scholarly journals Recombinant Fungal Cellulases for the Saccharification of Sugarcane Bagasse

2021 ◽  
Author(s):  
Raquel Guimarães Benevides ◽  
Sandra Aparecida de Assis ◽  
Alison Borges Vitor ◽  
Geise Camila Ribeiro ◽  
Cleidineia Souza de Santana ◽  
...  

Cellulases are important enzymes in cellulose degradation that occurs in nature, this degradation involves a system of extracellular multienzymes and have wide application. The construction of a high-quality system for the production of these enzymes is important for its application in the process of saccharification of biomass involved in the biofuel production process. Several species of fungi are capable of synthesizing and secreting high amounts of cellulase, most studies with fungal species use linearized plasmid, since these are encompassed to chromosomal DNA, improving its stability and expression efficiency. Advances in the production of recombinant enzymes focus on the search for industrially viable microorganisms capable of producing enzymes under various conditions, expressing them in a highly efficient manner, aiming at the synthesis of several copies of genes and a strong promoter. To resay these restrictions, molecular biology combined with recombinant DNA technology is a viable tool in enzymatic production. In subsequent topics, the production of endoglucanases, exoglucanases and β-glucosidase of fungi cloned in Escherichia coli, Pichia pastoris and other different expression systems will be addressed.

Author(s):  
Ishan H. Raval ◽  
Arvind Kumar Singh Chandel

The enzymes' biocatalysts act by lowering the activation energy without getting consumed in the reaction. The immense number of enzymes acts as a correctly matched orchestra to ensure that enormously complex life mechanisms and processes occur in a right direction. Sufficient quantity and accurate function of enzymes results in proper functional maintenance of body. The enzymes play a major role in the diagnosis, curing, biochemical investigation, and monitoring of many dreaded diseases of the century. The development of recombinant DNA technology had a significant impression on production levels of enzymes. Around 50% of the enzyme market is covered by recombinant enzymes. Because of development in molecular biology tools, several pharmaceutically enzymes have been identified and are being actively used in the pharmaceutical industry either for diagnostic or treatment. Information on this topic is very insufficient, and thus, the present chapter is an attempt to compile information on the sources, properties and applications of important therapeutic enzymes.


2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Md. Fakruddin ◽  
Reaz Mohammad Mazumdar ◽  
Khanjada Shahnewaj Bin Mannan ◽  
Abhijit Chowdhury ◽  
Md. Nur Hossain

E. coli is the most frequently used host for production of enzymes and other proteins by recombinant DNA technology. E. coli is preferable for its relative simplicity, inexpensive and fast high-density cultivation, well-known genetics, and large number of compatible molecular tools available. Despite all these advantages, expression and production of recombinant enzymes are not always successful and often result in insoluble and nonfunctional proteins. There are many factors that affect the success of cloning, expression, and mass production of enzymes by recombinant E. coli. In this paper, these critical factors and approaches to overcome these obstacles are summarized focusing controlled expression of target protein/enzyme in an unmodified form at industrial level.


2017 ◽  
Vol 2 (2) ◽  
pp. 74-97 ◽  
Author(s):  
Arnold L. Demain ◽  
Sergio Sánchez

For many years, industrial enzymes have played an important role in the benefit of our society due to their many useful properties and a wide range of applications. They are key elements in the progress of many industries including foods, beverages, pharmaceuticals, diagnostics, therapy, personal care, animal feed, detergents, pulp and paper, textiles, leather, chemicals and biofuels. During recent decades, microbial enzymes have replaced many plant and animal enzymes. This is because microbial enzymes are widely available and produced economically in short fermentations and inexpensive media. Screening is simple, and strain improvement for increased production has been very successful. The advances in recombinant DNA technology have had a major effect on production levels of enzymes and represent a way to overproduce industrially important microbial, plant and animal enzymes. It has been calculated that 50-60% of the world enzyme market is supplied with recombinant enzymes. Molecular methods, including genomics and metagenomics, are being used for the discovery of new enzymes from microbes. Also, directed evolution has allowed the design of enzyme specificities and better performance.


2008 ◽  
Vol 59 (11) ◽  
Author(s):  
Iulia Lupan ◽  
Sergiu Chira ◽  
Maria Chiriac ◽  
Nicolae Palibroda ◽  
Octavian Popescu

Amino acids are obtained by bacterial fermentation, extraction from natural protein or enzymatic synthesis from specific substrates. With the introduction of recombinant DNA technology, it has become possible to apply more rational approaches to enzymatic synthesis of amino acids. Aspartase (L-aspartate ammonia-lyase) catalyzes the reversible deamination of L-aspartic acid to yield fumaric acid and ammonia. It is one of the most important industrial enzymes used to produce L-aspartic acid on a large scale. Here we described a novel method for [15N] L-aspartic synthesis from fumarate and ammonia (15NH4Cl) using a recombinant aspartase.


2021 ◽  
Vol 11 (12) ◽  
pp. 5352
Author(s):  
Ana Margarida Pereira ◽  
Diana Gomes ◽  
André da Costa ◽  
Simoni Campos Dias ◽  
Margarida Casal ◽  
...  

Antibacterial resistance is a major worldwide threat due to the increasing number of infections caused by antibiotic-resistant bacteria with medical devices being a major source of these infections. This suggests the need for new antimicrobial biomaterial designs able to withstand the increasing pressure of antimicrobial resistance. Recombinant protein polymers (rPPs) are an emerging class of nature-inspired biopolymers with unique chemical, physical and biological properties. These polymers can be functionalized with antimicrobial molecules utilizing recombinant DNA technology and then produced in microbial cell factories. In this work, we report the functionalization of rPBPs based on elastin and silk-elastin with different antimicrobial peptides (AMPs). These polymers were produced in Escherichia coli, successfully purified by employing non-chromatographic processes, and used for the production of free-standing films. The antimicrobial activity of the materials was evaluated against Gram-positive and Gram-negative bacteria, and results showed that the polymers demonstrated antimicrobial activity, pointing out the potential of these biopolymers for the development of new advanced antimicrobial materials.


1992 ◽  
Vol 38 (Special) ◽  
pp. 263-266
Author(s):  
O. IFUKU ◽  
S. HAZE ◽  
J. KISHIMOTO ◽  
M. YANAGI

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