Compartmentalization of Pectinase within Cellulose Hydrogel: An Efficient Technique to Enhance the Catalytic Properties of Pectinase for Industrial Applications

2021 ◽  
Vol 8 (2) ◽  
Author(s):  
Rehman HU ◽  
◽  
Majeed A ◽  
Keyword(s):  
Plant Biomass ◽  
Catalytic Properties ◽  
Relative Activity ◽  
Industrial Applications ◽  
Original Activity ◽  
Hydrogel Beads ◽  
Cellulose Hydrogel ◽  
Km Value ◽  
Pectinase Activity ◽  
The Stability

Pectinase catalyze the breakdown of pectin polymer and widely has been used in different industrial preparations such as fruit juice preparation, liquification and scarification of plant biomass as well as coffee and tea fermentation. In this study, the pectinase from Bacillus licheniformis was compartmentalized within cellulose beads hydrogel using encapsulation technique to make it reusable with easy recovery from reaction mixture. The compartmentalization improved catalytic properties of pectinase and ensured its reusability for continuous uses. It was observed that 5.0% cellulose concentration was enough to form stable cellulose hydrogel beads with retention of high relative of activity of pectinase. The hydrogel compartmentalization didn’t change the optima pH and temperature for maximum relative activity and both the hydrogel compartmentalized pectinase and free pectinase maximum relative at same pH and temperature but the hydrogel compartmentalization increased the stability of pectinase against various temperatures and pH, and hydrogel compartmentalized pectinase showed higher relative activities against various temperature and pH as compared to free pectinase. The hydrogel compartmentalization slightly reduced the affinity of pectinase toward the substrate (pectin) and hydrogel compartmentalized pectinase showed little bit higher Km value as compared to soluble pectinase. Cellulose hydrogel compartmentalization retained the pectinase activity for reutilization in different reaction preparation and hydrogel compartmentalized pectinase showed more than 80% of its original activity after three times reusing.

scholarly journals Laccase Immobilized Fe3O4-Graphene Oxide Nanobiocatalyst Improves Stability and Immobilization Efficiency in the Green Preparation of Sulfa Drugs

Catalysts ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 459 ◽  
Author(s):  
Shamila Rouhani ◽  
Shohreh Azizi ◽  
Rose W. Kibechu ◽  
Bhekie B Mamba ◽  
Titus A. M. Msagati
Keyword(s):  
Storage Conditions ◽  
Relative Activity ◽  
The Novel ◽  
Original Activity ◽  
Immobilized Laccase ◽  
Time Period ◽  
Repeated Use ◽  
Graphene Nanocomposite ◽  
The Stability ◽  
And Storage

This paper, reports on the novel and green synthesis procedure for sulfonamides that involved the immobilization of Trametes Versicolor laccase onto the Fe3O4–graphene nanocomposite via glutaraldehyde (GA) crosslinking (Lac/Fe3O4/GO). Various parameters, mainly, activation time, GA, and laccase concentration were investigated and optimized. The results showed that the optimal contact time was 4 h, GA concentration was 5% while laccase concentration was 5 mg·mL−1, at which a high enzyme activity recovery was achieved (86%). In terms of the stability of immobilized laccase to temperature and storage conditions, the performance of the nanobiocatalyst was found to significantly exceed that of free laccase. The results have indicated that nearly 70% of relative activity for immobilized laccase remained after the incubation period of 2 h at 55 °C, but only 48% of free laccase remained within the same time period. Moreover, the immobilized laccase retained 88% of its initial activity after storage for 20 days. In case of the free laccase, the activity retained within the same time period was 32%. In addition, the nanobiocatalyst possessed better recycling performance as evidenced from the observation that after eight cycles of repeated use, it retained 85% of its original activity.

scholarly journals Dissecting cellobiose metabolic pathway and its application in biorefinery through consolidated bioprocessing in Myceliophthora thermophila

2019 ◽  
Vol 6 (1) ◽  
Author(s):  
Jingen Li ◽  
Shuying Gu ◽  
Zhen Zhao ◽  
Bingchen Chen ◽  
Qian Liu ◽  
...  
Keyword(s):  
Malic Acid ◽  
Plant Biomass ◽  
Consolidated Bioprocessing ◽  
Cellulase Activity ◽  
Industrial Applications ◽  
Efficient Production ◽  
Myceliophthora Thermophila ◽  
Final Strain ◽  
Cellobiose Metabolism ◽  
Cost Efficient

Abstract Background Lignocellulosic biomass has long been recognized as a potential sustainable source for industrial applications. The costs associated with conversion of plant biomass to fermentable sugar represent a significant barrier to the production of cost-competitive biochemicals. Consolidated bioprocessing (CBP) is considered a potential breakthrough for achieving cost-efficient production of biomass-based fuels and commodity chemicals. During the degradation of cellulose, cellobiose (major end-product of cellulase activity) is catabolized by hydrolytic and phosphorolytic pathways in cellulolytic organisms. However, the details of the two intracellular cellobiose metabolism pathways in cellulolytic fungi remain to be uncovered. Results Using the engineered malic acid production fungal strain JG207, we demonstrated that the hydrolytic pathway by β-glucosidase and the phosphorolytic pathway by phosphorylase are both used for intracellular cellobiose metabolism in Myceliophthora thermophila, and the yield of malic acid can benefit from the energy advantages of phosphorolytic cleavage. There were obvious differences in regulation of the two cellobiose catabolic pathways depending on whether M. thermophila JG207 was grown on cellobiose or Avicel. Disruption of Mtcpp in strain JG207 led to decreased production of malic acid under cellobiose conditions, while expression levels of all three intracellular β-glucosidase genes were significantly up-regulated to rescue the impairment of the phosphorolytic pathway under Avicel conditions. When the flux of the hydrolytic pathway was reduced, we found that β-glucosidase encoded by bgl1 was the dominant enzyme in the hydrolytic pathway and deletion of bgl1 resulted in significant enhancement of protein secretion but reduction of malate production. Combining comprehensive manipulation of both cellobiose utilization pathways and enhancement of cellobiose uptake by overexpression of a cellobiose transporter, the final strain JG412Δbgl2Δbgl3 produced up to 101.2 g/L and 77.4 g/L malic acid from cellobiose and Avicel, respectively, which corresponded to respective yields of 1.35 g/g and 1.03 g/g, representing significant improvement over the starting strain JG207. Conclusions This is the first report of detailed investigation of intracellular cellobiose catabolism in cellulolytic fungus M. thermophila. These results provide insights that can be applied to industrial fungi for production of biofuels and biochemicals from cellobiose and cellulose.

scholarly journals Suboptimal Disturbance Observer Design Using All Stabilizing Q Filter for Precise Tracking Control

Mathematics ◽  
2020 ◽  
Vol 8 (9) ◽  
pp. 1434 ◽  
Author(s):  
Wonhee Kim ◽  
Sangmin Suh
Keyword(s):  
Design Method ◽  
Industrial Applications ◽  
Point Of View ◽  
Observer Design ◽  
Linear Matrix ◽  
External Disturbances ◽  
Closed Loop Systems ◽  
Control Target ◽  
The Stability ◽  
Unified Index

For several decades, disturbance observers (DOs) have been widely utilized to enhance tracking performance by reducing external disturbances in different industrial applications. However, although a DO is a verified control structure, a conventional DO does not guarantee stability. This paper proposes a stability-guaranteed design method, while maintaining the DO structure. The proposed design method uses a linear matrix inequality (LMI)-based H∞ control because the LMI-based control guarantees the stability of closed loop systems. However, applying the DO design to the LMI framework is not trivial because there are two control targets, whereas the standard LMI stabilizes a single control target. In this study, the problem is first resolved by building a single fictitious model because the two models are serial and can be considered as a single model from the Q-filter point of view. Using the proposed design framework, all-stabilizing Q filters are calculated. In addition, for the stability and robustness of the DO, two metrics are proposed to quantify the stability and robustness and combined into a single unified index to satisfy both metrics. Based on an application example, it is verified that the proposed method is effective, with a performance improvement of 10.8%.

scholarly journals Biochemical and Structural Characterization of Cross-Linked Enzyme Aggregates (CLEAs) of Organic Solvent Tolerant Protease

Catalysts ◽  
2020 ◽  
Vol 10 (1) ◽  
pp. 55 ◽  
Author(s):  
Muhammad Syafiq Mohd Razib ◽  
Raja Noor Zaliha Raja Abd Rahman ◽  
Fairolniza Mohd Shariff ◽  
Mohd Shukuri Mohamad Ali
Keyword(s):  
Structural Analysis ◽  
Organic Solvent ◽  
Average Diameter ◽  
Relative Activity ◽  
Biochemical Properties ◽  
Biochemical Interaction ◽  
Organic Solvent Tolerant ◽  
Random Aggregate ◽  
Solvent Tolerant ◽  
The Stability

Cross-linked enzyme aggregates (CLEAs) is an immobilization technique that can be used to customize enzymes under an optimized condition. Structural analysis on any enzyme treated with a CLEA remains elusive and has been less explored. In the present work, a method for preparing an organic solvent tolerant protease using a CLEA is disclosed and optimized for better biochemical properties, followed by an analysis of the structure of this CLEA-treated protease. The said organic solvent tolerant protease is a metalloprotease known as elastase strain K in which activity of the metalloprotease is measured by a biochemical interaction with azocasein. Results showed that when a glutaraldehyde of 0.02% (v/v) was used under a 2 h treatment, the amount of recovered activity in CLEA-elastase was highest. The recovered activity of CLEA-elastase and CLEA-elastase-SB (which was a CLEA co-aggregated with starch and bovine serum albumin (BSA)) were at an approximate 60% and 80%, respectively. The CLEA immobilization of elastase strain K allowed the stability of the enzyme to be enhanced at high temperature and at a broader pH. Both CLEA-elastase and CLEA-elastase-SB end-products were able to maintain up to 67% enzyme activity at 60 °C and exhibiting an enhanced stability within pH 5–9 with up to 90% recovering activity. By implementing a CLEA on the organic solvent tolerant protease, the characteristics of the organic solvent tolerant were preserved and enhanced with the presence of 25% (v/v) acetonitrile, ethanol, and benzene at 165%, 173%, and 153% relative activity. Structural analysis through SEM and dynamic light scattering (DLS) showed that CLEA-elastase had a random aggregate morphology with an average diameter of 1497 nm.

A DENSITY FUNCTIONAL STUDY OF THE STRUCTURE OF SILANE COUPLING AGENT 3–AMINOPROPYLTRIETHOXYSILANE

2005 ◽  
Vol 04 (01) ◽  
pp. 117-126
Author(s):  
N. L. MA ◽  
P. WU
Keyword(s):  
Coupling Agent ◽  
Density Functional ◽  
Solution Structure ◽  
Silane Coupling Agent ◽  
Industrial Applications ◽  
Functional Study ◽  
Stable Form ◽  
Functional Theory ◽  
Silane Coupling ◽  
The Stability

Using density functional theory, we predicted the solution structure of the hydrolyzed 3–aminopropyltriethoxysilane (h–APS), which is a silane coupling agent commonly used in many industrial applications. We have located five stable minima on the potential energy surface of h–APS in which four of them are "neutral", and the remaining one is zwitterionic (dipolar) in nature. Our calculations suggested that the stability of the most stable form of h–APS in water (denoted as II_N) arose from strong intramolecular OH ⋯ N hydrogen bond. The least stable form is the zwitterionic form (I_ZW), which is estimated to be over 90 kJ mol -1 less stable than II_N. The factors governing the relative stabilities of different forms are discussed.

Effect of the ionizing radiation on the catalytic activity of the BASF K-3-10 catalyst in the low-temperature conversion of carbon monoxide by water vapour. Stability of the radiation catalytic effects

1986 ◽  
Vol 51 (8) ◽  
pp. 1571-1578 ◽  
Author(s):  
Alois Motl
Keyword(s):  
Carbon Monoxide ◽  
Catalytic Activity ◽  
Low Temperature ◽  
Catalytic Effect ◽  
Catalytic Properties ◽  
Beta Radiation ◽  
Fast Neutrons ◽  
Time Interval ◽  
The Stability ◽  
Catalytic Effects

The radiation catalytic properties of the BASF K-3-10 catalyst were studied, namely the dependence of these effects on the time interval between the catalyst irradiation and the reaction itself and also on the length of the catalyst use. The catalytic effects decrease exponentially with the interval between the irradiation and the reaction if the catalyst is kept in the presence of air. The stability of effects induced by various types of radiations increases in the sequence beta radiation - gamma radiation - fast neutrons. The radiation catalytic effect stability in the reaction increases in the same sequence.

scholarly journals Natural microbial polysaccharides as effective factors for modification of the catalytic properties of fungal cellobiose dehydrogenase

2021 ◽  
Author(s):  
Justyna Sulej ◽  
Magdalena Jaszek ◽  
Monika Osińska-Jaroszuk ◽  
Anna Matuszewska ◽  
Renata Bancerz ◽  
...  
Keyword(s):  
Catalytic Properties ◽  
Cellobiose Dehydrogenase ◽  
Pycnoporus Sanguineus ◽  
Practical Applications ◽  
Control Value ◽  
Electrochemical Parameters ◽  
Optimum Ph ◽  
Stabilization Effect ◽  
Fungal Polysaccharides ◽  
The Stability

AbstractPolysaccharides are biopolymers composed of simple sugars like glucose, galactose, mannose, fructose, etc. The major natural sources for the production of polysaccharides include plants and microorganisms. In the present work, four bacterial and two fungal polysaccharides (PS or EPS) were used for the modification and preservation of Pycnoporus sanguineus cellobiose dehydrogenase (CDH) activity. It was found that the presence of polysaccharide preparations clearly enhanced the stability of cellobiose dehydrogenase compared to the control value (4 °C). The highest stabilization effect was observed for CDH modified with Rh110EPS. Changes in the optimum pH in the samples of CDH incubated with the chosen polysaccharide modifiers were evidenced as well. The most significant effect was observed for Rh24EPS and Cu139PS (pH 3.5). Cyclic voltammetry used for the analysis of electrochemical parameters of modified CDH showed the highest peak values after 30 days of incubation with polysaccharides at 4 °C. In summary, natural polysaccharides seem to be an effective biotechnological tool for the modification of CDH activity to increase the possibilities of its practical applications in many fields of industry.

Chaos control of permanent magnet synchronous motor using simple controllers

2018 ◽  
Vol 41 (8) ◽  
pp. 2352-2364 ◽  
Author(s):  
Arif Iqbal ◽  
Girish Kumar Singh
Keyword(s):  
Permanent Magnet ◽  
Chaos Control ◽  
Permanent Magnet Synchronous Motor ◽  
Synchronous Motor ◽  
Industrial Applications ◽  
Stable Operation ◽  
Comparative Performance ◽  
Experimental Implementation ◽  
Chaotic Characteristic ◽  
The Stability

Owing to the superior properties and stable operation, the Permanent Magnet Synchronous Motor (PMSM) is preferably used in wide industrial applications. But, the stability of motor is found to be dependent on its initial operating condition, showing the chaotic characteristic. Therefore, this paper addresses the chaos control of PMSM by developing four simple but effective controllers, which are mathematically designed by using the principle of Lyapunov’s method for asymptotic global stability. A comparative performance assessment has been carried out for the developed controllers in terms of settling time and peak over shoot. Furthermore, the concept of conventional proportional-integration type controller has been extended to develop two more controllers for chaos control of PMSM. Numerical simulation has been carried out in Matlab environment for performance evaluation of developed controllers. The obtained analytical results have been validated through experimental implementation in real time environment on Multisim/Ultiboard platform.

scholarly journals Purification, characterization and application of novel alkaline protease from new Bacillus cereus UV-15 mutant

2017 ◽  
Vol 7 (4) ◽  
pp. 1 ◽  
Author(s):  
Sreedevi Basavaraju ◽  
Chandrasekhar Kathera ◽  
Pramoda Kumari Jasti
Keyword(s):  
Bacillus Cereus ◽  
Ammonium Sulphate ◽  
Alkaline Protease ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Tween 20 ◽  
Original Activity ◽  
Protease Enzyme

The alkaline protease produced by Bacillus cereus UV-15 mutant was purified by precipitation with ammonium sulphate and gel filtration through sephadex G-100. The enzyme has shown to have a molecular weight of 29kDa by SDS polyacrylamide gel electrophoresis. The extracted protease enzyme was purified by 16.64 fold through ammonium sulphate precipitation and chromatography separation in Sephadex G-100. The purified protease had a specific activity of 2915 (U/mg). The zymogram also revealed a clear hydrolytic zone due to proteolytic activity, which coincided with the band obtained with SDS–PAGE. The enzyme was remained active and stable at pH 8-11, with an optimum at pH 10.0. The protease was stable in the temperature ranging from 40°C to 60°C, but gradually decreased at temperature 70°C. The optimum temperature for protease activity was determined at 60°C. The enzyme showed stability towards non-ionic and anionic surfactants, and oxidizing agents. At 1% concentration of Tween-20 and Tween-80, the enzyme retained 78% and 94% relative activity respectively. Alkaline protease retained 95% activity toward 0.5% concentration of the anionic detergent SDS. The enzyme showed compatibility at 50°C with commercial detergents such as Ariel, Surf excel, Rin, wheel, Tide and Nirma. In the presence of Ariel and Rin the enzyme retained about 72 and 75% of the original activity respectively. The supplementation of the enzyme in detergents could improve the cleansing performance towards the blood stains and suggested to be used as a detergent additive. The enzyme also removed goat hide hairs completely after 15 hr of incubation. These characteristics may make the enzyme suitable for several industrial applications, especially in leather industries.

Sign in / Sign up

Export Citation Format

Share Document