scholarly journals Immobilized Forms of the Ophiostoma piceae Lipase for Green Synthesis of Biodiesel. Comparison with Eversa Transform 2.0 and Cal A

2021 ◽  
Vol 7 (10) ◽  
pp. 822
Author(s):  
María Molina-Gutiérrez ◽  
Lorena Alcaraz ◽  
Félix A. López ◽  
Leonor Rodríguez-Sánchez ◽  
María Jesús Martínez ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Green Synthesis ◽  
Catalytic Efficiency ◽  
Functionalized Nanoparticles ◽  
Enzymatic Transesterification ◽  
Recombinant Lipase ◽  
Cooking Oil ◽  
Ophiostoma Piceae ◽  
Mn Oxide ◽  
Green Production

In this work, we analyzed the suitability of a versatile recombinant lipase, secreted by Ophiostoma piceae (OPEr) and produced in Pichia pastoris, as a catalyst of the synthesis of biodiesel. The enzyme was immobilized by five covalent procedures and by hydrophobicity on functionalized nanoparticles of magnetite or of a novel Zn/Mn oxide named G1. Then, they were tested for green production of biodiesel by solventless enzymatic transesterification of discarded cooking oil and methanol (1:4) at 25 °C. The results were compared with those shown by free OPEr and the commercial lipases Eversa® and Cal A®. Several preparations with immobilized OPEr produced high synthesis yields (>90% transesterification), comparable to those obtained with Eversa®, the commercial enzyme designed for this application. Three of the biocatalysts maintained their catalytic efficiency for nine cycles. The process catalyzed by AMNP-CH-OPEr was scaled from 500 µL to 25 mL (50 times), improving its efficiency.

scholarly journals Mutational Analysis of Ocriplasmin to Reduce Proteolytic and Autolytic Activity in Pichia pastoris

2020 ◽  
Vol 22 (1) ◽  
Author(s):  
Roghayyeh Baghban ◽  
Safar Farajnia ◽  
Younes Ghasemi ◽  
Reyhaneh Hoseinpoor ◽  
Azam Safary ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Proteolytic Activity ◽  
Mutational Analysis ◽  
Expression System ◽  
Catalytic Efficiency ◽  
Site Directed Mutagenesis ◽  
Wild Type ◽  
Vitreomacular Adhesion ◽  
Autolytic Activity

Abstract Background Ocriplasmin (Jetrea) is using for the treatment of symptomatic vitreomacular adhesion. This enzyme undergoes rapid inactivation and limited activity duration as a result of its autolytic nature after injection within the eye. Moreover, the proteolytic activity can cause photoreceptor damage, which may result in visual impairment in more serious cases. Results The present research aimed to reduce the disadvantages of ocriplasmin using site-directed mutagenesis. To reduce the autolytic activity of ocriplasmin in the first variant, lysine 156 changed to glutamic acid and, in the second variant for the proteolytic activity reduction, alanine 59 mutated to threonine. The third variant contained both mutations. Expression of wild type and three mutant variants of ocriplasmin constructs were done in the Pichia pastoris expression system. The mutant variants were analyzed in silico and in vitro and compared to the wild type. The kinetic parameters of ocriplasmin variants showed both variants with K156E substitution were more resistant to autolytic degradation than wild-type. These variants also exhibited reduced Kcat and Vmax values. An increase in their Km values, leading to a decreased catalytic efficiency (the Kcat/Km ratio) of autolytic and mixed variants. Moreover, in the variant with A59T mutation, Kcat and Vmax values have reduced compared to wild type. The mix variants showed the most increase in Km value (almost 2-fold) as well as reduced enzymatic affinity to the substrate. Thus, the results indicated that combined mutations at the ocriplasmin sequence were more effective compared with single mutations. Conclusions The results indicated such variants represent valuable tools for the investigation of therapeutic strategies aiming at the non-surgical resolution of vitreomacular adhesion.

Corrigendum to: Green Synthesis of CoFe2O4 and Investigation of its Catalytic Efficiency for Degradation of Dyes in Aqueous Medium

2018 ◽  
Vol 0 (0) ◽  
Author(s):  
Muhammad Saeed ◽  
Asim Mansha ◽  
Muhammad Hamayun ◽  
Aziz Ahmad ◽  
Atta Ulhaq ◽  
...  
Keyword(s):  
Green Synthesis ◽  
Aqueous Medium ◽  
Catalytic Efficiency ◽  
Degradation Of Dyes

Evaluation of the performance of differently immobilized recombinant lipase B from Candida antarctica preparations for the synthesis of pharmacological derivatives in organic media

RSC Advances ◽  
2016 ◽  
Vol 6 (5) ◽  
pp. 4043-4052 ◽  
Author(s):  
Evelin A. Manoel ◽  
Julia M. Robert ◽  
Martina C. C. Pinto ◽  
Antonio C. O. Machado ◽  
Marina D. Besteti ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Candida Antarctica ◽  
Organic Media ◽  
Constitutive Promoter ◽  
Lipase B ◽  
Recombinant Lipase

This paper shows the production of lipase B fromCandida antarctica(LIPB) after cloning the gene that encoded it inPichia pastorisusing PGK as a constitutive promoter. The lipase was immobilized on different home-made supports for distinct reactions.

scholarly journals Green synthesis of Ag and Pd nanoparticles for water pollutants treatment

2020 ◽  
Vol 82 (11) ◽  
pp. 2344-2352
Author(s):  
C. Joseph Kirubaharan ◽  
Zhen Fang ◽  
Chong Sha ◽  
Yang-Chun Yong
Keyword(s):  
Green Synthesis ◽  
Metallic Nanoparticles ◽  
Rhodamine 6G ◽  
Catalytic Efficiency ◽  
Pd Nanoparticles ◽  
Antibacterial Activities ◽  
Klebsiella Pneumonia ◽  
Vibrio Cholera ◽  
Structural Nature ◽  
Ft Ir

Abstract Silver (Ag) and palladium (Pd) nanoparticles were synthesized via a green synthesis route, which was mediated with the extract of Daucus carota leaves. The morphological, crystalline and structural nature of the synthesized nanoparticles was characterized by UV-Vis spectrophotometer, and TEM, XRD and FT-IR analyses. High antibacterial activities of the prepared Ag and Pd nanoparticles were observed towards different water-borne pathogens of Klebsiella pneumonia, Vibrio cholera and Escherichia coli. The catalytic efficiency of the prepared nanoparticles for the removal of rhodamine 6G (Rh-6G) dye was also evaluated. Nearly 98% of the Rh-6G dye was decolorized by the synthesized Pd nanoparticles within 2 min, and the synthesized Ag nanoparticles took 30 min for 89.4% decolorization. This work provided greener nanocatalysts for pollutant treatment and demonstrated the power of green biosynthesis for metallic nanoparticles.

scholarly journals Mutational Analysis of Ocriplasmin to Reduce Proteolytic and Autolytic Activity in Pichia Pastoris

2020 ◽  
Author(s):  
Roghayyeh Baghban ◽  
Safar Farajnia ◽  
Younes Ghasemi ◽  
Reyhaneh Hoseinpoor ◽  
Azam Safary ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Mutational Analysis ◽  
Expression System ◽  
Catalytic Efficiency ◽  
Site Directed Mutagenesis ◽  
Wild Type ◽  
Vitreomacular Adhesion ◽  
Km Value ◽  
Autolytic Activity

Abstract Background: Ocriplasmin (Jetrea) is using for the treatment of symptomatic vitreomacular adhesion. This enzyme undergoes rapid inactivation and limited activities duration as a result of its autolytic and proteolytic nature after injection within the eye. Moreover, the proteolytic activities can cause photoreceptor damage, which may result in visual impairment in the more serious cases.Results: The present research aimed to reduce the disadvantages of ocriplasmin using site-directed mutagenesis. To reduce the autolytic activity of ocriplasmin in the first variant, lysine 156 changed to glutamic acid and in the second variant for the proteolytic activity reduction, alanine 59 mutated to threonine. The third variant contained both the mutations. Expression of wild type and three mutant variants of ocriplasmin constructs were done in Pichia pastoris expression system. The mutant variants analyzed in silico and in vitro and compared to the wild type. The kinetic parameters of ocriplasmin variants showed both variants with K156E substitution were more resistant to autolytic degradation than wild-type. These variants also exhibited reduced Kcat and Vmax values. An increase in their Km values, leading to a decreased catalytic efficiency (the Kcat/Km ratio) of autolytic and mix variants. Moreover, in variant with A59T mutation, Kcat and Vmax values have reduced compared to wild type. The mix variants showed the most increase in Km value (almost 2-fold) as well as reduced enzymatic affinity to the substrate. Thus, the results indicated combine mutations at ocriplasmin sequence were more effective compared with single mutations. Conclusions: The results indicated such variants represent valuable tools for the investigation of therapeutic strategies aiming at non-surgical resolution of vitreomacular adhesion.

Microwave Assisted Envirocat EPZ-10 Catalyzed Multi-component Synthesis of 1-Amidoalkyl-2-naphthols

2021 ◽  
Vol 6 (3) ◽  
pp. 204-210
Author(s):  
Kanchan Joshi-Kulkarni ◽  
Tarulata Chhowala ◽  
Balu Ajalkar
Keyword(s):  
Reaction Time ◽  
Green Synthesis ◽  
Mass Spectroscopy ◽  
Heterogeneous Catalysts ◽  
Catalytic Efficiency ◽  
Solvent Free ◽  
Spectroscopic Methods ◽  
Synthetic Method ◽  
Microwave Assisted ◽  
Solvent Free Reaction

Microwave assisted catalytic efficiency of Envirocat EPZ-10 was explored in solvent free green synthesis of 1-amidoalkyl-2-naphthols by the reaction of aldehyde, 2-naphthol and acetamide. The products formed were characterized by spectroscopic methods such as NMR, IR and mass spectroscopy. The merits of developed synthetic method are use of Envirocat EPZ-10 as eco-friendly, reusable and heterogeneous catalysts, solvent-free reaction, shorter reaction time and easy isolation of product.

Green Synthesis of CoFe2O4 and Investigation of its Catalytic Efficiency for Degradation of Dyes in Aqueous Medium

2018 ◽  
Vol 232 (3) ◽  
pp. 359-371 ◽  
Author(s):  
Muhammad Saeed ◽  
Asim Mansha ◽  
Muhammad Hamayun ◽  
Aziz Ahmad ◽  
Atta Ulhaq ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Green Synthesis ◽  
Aqueous Medium ◽  
Heterogeneous Catalysts ◽  
Aqueous Media ◽  
Catalytic Efficiency ◽  
Catalytic Wet Oxidation ◽  
Simple Method ◽  
Langmuir Hinshelwood Mechanism ◽  
Bimetallic Oxides

AbstractThe catalytic wet oxidation is one the methods used for elimination of dyes from aqueous medium in which various metal based materials can be used as heterogeneous catalysts. Bimetallic oxides as heterogeneous catalysts have gained much attention as bimetallization improve the catalytic properties of the resulting particles. The biosynthetic green method is the most viable and simple method for synthesis of bimetallic oxides nanoparticles. Here, we report the green synthesis of CoFe2O4particles usingAzadirachata indicaleaves extract as reducing and stabilizing agent. The synthesized particles were characterized using X-ray diffraction, thermogravimetric analysis, Fourier-transform infrared spectroscopy and scanning electron microscopy. The synthesized CoFe2O4particles were tested as a catalyst for mineralization of rhodamine B and methylene blue dyes in the presence of hydrogen peroxide in aqueous media. More than 95% dyes degraded in 120 min. The reaction kinetics was described in terms of Langmuir–Hinshelwood mechanism which suggests that molecules of dye and hydrogen peroxide adsorbed surface of CoFe2O4and then react together.

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