Engineering of Extremophilic Phosphotriesterase-Like Lactonases for Biotechnological Applications

2016 ◽  
pp. 471-503 ◽  
Author(s):  
Elena Porzio ◽  
Immacolata Del Giudice ◽  
Giuseppe Manco
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.

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

Momordica balsamina L.: An Appraisal on Morphology, Ecological Diversity, Phytochemistry, Pharmacological and Biotechnological Applications

2020 ◽  
Vol 06 ◽  
Author(s):  
Saheed Sabiu ◽  
Christiana Eleojo Aruwa ◽  
Viresh Mohanlall ◽  
Himansu Baijnath
Keyword(s):  
Relevant Information ◽  
Perennial Herb ◽  
Biotechnological Applications ◽  
Tropical Regions ◽  
Toxicological Data ◽  
Human Disorders ◽  
Potential Applications ◽  
Baseline Information ◽  
The Caribbean ◽  
Bioactive Agents

Background: Momordica balsamina L. is a monoecious climbing vine and perennial herb native to the tropical regions of Asia, Arabia and the Caribbean, and with prominent presence in Nigeria, Botswana, Namibia, Swaziland and Southern African provinces. While evidence of its anecdotal usage as medicine exist, scientific reports complementing the claims are still emerging or at their infancy. Objective: This review appraised the morphology, therapeutic and biotechnological significance of M. balsamina. Method: Online resources such as Google Scholar, PubMed, ScienceDirect and MeSH were utilized for literature search and included relevant information from inception till May 2020 to streamline sought outcomes for in-depth discussion. Results: The data gathered and considered worthy of inclusion in this study revealed that M. balsamina is rich in phytonutrients of medicinal significance with cucurbitane-type triterpenoids, balsamin and momordins well characterized and fully elucidated. These compounds and other novel bioactive agents in M. balsamina have found remarkable pharmacological relevance and could further be harnessed for use against several debilitating human disorders. Conclusion: The potential applications of M. balsamina as nutraceutical and pharmaceutical agent should not be undermined. Also, with the inadequate toxicological data on this wild species, its consumption should be with caution and translational studies that could advance scientific knowledge and aid better understanding of both its pharmacokinetics and pharmacodynamics without sidelining its potent biotechnological applications are highly encouraged. It is hoped that this paper will provide baseline information that could serve as a guide and inspiration for further studies on the prospects of M. balsamina.

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