scholarly journals Extraction cellulose from corn-stalk taking advantage of pretreatment technology with immobilized enzyme

RSC Advances ◽  
2022 ◽  
Vol 12 (2) ◽  
pp. 1208-1215
Author(s):  
Chunhua Lou ◽  
Yongli Zhou ◽  
An Yan ◽  
Yang Liu
Keyword(s):  
Immobilized Enzyme ◽  
Corn Stalk ◽  
Pretreatment Technology

In this paper, the corn-stalk cellulose (CSC) was extracted from the corn-stalk pretreated by the immobilized enzyme which was prepared using xylanase and laccase.

Experimental Study on Anaerobic Fermentation of Steam Explosion Pretreated Corn Stalk

2011 ◽  
Vol 183-185 ◽  
pp. 1975-1978 ◽  
Author(s):  
Xu Tao Wang ◽  
Hua Zhen Cai ◽  
Li Sha Liu
Keyword(s):  
Steam Explosion ◽  
Anaerobic Fermentation ◽  
Biogas Production ◽  
Steam Pressure ◽  
Gas Production ◽  
Total Production ◽  
Corn Stalk ◽  
Medium Temperature ◽  
Production Area ◽  
Pretreatment Technology

Using the steam exploded pretreatment technology to process the corn stalk, and then the pretreated corn stalk were used the materials of anaerobic fermentation under the temperature 35°C. Experimental results show that: the biogas production per unit of pretreated corn stalk increased 16.8 % ~ 63.2% than the unexploded corn stalk. The gas production can up to the peak (484.3ml / g dry steam exploded straw) under the condition (retained time 90s, pressure 3.0Mpa). The longer the retained time is the earlier the gas production peak occurs under the same steam pressure and the peak range become wider. The main gas production area is the former 20d, the production amount to about 80% of total production, while the gas production of untreated straw fermentation in is only 60% of total production under medium temperature.

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.

Immobilized Nanoparticles-Mediated Enzymatic Hydrolysis of Cellulose for Clean Sugar Production: A Novel Approach

2019 ◽  
Vol 15 (3) ◽  
pp. 296-303 ◽  
Author(s):  
Swapnil Gaikwad ◽  
Avinash P. Ingle ◽  
Silvio Silverio da Silva ◽  
Mahendra Rai
Keyword(s):  
Catalytic Activity ◽  
Enzymatic Hydrolysis ◽  
Immobilized Enzyme ◽  
Free Enzyme ◽  
Magnetic Nanomaterials ◽  
Sugar Production ◽  
Cellulase Enzyme ◽  
Enzymatic Hydrolysis Of Cellulose ◽  
Hydrolysis Of Cellulose ◽  
Hydrolysis Of

Background: Enzymatic hydrolysis of cellulose is an expensive approach due to the high cost of an enzyme involved in the process. The goal of the current study was to apply magnetic nanomaterials as a support for immobilization of enzyme, which helps in the repeated use of immobilized enzyme for hydrolysis to make the process cost-effective. In addition, it will also provide stability to enzyme and increase its catalytic activity. Objective: The main aim of the present study is to immobilize cellulase enzyme on Magnetic Nanoparticles (MNPs) in order to enable the enzyme to be re-used for clean sugar production from cellulose. Methods: MNPs were synthesized using chemical precipitation methods and characterized by different techniques. Further, cellulase enzyme was immobilized on MNPs and efficacy of free and immobilized cellulase for hydrolysis of cellulose was evaluated. Results: Enzymatic hydrolysis of cellulose by immobilized enzyme showed enhanced catalytic activity after 48 hours compared to free enzyme. In first cycle of hydrolysis, immobilized enzyme hydrolyzed the cellulose and produced 19.5 ± 0.15 gm/L of glucose after 48 hours. On the contrary, free enzyme produced only 13.7 ± 0.25 gm/L of glucose in 48 hours. Immobilized enzyme maintained its stability and produced 6.15 ± 0.15 and 3.03 ± 0.25 gm/L of glucose in second and third cycle, respectively after 48 hours. Conclusion: This study will be very useful for sugar production because of enzyme binding efficiency and admirable reusability of immobilized enzyme, which leads to the significant increase in production of sugar from cellulosic materials.

Mass transfer in heterogeneous system enzyme-substrate; Approximate analytical model for the case of liquid substrate-immobilized enzyme

1982 ◽  
Vol 47 (11) ◽  
pp. 3013-3018
Author(s):  
František Kaštánek ◽  
Jindřich Zahradník ◽  
Germanico Ocampo
Keyword(s):  
Mass Transfer ◽  
Heterogeneous System ◽  
Immobilized Enzyme ◽  
Enzymatic Reaction ◽  
Analytical Form ◽  
Approximate Model ◽  
Basic Type ◽  
Reaction Interface ◽  
Enzyme Substrate ◽  
Flow Intensity

Calculation procedure is suggested for flow intensity of substrate toward reaction interface of immobilized enzyme at simultaneous effect of enzymatic reaction and internal diffusion. The approximate model is presented in an analytical form for the basic type of Michaelis-Menten kinetics and for the case of inhibition in excess of substrate.

An Investigation on Devolatilization Characteristics of Pulverized Corn Stalk at Flash Heating Rates

2004 ◽  
Author(s):  
Weiming ◽  
YI. ◽  
Xueyuan ◽  
BAI. ◽  
Zhihe ◽  
...  
Keyword(s):  
Corn Stalk ◽  
Heating Rates

Effect of Rhodococcus sp. pretreatment on cellulose hydrolysis of corn stalk

2020 ◽  
pp. 1-7
Author(s):  
Pan Hu ◽  
Huanan Li ◽  
Wenjing Xiao ◽  
Xiaohang Xie ◽  
Yuxian Yang ◽  
...  
Keyword(s):  
Cellulose Hydrolysis ◽  
Corn Stalk ◽  
Hydrolysis Of ◽  
Rhodococcus Sp

scholarly journals Self-assembling thermostable chimeras as new platform for arsenic biosensing

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Rosanna Puopolo ◽  
Ilaria Sorrentino ◽  
Giovanni Gallo ◽  
Alessandra Piscitelli ◽  
Paola Giardina ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Association Constant ◽  
Immobilized Enzyme ◽  
Thermus Thermophilus ◽  
Chimeric Protein ◽  
The Self ◽  
Chimeric Proteins ◽  
Self Assembling ◽  
Langmuir Isotherm Model ◽  
Activity Loss

AbstractThe correct immobilization and orientation of enzymes on nanosurfaces is a crucial step either for the realization of biosensors, as well as to guarantee the efficacy of the developed biomaterials. In this work we produced two versions of a chimeric protein, namely ArsC-Vmh2 and Vmh2-ArsC, which combined the self-assembling properties of Vmh2, a hydrophobin from Pleurotus ostreatus, with that of TtArsC, a thermophilic arsenate reductase from Thermus thermophilus; both chimeras were heterologously expressed in Escherichia coli and purified from inclusion bodies. They were characterized for their enzymatic capability to reduce As(V) into As(III), as well as for their immobilization properties on polystyrene and gold in comparison to the native TtArsC. The chimeric proteins immobilized on polystyrene can be reused up to three times and stored for 15 days with 50% of activity loss. Immobilization on gold electrodes showed that both chimeras follow a classic Langmuir isotherm model towards As(III) recognition, with an association constant (KAsIII) between As(III) and the immobilized enzyme, equal to 650 (± 100) L mol−1 for ArsC-Vmh2 and to 1200 (± 300) L mol−1 for Vmh2-ArsC. The results demonstrate that gold-immobilized ArsC-Vmh2 and Vmh2-ArsC can be exploited as electrochemical biosensors to detect As(III).

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