acid of the upper glycerate 3-phosphate) and the formation of pyruvate. Fully activated enzyme catalyses the complete hydrolysis of CKABP to glycerate 3-phosphate, although enzymic hydrolysis of CKABP is limited by an event not on the direct path of carboxylation. Carbon-13 NMR analysis of [2',3- 13 C]CKABP indicates that it exists in solution predominantly (> 85%) as the C-3 ketone. In contrast, borohydride trapping of CKABP formed from [3- 18 O]RuBP indicates that the intermediate exists on the enzyme predominantly (> 94%) as the hydrated C-3 gem-diol. In solution, the hydration of the C-3 ketone of CKABP proceeds slowly ( k = 2.5 x 10 -3 s -1 ). The enzymatic hydration of CKABP must proceed at least as fast as k cat ( ca. 5 s -1 ) or at least 2000 times faster than the hydration of CKABP in solution.

Mitigation of High Temperature Challenges in Limestone Acidizing through the use of Chelating Agents

2021 ◽  
Author(s):  
Mandeep Khan ◽  
Mohammed Qamruzzaman ◽  
Dhirendra Chandra Roy ◽  
Ravi Raman
Keyword(s):  
High Temperature ◽  
Chelating Agents ◽  
Elevated Temperatures ◽  
Chelating Agent ◽  
Point Of View ◽  
Core Flooding ◽  
Agent Based ◽  
Asphaltene Deposition ◽  
Wide Ph Range ◽  
Ph Range

Abstract Acid jobs with conventional acid systems like hydrochloric acid in high temperature conditions is challenging on various fronts. Enhanced reactivity of strong acids results in poor penetration and severe face dissolution. Also, it aggravates the issue of corrosion of downhole equipment and may also result in sludge formation/asphaltene deposition. Worldwide, chelating agents has emerged as a standalone stimulation fluid for high temperature acidizing. Their unique attributes and properties have been proved very useful for acid jobs at elevated temperatures. However, the chelating agents-based formulations need to be carefully evaluated on various acidization parameters for a fruitful stimulation. Mumbai Offshore field has been encountering the above-mentioned problems in acidizing of its high temperature (>275°F) limestone reservoirs. The paper presents innovative solutions devised for high temperature matrix acidizing. Two chelating agents viz., EDTA (Ethylenediaminetetraceticacid) and GLDA (L-Glutamic Acid N, N-diacetic acid) were explored and evaluated with meticulous laboratory studies. The performance of the chelating agent-based stimulation fluid was compared with acetic acid. Slurry tests were performed to quantify the dissolving power of each acid. Consequently, core flooding tests were carried out to to find the optimum pH of the chelating agents from stimulation point of view. Core flooding studies were performed at anticipated injection rates on representative core samples from a payzone A, with BHT 275-290° F, from Mumbai Offshore. pH optimized formulations were tested against N-80 metallurgy coupons at reservoir temperature for corrosion potential estimation. Also, sludge, asphaltene and emulsion formation tendencies were analyzed with representative oil samples. The results convey that both EDTA and GLDA were able to mitigate the challenges encountered at elevated temperatures. EDTA and GLDA were found to stimulate the cores with wormholes formed at wide pH range with no face dissolution observed. Chelating agents enjoyed good dissolving power with negligible corrosion rates, absence of sludge and asphaltene deposition, compatibility with formation fluid and excellent iron control properties.

scholarly journals Stability of gamma-valerolactone under pulping conditions as a basis for process optimization and chemical recovery

Cellulose ◽  
2021 ◽  
Author(s):  
Marianna Granatier ◽  
Inge Schlapp-Hackl ◽  
Huy Quang Lê ◽  
Kaarlo Nieminen ◽  
Leena Pitkänen ◽  
...  
Keyword(s):  
Elevated Temperatures ◽  
Treatment Time ◽  
Reaction Times ◽  
Chemical Recovery ◽  
Wide Ph Range ◽  
Alkaline Conditions ◽  
Naoh Solution ◽  
Hydroxyvaleric Acid ◽  
Ph Range ◽  
Spent Liquor

AbstractThis study focuses on the investigation of the extent of the γ-valerolactone (GVL) hydrolysis forming an equilibrium with 4-hydroxyvaleric acid (4-HVA) in aqueous solutions over a wide pH range. The hydrolysis of a 50 wt% GVL solution to 4-HVA (3.5 mol%) was observed only at elevated temperatures. The addition of sulfuric acid (0.2 × 10–5 wt% to 6 wt%) at elevated temperatures (150–180 °C) and reaction times between 30 and 180 min caused the formation of 4 mol% 4-HVA. However, with decreasing acidity, the 4-HVA remained constant at about 3 mol%. The hydrolysis reactions in alkaline conditions were conducted at a constant time (30 min) and temperature (180 °C) with the variation of the NaOH concentration (0.2 × 10–6 wt% to 7 wt%). The addition of less than 0.2 wt% of NaOH resulted in the formation of less than 4 mol% of sodium 4-hydroxyvalerate. A maximum amount of 21 mol% of 4-HVA was observed in a 7 wt% NaOH solution. The degree of decomposition after treatment was determined by NMR analysis. To verify the GVL stability under practical conditions, Betula pendula sawdust was fractionated in 50 wt% GVL with and without the addition of H2SO4 or NaOH at 180 °C and a treatment time of 120 min. The spent liquor was analyzed and a 4-HVA content of 5.6 mol% in a high acidic (20 kg H2SO4/t wood) and 6.0 mol% in an alkaline (192 kg NaOH/t wood) environment have been determined.

scholarly journals Stability of Gamma-valerolactone Under Pulping Conditions as a Basis for Process Optimization and Chemical Recovery

2021 ◽  
Author(s):  
Marianna Granatier ◽  
Inge Schlapp-Hackl ◽  
Huy Quang Lê ◽  
Kaarlo Nieminen ◽  
Herbert Sixta
Keyword(s):  
Elevated Temperatures ◽  
Reaction Times ◽  
Chemical Recovery ◽  
Wide Ph Range ◽  
Alkaline Conditions ◽  
Naoh Solution ◽  
Hydroxyvaleric Acid ◽  
The Stability ◽  
Ph Range ◽  
Spent Liquor

Abstract This study investigates the extent of the g-valerolactone (GVL) hydrolysis forming an equilibrium with 4-hydroxyvaleric acid (4-HVA) in aqueous solutions over a wide pH range. The hydrolysis of pure 50 wt% GVL to 4-HVA (3.5 mol%) was observed only at elevated temperatures. The addition of sulfuric acid (0.2×10-5 wt% to 6 wt%) at elevated temperatures (150 – 180°C) and reaction times between 30-180 min caused the formation of 4 mol% 4-HVA but with decreasing acidity, the 4-HVA remained constant at about 3 mol%. The hydrolysis reactions in alkaline conditions were conducted at constant time (30 min) and temperature (180 °C) with variation of the NaOH concentration (0.2×10-6 wt% to 7 wt%). The addition of less than 0.2 wt % of NaOH resulted in the formation of less than 4 mol% of sodium 4-hydroxyvalerate. A maximum amount of 21 mol% of 4-HVA was observed in a 7 wt% NaOH solution. The stability after synthesis was determined by NMR analysis. To verify the GVL stability results obtained under practical conditions, Betula pendula sawdust was fractionated in 50% GVL with and without addition of H2SO4 or NaOH at 180°C and 120 min, and spent liquor was analyzed. The spent liquor contained 5.6 mol% and 6.0 mol% of 4-HVA in a highly acidic (20 kg H2SO4/t wood) and alkaline (192 kg NaOH/ t wood) environment, respectively.

Polarographic and spectrophotometric behaviour of some N-p-phenyl substituted benzamidines

1991 ◽  
Vol 56 (12) ◽  
pp. 2791-2799 ◽  
Author(s):  
Juan A. Squella ◽  
Luis J. Nuñez-Vergara ◽  
Hernan Rodríguez ◽  
Amelia Márquez ◽  
Jose M. Rodríguez-Mellado ◽  
...  
Keyword(s):  
Spectrophotometric Study ◽  
Absorption Bands ◽  
Electrochemical Parameters ◽  
Wide Ph Range ◽  
Group A ◽  
Substituent Constants ◽  
Ph Range ◽  
The Waves

Five N-p-phenyl substituted benzamidines were studied by DC and DP polarography in a wide pH range. Coulometric results show that the overall processes are four-electron reductions. Logarithmic analysis of the waves indicate that the process are irreversible. The influence of the pH on the polarographic parameters was also studied. A UV spectrophotometric study was performed in the pH range 2-13. In basic media some variations in the absorption bands were observed due to the dissociation of the amidine group. A determination of the pK values was made by deconvolution of the spectra. Correlations of both the electrochemical parameters and spectrophotometric pK values with the Hammett substituent constants were obtained.

High degradation efficiency of sulfamethazine with the dual-reaction-center Fe-Mn-SiO2 Fenton-like nanocatalyst in a wide pH range

2021 ◽  
Author(s):  
Manoj Kumar Panjwani ◽  
Qing Wang ◽  
Yueming Ma ◽  
Yuxuan Lin ◽  
Feng Xiao ◽  
...  
Keyword(s):  
Wastewater Treatment ◽  
Reaction Center ◽  
Degradation Efficiency ◽  
Heterogeneous Fenton ◽  
Wide Ph Range ◽  
Ph Range

The development of a heterogeneous Fenton-like catalyst, possessing high degradation efficiency in a wide pH range, is crucial for wastewater treatment. The Fe-Mn-SiO2 catalyst was designed, and prepared by a...

scholarly journals The Hsp60 Protein of Helicobacter Pylori Exhibits Chaperone and ATPase Activities at Elevated Temperatures

BioChem ◽  
2021 ◽  
Vol 1 (1) ◽  
pp. 19-25
Author(s):  
Jose A. Mendoza ◽  
Julian L. Ignacio ◽  
Christopher M. Buckley
Keyword(s):  
Helicobacter Pylori ◽  
Heat Stress ◽  
Molecular Chaperone ◽  
Elevated Temperatures ◽  
Citrate Synthase ◽  
Gastric Epithelium ◽  
Acidic Conditions ◽  
H Pylori ◽  
Induced Aggregation ◽  
Hydrolysis Of

The heat-shock protein, Hsp60, is one of the most abundant proteins in Helicobacter pylori. Given its sequence homology to the Escherichia coli Hsp60 or GroEL, Hsp60 from H. pylori would be expected to function as a molecular chaperone in this organism. H. pylori is a type of bacteria that grows on the gastric epithelium, where the pH can fluctuate between neutral and 4.5, and the intracellular pH can be as low as 5.0. We previously showed that Hsp60 functions as a chaperone under acidic conditions. However, no reports have been made on the ability of Hsp60 to function as a molecular chaperone under other stressful conditions, such as heat stress or elevated temperatures. We report here that Hsp60 could suppress the heat-induced aggregation of the enzymes rhodanese, malate dehydrogenase, citrate synthase, and lactate dehydrogenase. Moreover, Hsp60 was found to have a potassium and magnesium-dependent ATPase activity that was stimulated at elevated temperatures. Although, Hsp60 was found to bind GTP, the hydrolysis of this nucleotide could not be observed. Our results show that Hsp60 from H. pylori can function as a molecular chaperone under conditions of heat stress.

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