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Microalgae as a Source of Sustainability
Published in Pau Loke Show, Wai Siong Chai, Tau Chuan Ling, Microalgae for Environmental Biotechnology, 2023
Pik Han Chong, Jian Hong Tan, Joshua Troop
In the industry of fine chemicals, natural or modified enzymes are utilized in a process called Biocatalysis (same as biotransformation or bioconversion) to enhance or facilitate the production of molecules. Biocatalysis simplifies the operation of production and saves cost, without the need for living organisms, but it requires chemicals as starting materials. Biosynthesis, on the other hand, uses living organisms to convert organic material into fine chemicals from its cheap and natural feedstock. Recombinant DNA technology is widely applied to produce pharmaceuticals including proteins, antibodies, and hormones. Mammalian cell and plant cell cultures are the common two technologies used to produce fine chemicals. However, mammalian cell culture is much more demanding, requiring stringent operating parameters that cost higher with a factor of 105 (Pollak and Vouillamoz 2013). Mammalian cells cultures are also susceptible to the infection risk or contamination by pathogens from humans or animals. On the contrary, due to the lack of plasmodesmata, plant cell cultures have no means to be susceptible to both plant and animal pathogens, thus making plants a safer choice for pharmaceutical manufacturing. Even so, plant cell technology was not efficient enough to become industrially viable (Xu and Zhang 2014; R. B. Santos et al. 2016).
Soil
Published in Stanley E. Manahan, Environmental Chemistry, 2022
Until the latter 1900s, breeding of improved crops had been a slow process. Starting with domestication of wild species, the development of desired properties, especially higher yield, has occurred over thousands of years. Traditional breeding normally takes such a long time because it depends largely on random mutations to generate desirable characteristics. One of its greatest limitations has been that it is essentially confined to the same species, whereas more often than not, desired characteristics occur in species other than those being bred. Since about the 1970s, however, humans have developed the ability to alter DNA so that organisms synthesize specific proteins and perform other metabolic feats that would otherwise be impossible. Such alteration of DNA by challenging, sophisticated procedures of “cutting and pasting” segments of DNA molecules is commonly known as genetic engineering and recombinant DNA technology. Organisms produced by recombinant DNA techniques that contain DNA from other organisms are called transgenic organisms. With recombinant DNA technology, segments of DNA that contain information for the specific syntheses of particular proteins are transferred between organisms.
Principles and Techniques for Deoxyribonucleic Acid (DNA) Manipulation
Published in Hajiya Mairo Inuwa, Ifeoma Maureen Ezeonu, Charles Oluwaseun Adetunji, Emmanuel Olufemi Ekundayo, Abubakar Gidado, Abdulrazak B. Ibrahim, Benjamin Ewa Ubi, Medical Biotechnology, Biopharmaceutics, Forensic Science and Bioinformatics, 2022
Nwadiuto (Diuto) Esiobu, Ifeoma M. Ezeonu, Francisca Nwaokorie
In nature, DNA replication plays an important role in cell proliferation. It occurs to enhance development of any organism during conception. DNA replication helps in the transfer of genetic information from one generation another through the daughter cells or organisms. Similarly, replication helps to grow organism during infant stage, puberty and adulthood. Furthermore, damaged or aged tissues are replaced by this process. DNA replication can also be demonstrated experimentally. This has formed the basis for several discoveries and applications in biotechnology. Our understanding of the mechanisms underlying the in-vivo DNA replication, has fueled many advances in the production of recombinant DNA used for genetic engineering, and in genetic modification. In vitro techniques like polymerase chain reaction (PCR) for example, use synthetic primers (to mimic the role of the primase and RNA primers in vivo) for “replication” of DNA segments. During cloning, the DNA must be replicated within a host to provide a large quantity of identical DNA needed for probes or other research applications. DNA replication takes place continuously and at a faster rate in prokaryotes than in eukaryotes. DNA replication is a timed event that correlates with characteristics and functionalities of gene expression, chromatin state, Guanine and Cytosine (GC) contents, and sub-nuclear structure. In biotechnology, plasmids, which are autonomously replicating circular DNA molecules found in most bacteria, are used extensively in many recombinant DNA projects.
Challenges and advancements in the pharmacokinetic enhancement of therapeutic proteins
Published in Preparative Biochemistry & Biotechnology, 2021
Farnaz Khodabakhsh, Morteza Salimian, Mohammad Hossein Hedayati, Reza Ahangari Cohan, Dariush Norouzian
Recently, blood coagulation factors, hormones, cytokines, and monoclonal antibodies have been popularly used in the treatment of human disorders. Medical application of proteins has further expanded with the advent of recombinant DNA technology as recombinant proteins are now considered as main regimens in therapeutic protocols.[1] However, based on complications related to the therapeutic proteins, in vivo administration of proteins are often encountered with some limitations that restrict their clinical applications. Like chemical drugs, therapeutic proteins must reach a specific plasma range, called the therapeutic window, to show the beneficial effects, and therefore, their efficacies mainly depend on the residence time in the body. Unfortunately, proteins have a rapid clearance from the body based on intrinsic structural instability and body environment. The elementary solution for solving this problem was frequent administrations of proteins at specific intervals to achieve the therapeutic goal. However, frequent administration increases both therapy costs and by-stander effects that finally lead to low patient compliance.[2] Moreover, dose enhancement cannot be used for the compensation of short in vivo half-life of proteins because it remarkably leads to an increase in the side-effects.[3] Therefore, many attempts have been carried out to extend the plasma half-life of therapeutic proteins through different approaches. Since information about the metabolic pathways of protein is essential and gives us a better comprehensive understanding of the half-life of proteins in the body, the following section describes these pathways in detail.
Compartmentalization of therapeutic proteins into semi-crystalline PEG-PCL polymersomes
Published in Soft Materials, 2021
Juliana de Almeida Pachioni-Vasconcelos, Alexsandra Conceição Apolinário, André Moreni Lopes, Adalberto Pessoa, Leandro Ramos Souza Barbosa, Carlota de Oliveira Rangel-Yagui
Recombinant DNA technology has allowed a widespread production of biological drugs such as enzymes, antibodies, and hormones, which are attractive due to their high potency and high selectivity.[1] However, protein drugs usually present pharmacokinetic limitations such as short therapeutic half-lives attributed to poor in vivo stability and immunogenicity.[2d] To overcome these drawbacks, nanocarriers are an interesting alternative, allowing protein drugs stabilization and increasing their applications.[3]
Optimizing secretory expression of recombinant human interferon gamma from Kluyveromyces lactis
Published in Preparative Biochemistry & Biotechnology, 2018
Rajat Pandey, Venkata Dasu Veeranki
Producing therapeutic proteins in vitro using modern recombinant DNA technologies has become an established yet active field of research for major pharmaceutical companies as well as academic institutions. To minimize the upstream processing cost, for the most obvious and cheap expression system Escherichia coli is most widely used to produce these proteins, but major problems arising due to the use of E. coli are bacterial endotoxin,[1] inclusion body formation, and expensive downstream processing cost. Purification of target protein from a vast pool of E. coli native proteins also becomes a bottleneck. The need to produce recombinant therapeutic proteins in large quantities without forming inclusion bodies and ease of target protein purification directly from medium broth has pushed researchers to go beyond E. coli and explore alternate USFDA-approved GRAS (generally regarded as safe) platforms for therapeutic protein production such as Kluyveromyces lactis,[2]Bacillus subtilis,[3]and Pichia pastoris.[4] Expressing heterologous proteins in these organisms not only eliminates the need of endotoxin analysis but some of these organisms are also capable of secreting the target protein in the fermentation medium as well, thereby easing the task of target protein isolation and reducing the cost of purification drastically. Our research group at Biochemical engineering laboratory, IIT Guwahati, is working toward redressal of this problem by investigating several GRAS expression systems such as K. lactis, B. subtilis, P. pastoris for their ability to produce recombinant therapeutic proteins. K. lactis is “budding yeast” from the phylum Ascomycota. It is evolutionarily closely related to the well-known baker’s yeast Saccharomyces cerevisiae.[5]K. lactis possesses a highly expressed β-galactosidase that degrades milk sugar lactose to galactose and glucose.[6]K. lactis is a natural and indispensable component of cultured dairy processes where lactose concentration is very high.