44 Amino acids in livestock: A historical perspective

Abstract The advent of commercially viable synthetic amino acids (AA) and least cost formulation (LCF) have fundamentally changed swine and poultry diets over the past 40 years. Amino acids can be produced by chemical synthesis, hydrolysis of intact proteins and fermentation. Chemical synthesis of AA was first reported by Strecker (1850). Discovery of glutamate as the basis of Umami taste category (1907) spurred commercial AA production by hydrolysis. The discovery of commercially viable fermentative production of glutamate, by Kyowa Hakko Kogyo Co. (1957), revolutionized AA production. Their parallel discovery of lysine (Lys) production, using a natural C. glutmanicum mutant subsequently followed. This led to further screening for bacterial mutants for threonine (Thr, 1961), tryptophan (Trp, 1972), valine (Val, 1959) and isoleucine (Ile, 1972). The next milestone occurred with development of the first main-frame LCF programs (1960s). The first commercial application of dietary AA involved methionine (Met) for poultry, followed closely by Lys in swine. Use of other synthetic AA was cost-prohibitive, but they served as research tools. The next revolution involved recombinant DNA technology (1980s), which dramatically increased AA yield and reduced production cost. Simultaneously, development of PC based LCF enabled cost effective formulation. Subsequently, growth-derived AA ratio’s emerged from the labs of Fuller (1989) and Baker (1992). Patent expirations in the late 1980s led to new companies that produced rapid advances in fermentation methods, with new recombinant strains. Production cost declined further for Lys (1988), and production efficiencies allowed Thr (1995) and Trp (2000) to enter commercial diets. Advances in fermentation technology have enabled production of all ten essential AA. Extensive AA displacement of protein supplements has led to an ever-expanding global tonnage of AA for food and pet animals. With routine addition of 4–6 AA in swine diets, we question whether non-essential AA nitrogen may emerge as limiting (essential).

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Enzymatic Synthesis of 15N-L-aspartic Acid Using Recombinant Aspartase from Escherichia Coli K12

Revista de Chimie ◽

10.37358/rc.08.11.2004 ◽

2008 ◽

Vol 59 (11) ◽

Cited By ~ 1

Author(s):

Iulia Lupan ◽

Sergiu Chira ◽

Maria Chiriac ◽

Nicolae Palibroda ◽

Octavian Popescu

Keyword(s):

Amino Acids ◽

Aspartic Acid ◽

Enzymatic Synthesis ◽

Large Scale ◽

Recombinant Dna ◽

Industrial Enzymes ◽

Recombinant Dna Technology ◽

Bacterial Fermentation ◽

Natural Protein ◽

Novel Method

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.

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Biological control of arthropod pests: Traditional and emerging technologies

American Journal of Alternative Agriculture ◽

10.1017/s0889189300002198 ◽

1988 ◽

Vol 3 (2-3) ◽

pp. 63-68 ◽

Cited By ~ 6

Author(s):

Marjorie A. Hoy

Keyword(s):

Biological Control ◽

Genetic Improvement ◽

New Technologies ◽

Recombinant Dna ◽

Cost Effective ◽

Agricultural Crops ◽

Practical Application ◽

Recombinant Dna Technology ◽

History Of ◽

Arthropod Pests

AbstractBiological control of arthropod pests has a long history of useful practical application. Parasites, predators, and pathogens have been employed in many cases to control pest arthropods in an efficient, cost-effective, and permanent manner. The traditional tactics used in biological control (classical, augmentation, and conservation) remain vital and valuable tools in the biological control of pests for agricultural crops, range lands, forests, and glasshouses. New technologies offer promise. One emerging technique involves the genetic improvement of natural enemies of arthropods through selection, hybridization, or recombinant DNA technology.

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Biosynthesis and Processing of Silk Proteins

MRS Bulletin ◽

10.1557/s0883769400046479 ◽

1992 ◽

Vol 17 (10) ◽

pp. 41-47 ◽

Cited By ~ 41

Author(s):

David L. Kaplan ◽

Stephen Fossey ◽

Charlene M. Mello ◽

Steven Arcidiacono ◽

Kris Senecal ◽

...

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Recombinant Dna ◽

Hydrophobic Interactions ◽

Genetic Manipulation ◽

Larval Instar ◽

Side Chain ◽

Recombinant Dna Technology ◽

Short Side ◽

Orb Web

Silks produced by silkworms (e.g., Bombyx mori) and orb-web weaving spiders (e.g., Nephila clavipes) are essentially pure protein, that is, complexes of amino acid polymers. They are the most common fibers spun by biological systems. There has been a long-standing interest in the use of these and similar fibers in textiles, cables, fiber reinforcement in composites, in addition, for example, to cross hairs in optical instruments, and fishing nets. Both nylon, a homo-polymer of the amino acid glycine, and Kevlar, a polymer of a nonnatural aromatic amino acid, can be considered modified, synthetic versions of silk and are used for some of the applications mentioned above. The potential for genetic manipulation, through recombinant DNA technology, of the natural biosynthetic process for these natural proteins (see the article by Cappello in this issue) has renewed interest in the production of new silklike proteins.The natural silks are characterized by a β-sheet secondary structure which is stabilized by interchain hydrogen bonds and intersheet hydrophobic interactions (Figure 1). Silks can be considered block copolymers, with crystalline domains consisting of short side chain monomers (the amino acids glycine, alanine, and serine) interspersed in amorphous domains consisting of bulkier side chain amino acids.This family of fibers is naturally tailored to perform functions such as catching prey (orb web) or serving as a barrier against environmental challenges (cocoon). The domestic silkworm (B. mori) produces only one type of silk, cocoon silk, at only one stage in its lifecyle, during the fifth larval instar just before molt to the pupa. The silk is produced in modified salivary glands and spun from the mouth.

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A comprehensive comparison between camelid nanobodies and single chain variable fragments

Biomarker Research ◽

10.1186/s40364-021-00332-6 ◽

2021 ◽

Vol 9 (1) ◽

Author(s):

Yasaman Asaadi ◽

Fatemeh Fazlollahi Jouneghani ◽

Sara Janani ◽

Fatemeh Rahbarizadeh

Keyword(s):

Production Cost ◽

Recombinant Dna ◽

Antibody Fragments ◽

Structure And Properties ◽

Single Chain ◽

Recombinant Dna Technology ◽

Variable Domains ◽

Comprehensive Comparison ◽

Single Chain Variable Fragments ◽

Lower Production

AbstractBy the emergence of recombinant DNA technology, many antibody fragments have been developed devoid of undesired properties of natural immunoglobulins. Among them, camelid heavy-chain variable domains (VHHs) and single-chain variable fragments (scFvs) are the most favored ones. While scFv is used widely in various applications, camelid antibodies (VHHs) can serve as an alternative because of their superior chemical and physical properties such as higher solubility, stability, smaller size, and lower production cost. Here, these two counterparts are compared in structure and properties to identify which one is more suitable for each of their various therapeutic, diagnosis, and research applications.

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Design, Development, and Performance Evaluation of a Power-Operated Jute Fiber Extraction Machine

AgriEngineering ◽

10.3390/agriengineering3020027 ◽

2021 ◽

Vol 3 (2) ◽

pp. 403-422

Author(s):

Md. Rejaul Karim ◽

Muhammad Arshadul Hoque ◽

Alamgir Chawdhury ◽

Faruk-Ul-Islam ◽

Sharif Ahmed ◽

...

Keyword(s):

Performance Evaluation ◽

Production Cost ◽

Cost Effective ◽

Labor Cost ◽

Jute Fiber ◽

Design Development ◽

Regional Office ◽

Practical Action ◽

Traditional System ◽

Fiber Extraction

Jute is the golden fiber of Bangladesh, but its production is declining due to the involvement of higher production and processing costs, where a major portion of the cost is needed for fiber extraction. Labor unavailability and increasing labor cost have led to higher jute fiber production cost. To address these issues, this study looks at the development of a power-operated and cost-effective fiber extraction machine aiming at reducing the production cost. The study was conducted at the Rangpur regional office premises of Practical Action in Bangladesh, and the developed machine was branded as “Aashkol”, which had the following major parts: a feeding tray, a primary extraction roller, a secondary extraction roller, grabbing rollers, fiber collection stand, base frame, protection cover, and a spring-loaded tray under the primary extraction roller. The Aashkol can extract green ribbon from the jute stem, but jute sticks were broken down into smaller pieces (3–6 cm). The performance evaluation of the machine was conducted using different types of jute (Deshi, Kenaf, and Tossa) and compared with another jute extraction machine (KP model, introduced by Karupannya Rangpur Ltd.). The Aashkol-based extraction and improved retting systems were also evaluated and compared with traditional jute extraction systems. The jute stem input capacity (4.99 t h−1) of the Aashkol was 47.6% higher than the KP model (3.38 t h−1). Compared with the traditional system, across jute types, the Aashkol produced a 9% higher fiber yield and saved 46% retting time. Overall, the Aashkol reduced 90% of the labor requirement and saved 11.6 USD t−1 in jute fiber extraction and retting than the traditional method.

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Protein-Engineered Polymers Functionalized with Antimicrobial Peptides for the Development of Active Surfaces

Applied Sciences ◽

10.3390/app11125352 ◽

2021 ◽

Vol 11 (12) ◽

pp. 5352

Author(s):

Ana Margarida Pereira ◽

Diana Gomes ◽

André da Costa ◽

Simoni Campos Dias ◽

Margarida Casal ◽

...

Keyword(s):

Antimicrobial Activity ◽

Antimicrobial Peptides ◽

Recombinant Dna ◽

Biological Properties ◽

Resistant Bacteria ◽

Recombinant Dna Technology ◽

Free Standing ◽

Microbial Cell Factories ◽

Cell Factories ◽

Antimicrobial Materials

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.

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