Polypropylene As A Selective Support For The Immobilization Of Lipolytic Enzymes: Hyper‐Activation, Purification And Biotechnological Applications

2021 ◽  
Author(s):  
M. Guadalupe Sánchez‐Otero ◽  
Rodolfo Quintana‐Castro ◽  
Adela‐Sofía Rojas‐Vázquez ◽  
Giselle‐Lilian Badillo‐Zeferino ◽  
Karina Mondragón‐Vázquez ◽  
...  
Keyword(s):  
Biotechnological Applications ◽  
Lipolytic Enzymes

scholarly journals Classification of lipolytic enzymes and their biotechnological applications in the pulping industry

2017 ◽  
Vol 63 (3) ◽  
pp. 179-192 ◽  
Author(s):  
L. Ramnath ◽  
B. Sithole ◽  
R. Govinden
Keyword(s):  
Fatty Acids ◽  
Paper Industry ◽  
Pulp And Paper Industry ◽  
Pulp And Paper ◽  
Biotechnological Applications ◽  
Lipolytic Enzymes ◽  
Prevention And Treatment ◽  
Potential Applications ◽  
Microbial Sources

In the pulp and paper industry, during the manufacturing process, the agglomeration of pitch particles (composed of triglycerides, fatty acids, and esters) leads to the formation of black pitch deposits in the pulp and on machinery, which impacts on the process and pulp quality. Traditional methods of pitch prevention and treatment are no longer feasible due to environmental impact and cost. Consequently, there is a need for more efficient and environmentally friendly approaches. The application of lipolytic enzymes, such as lipases and esterases, could be the sustainable solution to this problem. Therefore, an understanding of their structure, mechanism, and sources are essential. In this report, we review the microbial sources for the different groups of lipolytic enzymes, the differences between lipases and esterases, and their potential applications in the pulping industry.

Plant Lipases

2018 ◽  
pp. 58-88
Keyword(s):  
Gastrointestinal Tract ◽  
Structural Characterization ◽  
Pancreatic Insufficiency ◽  
Biochemical Properties ◽  
Biotechnological Applications ◽  
Lipolytic Enzymes ◽  
Acid Stable ◽  
Alternative Remedies

Most searches in plant lipases have been devoted to seed lipases, but other sources of plant lipases are being exploited. The current chapter is undertaken to show readily available sources of lipases from plants as well as for their biochemical properties and some of their other eminent characteristics. The sequence and structural characterization into these lipolytic enzymes as well as their importance for biotechnological applications would also be the focus of this chapter. In fact, plant lipases have interesting features, particularly biochemical properties (e.g., pH and temperature), and with respect to their specific hydrolytic properties would make these enzymes alternative remedies for treatment of many diseases of the gastrointestinal tract and of pancreatic insufficiency with exogenous plant acid stable lipases.

C1 Microbes And Biotechnological Applications

2018 ◽  
Author(s):  
Ludmila Chistoserdova
Keyword(s):  
Biotechnological Applications

Nε-Acetyl L-α Lysine Improves Activity and Stability of α-Amylase at Acidic Conditions: A Comparative Study with other Osmolytes

2020 ◽  
Vol 27 (6) ◽  
pp. 551-556
Author(s):  
Nidhya N. Joghee ◽  
Gurunathan Jayaraman ◽  
Masilamani Selladurai
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Thermodynamic Stability ◽  
Protective Effects ◽  
Residual Enzyme Activity ◽  
Functional Stability ◽  
Biotechnological Applications ◽  
Optimal Temperature ◽  
Acidic Conditions ◽  
Cellular Components

Background: Nε-acetyl L-α lysine is an unusual acetylated di-amino acid synthesized and accumulated by certain halophiles under osmotic stress. Osmolytes are generally known to protect proteins and other cellular components under various stress conditions. Objective: The structural and functional stability imparted by Nε-acetyl L-lysine on proteins were unknown and hence was studied and compared to other commonly known bacterial osmolytes - ectoine, proline, glycine betaine, trehalose and sucrose. Methods: Effects of osmolytes on the temperature and pH profiles, pH stability and thermodynamic stability of the model enzyme, α-amylase were analyzed. Results: At physiological pH, all the osmolytes under study increased the optimal temperature for enzyme activity and improved the thermodynamic stability of the enzyme. At acidic conditions (pH 3.0), Nε-acetyl L-α lysine and ectoine improved both the catalytic and thermodynamic stability of the enzyme; it was reflected in the increase in residual enzyme activity after incubation of the enzyme at pH 3.0 for 15 min by 60% and 63.5% and the midpoint temperature of unfolding transition by 11°C and 10°C respectively. Conclusion: Such significant protective effects on both activity and stability of α-amylase imparted by addition of Nε-acetyl L-α lysine and ectoine at acidic conditions make these osmolytes interesting candidates for biotechnological applications.

Enhanced Biocatalytic Activity of Recombinant Lipase Immobilized on Gold Nanoparticles

2019 ◽  
Vol 20 (6) ◽  
pp. 497-505 ◽  
Author(s):  
Abeer M. Abd El-Aziz ◽  
Mohamed A. Shaker ◽  
Mona I. Shaaban
Keyword(s):  
Gold Nanoparticles ◽  
Lipolytic Activity ◽  
Market Demand ◽  
Biotechnological Applications ◽  
Lipase Gene ◽  
Expression Plasmid ◽  
E Coli ◽  
Nickel Affinity Chromatography ◽  
Recombinant Production ◽  
Sds Page

Background: Bacterial lipases especially Pseudomonas lipases are extensively used for different biotechnological applications. Objectives: With the better understanding and progressive needs for improving its activity in accordance with the growing market demand, we aimed in this study to improve the recombinant production and biocatalytic activity of lipases via surface conjugation on gold nanoparticles. Methods: The full length coding sequences of lipase gene (lipA), lipase specific foldase gene (lipf) and dual cassette (lipAf) gene were amplified from the genomic DNA of Pseudomonas aeruginosa PA14 and cloned into the bacterial expression vector pRSET-B. Recombinant lipases were expressed in E. coli BL-21 (DE3) pLysS then purified using nickel affinity chromatography and the protein identity was confirmed using SDS-PAGE and Western blot analysis. The purified recombinant lipases were immobilized through surface conjugation with gold nanoparticles and enzymatic activity was colorimetrically quantified. Results: Here, two single expression plasmid systems pRSET-B-lipA and pRSET-B-lipf and one dual cassette expression plasmid system pRSET-B-lipAf were successfully constructed. The lipolytic activities of recombinant lipases LipA, Lipf and LipAf were 4870, 426 and 6740 IUmg-1, respectively. However, upon immobilization of these recombinant lipases on prepared gold nanoparticles (GNPs), the activities were 7417, 822 and 13035 IUmg-1, for LipA-GNPs, Lipf-GNPs and LipAf-GNPs, respectively. The activities after immobilization have been increased 1.52 and 1.93 -fold for LipA and LipAf, respectively. Conclusion: The lipolytic activity of recombinant lipases in the bioconjugate was significantly increased relative to the free recombinant enzyme where immobilization had made the enzyme attain its optimum performance.

Significance of Lipolytic Enzymes in Pathogenesis and Treatment of Neglected Diseases

2015 ◽  
Vol 16 (999) ◽  
pp. 1-1
Author(s):  
D Chakravorty ◽  
S Patra
Keyword(s):  
Neglected Diseases ◽  
Lipolytic Enzymes

Biotechnological Applications of Thermus thermophilus as Host

2013 ◽  
Vol 2 (4) ◽  
pp. 304-312 ◽  
Author(s):  
Aurelio Hidalgo ◽  
José Berenguer
Keyword(s):  
Thermus Thermophilus ◽  
Biotechnological Applications

Editorial (Thematic Issue: Biotechnological Applications of Extremophiles)

2013 ◽  
Vol 2 (4) ◽  
pp. 273-274 ◽  
Author(s):  
Pabulo Rampelotto
Keyword(s):  
Thematic Issue ◽  
Biotechnological Applications

Isolation of Astaxanthin-Producing Microalgae and Potential Biotechnological Applications

2016 ◽  
Vol 4 (4) ◽  
pp. 492-498 ◽  
Author(s):  
Katsuhiko Fujii
Keyword(s):  
Biotechnological Applications
Sign in / Sign up

Export Citation Format

Share Document