scholarly journals Enzymatic depolymerization of wheat straw polysaccharides

2021 ◽  
Vol 939 (1) ◽  
pp. 012005
Author(s):  
Zh Makhatov ◽  
N Alibayev ◽  
Z Konarbayeva ◽  
B Makhatov ◽  
A Makhatova ◽  
...  
Keyword(s):  
Wheat Straw ◽  
Specific Activity ◽  
Maximum Yield ◽  
High Yield ◽  
Cellulolytic Enzymes ◽  
Cultivation Conditions ◽  
Glucose Yield ◽  
Complex Preparation ◽  
Hydrolysis Of ◽  
Enzymatic Depolymerization

Abstract The purpose of this study is to develop a technology for enzymatic processing for depolymerization of polysaccharides in wheat straw to obtain the maximum yield of glucose and sorbitol. Cellulolytic enzymes endo-1,4-β-glucanase (EC 3.2.1.4) and cellobiose (1,3-β-glucosidase) (CF 3.2.1.21) were isolated and studied in local strains Tr. viride 121, which are grown under deep cultivation conditions. A technology has been developed for obtaining a complex preparation “Cellozyme G20x” with a high yield and specific activity of cellulase, xylanase, β-glucanase and pectinase, and a scheme for purification from cellulases by precipitation, ultrafiltration, and freeze drying is not inferior in efficiency to commercial preparations. The physicochemical properties of the preparation “Cellozyme G20x” have been studied, the optimal parameters of the action and stability of the enzyme preparation have been established. The efficiency of Cellozyme G20x for hydrolysis of straw polysaccharides was 35-40% in terms of glucose yield.

scholarly journals Study of the effect of process parameters on the yield of fermentable sugar from red cocoyam (Xanthosoma sagittifolium) peels via acid and enzyme hydrolysis

2021 ◽  
Vol 1 (1) ◽  
pp. 061-069
Author(s):  
Onoh Ikechukwu Maxwell ◽  
Anho Lawrence Oghenerivwe ◽  
Egwuagu Onyekachi
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Groups ◽  
Process Parameters ◽  
Maximum Yield ◽  
Proximate Analysis ◽  
Enzyme Hydrolysis ◽  
Glucose Yield ◽  
Xanthosoma Sagittifolium ◽  
Hydrolysis Of ◽  
Fermentative Process

The aim of this work is to study the acid and enzymatic hydrolysis of cocoyam peels using HCl, H2S04 acids and cellulase enzyme. The cellulase was secreted from Aspergillus Niger (A. niger) fungi. The proximate analysis of the substrate showed that cocoyam peel is a lignocellulosic biomass with a cellulose composition of 48%. The effect of the process parameters (time, temperature, acid concentration and pH) on the yield of glucose in acid and enzymatic hydrolysis of the cocoyam peel was respectively investigated. Maximum glucose yield of 44.5% was obtained after 3 days of enzymatic hydrolysis at 30°C and pH 5. The HCl acid hydrolysis showed a maximum glucose yield of 27.3% at 70°C, 5% HCl after 180 minutes. The glucose yield in H2S04 hydrolysis was relatively lower than that of the HCl with a maximum yield of 26.5% at 70°C, 5% H2SO4 after 180 minutes. In addition to, the functional groups present in the glucose synthesized from cocoyam ground peels and the standard glucose were evaluated using Fourier Transformed Infrared (FTIR). The FTIR results showed similarities in the functional groups present in both sugars. Cocoyam peel can be used for the production of glucose and further fermentative process to produce ethanol.

scholarly journals Development of Improved Cellulase Variants for the Conversion of Spent Mushroom Substrate Supplemented with Wheat Straw by Directed Evolution

2021 ◽  
Author(s):  
Valentina Mauriello ◽  
Anna Pennacchio ◽  
Irantzu Alegria Dallo ◽  
Laura Garcia Saez ◽  
Petri Ihalainen ◽  
...  
Keyword(s):  
Directed Evolution ◽  
Wheat Straw ◽  
Recombinant Expression ◽  
Scale Up ◽  
Wild Type ◽  
Spent Mushroom Substrate ◽  
Glucose Yield ◽  
Hydrolysis Of ◽  
Selection Of

Abstract To improve the Spent mushroom substrate (SMS) saccharification, cloning, recombinant expression in Escherichia coli and characterization of two new GH5 family cellulases (Cel1 and Cel2) were performed. Based on enzymes properties, Cel2 was selected for the generation of 30,000 random mutants by directed evolution in order to develop improved biocatalysts. Error-prone Polymerase Chain Reaction was used for diversity generation in cel2 gene and the screening for activity of mutants allowed selection of 63 improved variants that were subjected to a scale up production. Among these, 13 clones exhibited two-fold higher activity than Cel2 and a higher thermoresistance after 72h. The performances of these mutants in the hydrolysis of pretreated SMS/ wheat straw (40/60) were compared to the wild type Cel2 in conjunction with a commercial enzymatic mixture (MetZyme® SUNO™ BOOSTER 144). All the mutants exhibited a glucose yield two-fold or four fold higher than wild-type Cel2 after 72h of incubation.

scholarly journals Hydrolysis of wheat straw hemicelluloses for maximum xylose extraction

2021 ◽  
Vol 939 (1) ◽  
pp. 012006
Author(s):  
Zh Makhatov ◽  
Zh Yelemanova ◽  
R Aitkulova ◽  
Z Narymbayeva ◽  
A Dairabayeva ◽  
...  
Keyword(s):  
Wheat Straw ◽  
Atmospheric Pressure ◽  
Reaction Conditions ◽  
Glucose Yield ◽  
Process Duration ◽  
Mild Conditions ◽  
Dilute Sulfuric Acid ◽  
Hydrolysis Process ◽  
Initial Content ◽  
Hydrolysis Of

Abstract The aim of the study is to select reaction conditions for hydrolysis of wheat straw with dilute sulfuric acid for maximum xylose extraction under mild conditions (at atmospheric pressure and temperature of 100°C). The authors found that maximum glucose yield (72.4-77.1 weight % of the initial content of hemicelluloses in wheat straw) is achieved at a concentration of H2SO4 2-3 weight % and the hydrolysis process duration of 5 hours. Analysis of the obtained hydrolysates showed that they contain cellulose (56.8-70.4 weight %), lignin (19.8-28.8 weight %) and hemicelluloses (2.8-15.3 weight %).

scholarly journals A monoclonal antibody to bovine brain inositol monophosphatase. Immunoaffinity purification of the brain and kidney enzymes and evidence for their structural identity

1989 ◽  
Vol 264 (3) ◽  
pp. 793-798 ◽  
Author(s):  
N S Gee ◽  
S Howell ◽  
G Ryan ◽  
C I Ragan
Keyword(s):  
Monoclonal Antibody ◽  
Specific Activity ◽  
Binding Capacity ◽  
Bovine Brain ◽  
High Yield ◽  
Brain Extract ◽  
Kidney Cortex ◽  
Inositol Monophosphatase ◽  
Hydrolysis Of ◽  
The Brain

A monoclonal IgG2b(K) antibody, G-2A4, has been generated against bovine brain myo-inositol monophosphatase (EC 3.1.3.25). The identity of the antigen recognized by the antibody was established by using e.l.i.s.a. and Western blotting procedures, and by immunoprecipitation of enzyme activity from crude brain supernatant. In addition, the hydrolysis of Ins1P by crude brain extract was inhibited by up to 83% by the pure antibody. Under identical conditions, the hydrolysis of Ins(1,4)P2 was unaffected. An immunoadsorbent column containing monoclonal antibody G-2A4 covalently attached to CNBr-activated Sepharose 4B has been used for rapid purification of the brain enzyme. Elution conditions have been optimized to allow isolation of the enzyme in high yield (54%) with full retention of column-binding capacity. The enzyme was electrophoretically homogeneous, Mr 30,000 and of higher specific activity than that purified conventionally. Chromatography of the pure enzyme on high resolution ion-exchange columns revealed some charge heterogeneity, possibly indicative of some type of post-translational modification. The immunoadsorbent column has also been used to purify the bovine kidney cortex enzyme to homogeneity. Partial proteolytic fragmentation patterns of the brain and kidney enzymes using endoprotease glu-C were identical, suggesting that they are almost certainly products of the same gene.

scholarly journals Cloning and Overexpression of Pyrococcus Furiosus Endoglucanase A Gene (egIA) in Escherichia Coli

2021 ◽  
Vol 1 (1) ◽  
pp. 23-26
Author(s):  
Najam-us-Sahar Sadaf Zaidi ◽  
M. Waheed Akhtar
Keyword(s):  
Inclusion Bodies ◽  
Plant Biomass ◽  
Specific Activity ◽  
Pyrococcus Furiosus ◽  
Fold Increase ◽  
Cellulolytic Enzymes ◽  
High Level Expression ◽  
Hydrolysis Of Cellulose ◽  
High Level ◽  
Hydrolysis Of

This study describes the cloning and high-level expression of an Endoglucanase A Gene (egIA) from a hyperthermophilic archeon Pyrococcus Furiosus. An expression plasmid pET-EgIA was constructed for the production of recombinant EgIA in E.Coli B12 (DE3) under the control of T7lac promoter. Following induction, ~35kDa protein expressed at levels greater than 20% of the total E.Coli cellular proteins. The expressed protein, however, was in the form of inclusion bodies with little enzymatic activity, which was solubilized using higher concentration of denaturing agent (8M urea) followed by its refolding to an active state. A 7-8 fold increase in enzyme activity corresponding to 285U/mg specific activity could be achieved after refolding. The refolded egIA, partially purified by heat treatment upto ~92%, is being investigated for applications like hydrolysis of cellulose, a major component of plant biomass. Local, upscale and cheap production of these cellulolytic enzymes can help in reducing the costs of many processes in various industries like poultry and textile. 

scholarly journals Ethanol Production from Hydrolyzed Kraft Pulp by Mono- and Co-Cultures of Yeasts: The Challenge of C6 and C5 Sugars Consumption

Energies ◽  
2020 ◽  
Vol 13 (3) ◽  
pp. 744 ◽  
Author(s):  
Rita H. R. Branco ◽  
Mariana S. T. Amândio ◽  
Luísa S. Serafim ◽  
Ana M. R. B. Xavier
Keyword(s):  
Ethanol Production ◽  
Kraft Pulp ◽  
Ethanol Yield ◽  
High Yield ◽  
Glucose Yield ◽  
Erlenmeyer Flask ◽  
Second Generation Bioethanol ◽  
Separate Hydrolysis And Fermentation ◽  
Chemical Pulping ◽  
Hydrolysis Of

Second-generation bioethanol production’s main bottleneck is the need for a costly and technically difficult pretreatment due to the recalcitrance of lignocellulosic biomass (LCB). Chemical pulping can be considered as a LCB pretreatment since it removes lignin and targets hemicelluloses to some extent. Chemical pulps could be used to produce ethanol. The present study aimed to investigate the batch ethanol production from unbleached Kraft pulp of Eucalyptus globulus by separate hydrolysis and fermentation (SHF). Enzymatic hydrolysis of the pulp resulted in a glucose yield of 96.1 ± 3.6% and a xylose yield of 94.0 ± 7.1%. In an Erlenmeyer flask, fermentation of the hydrolysate using Saccharomyces cerevisiae showed better results than Scheffersomyces stipitis. At both the Erlenmeyer flask and bioreactor scale, co-cultures of S. cerevisiae and S. stipitis did not show significant improvements in the fermentation performance. The best result was provided by S. cerevisiae alone in a bioreactor, which fermented the Kraft pulp hydrolysate with an ethanol yield of 0.433 g·g−1 and a volumetric ethanol productivity of 0.733 g·L−1·h−1, and a maximum ethanol concentration of 19.24 g·L−1 was attained. Bioethanol production using the SHF of unbleached Kraft pulp of E. globulus provides a high yield and productivity.

scholarly journals Ultrafast synthesis of isoquercitrin by enzymatic hydrolysis of rutin in a continuous-flow microreactor

2015 ◽  
Vol 80 (7) ◽  
pp. 853-866 ◽  
Author(s):  
Jun Wang ◽  
Gong An ◽  
Shuangshuang Gu ◽  
Hongsheng Cui ◽  
Xiangyang Wu
Keyword(s):  
Enzymatic Hydrolysis ◽  
Continuous Flow ◽  
Biological Activities ◽  
Batch Reactor ◽  
Maximum Yield ◽  
Enzymatic Reaction ◽  
High Yield ◽  
Flow Microreactor ◽  
Wide Range ◽  
Hydrolysis Of

Isoquercitrin is a rare flavonol glycoside with a wide range of biological activities and is a key synthetic intermediate for the production of enzymatically modified isoquercitrin. In order to establish an ultrafast bioprocess for obtaining isoquercitrin, a novel continuous flow biosynthesis of isoquercitrin using the hesperidinase-catalyzed hydrolysis of rutin in a glass-polydimethylsiloxane (PDMS) microreactor was first carried out. Using the developed microchannel reactor (200?m width, 50?m depth, and 2 m length) with one T-shaped inlet and one outlet, the maximum yield of isoquercitrin (98.6%) was achieved in a short time (40 min) under the following optimum conditions: rutin concentration at 1 g L-1, hesperidinase concentration at 0.1 g mL-1, reaction temperature at 40?C, and a flow rate at 2 ?L min-1. The activation energy value Ea of the enzymatic reaction was 4.61 kJ mol-1, and the reaction rate and volumetric productivity were approximately 16.1-fold and 30% higher, respectively, than those in the batch reactor. Thus, the use of a continuous-flow microreactor for the enzymatic hydrolysis of rutin is an efficient and simple approach to achieve a relative high yield of isoquercitrin.

scholarly journals Study of the Effect of Process Parameters on the Yield of Fermentable Sugar from Tuber Peels Via Acid and Enzyme Hydrolysis

2021 ◽  
pp. 24-32
Author(s):  
Onoh Ikechukwu Maxwell ◽  
Anho Lawrence Oghenerivwe ◽  
Egwuagu Onyekachi
Keyword(s):  
Enzymatic Hydrolysis ◽  
Functional Groups ◽  
Process Parameters ◽  
Maximum Yield ◽  
Proximate Analysis ◽  
Enzyme Hydrolysis ◽  
Glucose Yield ◽  
Hydrolysis Of ◽  
Fermentative Process ◽  
Water Yam

The aim of this work is to study the acid and enzymatic hydrolysis of water yam peels using HCl, H2S04 acids and cellulase enzyme. The cellulase was secreted from Aspergillus niger (A.niger). The proximate analysis of the substrate showed that water yam peel is a lignocellulosic biomass with a cellulose composition of 48%. The effect of the process parameters (time, temperature, acid concentration and pH) on the yield of glucose in acid and enzymatic hydrolysis of the water yam peel was respectively investigated. Maximum glucose yield of 44.5% was obtained after 3 days of enzymatic hydrolysis at 30°C and pH 5. The HCl acid hydrolysis showed a maximum glucose yield of 27.3% at 70°C, 5% HCl after 180 minutes. The glucose yield in H2S04 hydrolysis was relatively lower than that of the HCl with a maximum yield of 26.5% at 70°C, 5% H2SO4 after 180 minutes. In addition to, the functional groups present in the glucose synthesized from ground water yam peels and the standard glucose were evaluated using Fourier Transformed Infrared (FTIR) Spectroscopy. The FTIR results showed similarities in the functional groups present in both sugars. Yam peel can be used for the production of glucose and further fermentative process to produce ethanol.

scholarly journals STUDY OF METHOD OF PROCESSING CELLULOSIC AND LIGNIN-CONTAINING RAW MATERIALS USING CELLULOLYTIC ENZYMES

2017 ◽  
Vol 61 (1) ◽  
pp. 78
Author(s):  
Natalia V. Lakina ◽  
Valentin Yu. Doluda ◽  
Esfir M. Sulman ◽  
Irina P. Shkileva ◽  
Olga S. Burmatova
Keyword(s):  
High Performance ◽  
Animal Feed ◽  
Raw Materials ◽  
Maximum Yield ◽  
Bacterial Biomass ◽  
Raw Material ◽  
Cellulolytic Enzymes ◽  
Material Efficiency ◽  
Reducing Substances ◽  
Hydrolysis Of

In the research the results of bioethanol and other valuable products formation are described during peat hydrolytic formation. The factors of cellulose-lignin raw materials (peat and wood sawdust) stability to the action of various hydrolyzing agents were determined. The obtained experimental data indicate the efficiency of peat and sawdust samples pre-treatment with H2SO4 (90 wt.%), which is expressed in the highest yield of reducing substances during hydrolysis of the samples, in comparison with the results obtained with H2SO4 pretreatment of a lower concentration. The article shows the results of cellulose-containing raw materials hydrolysis process study with various ways, including enzymatic treatment. Enzyme complex sample of Celloviridine, containing both exo-and endo-enzymes, was used. Qualitative and quantitative analysis of the cellulose-lignin-containing raw materials hydrolysis products was carried out using high-performance liquid chromatography. It was found that the maximum rate of glucose accumulation (the final product of the hydrolytic process of cellulose-lignin raw materials) was observed when using samples of peat and sawdust pretreated with H2SO4 (90wt.%). As a result of cellulosulignin raw material subsequent enzymatic hydrolysis, the amount of D-glucose in the hydrolyzate increased with the help of the Celloviridin preparation in comparison with its amount in the H2SO4 pretreatment. A comparative characterization of the raw material efficiency for the yield of the desired product - D-glucose is shown. In the process of combined hydrolysis of cellulose and lignin-containing raw materials the maximum yield of the monosaccharide was observed during the hydrolysis of peat samples. After appropriate neutralization the resulting hydrolysis solution can be used to produce bioethanol and bacterial biomass in the microbial synthesis of products used for animal feed, as well as for pharmaceutical practice.Forcitation:Lakina N.V., Doluda V.Yu., Sulman E.M., Shkileva I.P., Burmatova O.S. Study of method of processing cellulosic and lignin-containing raw materials using cellulolytic enzymes. Izv. Vyssh. Uchebn. Zaved. Khim. Khim. Tekhnol. 2018. V. 61. N 1. P. 78-83

On the Preparation of Bovine α-Thrombin

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad
Keyword(s):  
Immobilized Enzyme ◽  
Catalytic Properties ◽  
Specific Activity ◽  
Guanidine Hydrochloride ◽  
Low Molecular Weight ◽  
Reversible Process ◽  
Gel Beads ◽  
Tissue Thromboplastin ◽  
C 50 ◽  
Hydrolysis Of

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.

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