Evolutionary Trends in Industrial Production of α-amylase

Background: Amylase catalyzes the breakdown of long-chain carbohydrates to yield maltotriose, maltose, glucose and dextrin as end products. It is present in mammalian saliva and helps in digestion. Objective: Their applications in biotechnology include starch processing, biofuel, food, paper, textile and detergent industries, bioremediation of environmental pollutants and in clinical and medical applications. The commercial microbial strains for production of α-amylase are Bacillus subtilis, B. licheniformis, B. amyloliquefaciens and Aspergillus oryzae. Industrial production of enzymes requires high productivity and cannot use wild-type strains for enzyme production. The yield of enzyme from bacteria can be increased by varying the physiological and genetic properties of strains. Results: The genetic properties of a bacterium can be improved by enhancing the expression levels of the gene and secretion of the enzyme outside the cells, thereby improving the productivity by preventing degradation of enzymes. Overall, the strain for specific productivity should have the maximum ability for synthesis and secretion of an enzyme of interest. Genetic manipulation of α-amylase can also be used for the production of enzymes with different properties, for example, by recombinant DNA technology. Conclusion: This review summarizes different techniques in the production of recombinant α- amylases along with the patents in this arena. The washing out of enzymes in reactions became a limitation in utilization of these enzymes in industries and hence immobilization of these enzymes becomes important. This paper also discusses the immobilization techniques for used α-amylases.

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THE ROLES OF ENZYME IN FOOD PROCESSING - AN OVERVIEW

FUDMA Journal of Sciences ◽

10.33003/fjs-2021-0501-549 ◽

2021 ◽

Vol 5 (1) ◽

pp. 157-164

Author(s):

N. Abdullahi ◽

M. K. Atiku ◽

N. B. Umar

Keyword(s):

Food Processing ◽

Recombinant Dna ◽

Commercial Production ◽

Animal Tissues ◽

Recombinant Dna Technology ◽

Cheese Making ◽

Processing Enzymes ◽

Current Trends ◽

Shelf Life Stability ◽

Immobilization Techniques

Enzymes haven used long in food processing before their discovery as a biological catalyst. Food fermentation was among the early art of food processing and the use of enzymes in fermentation and cheese making started about 6000 BC. The roles of enzymes in food processing and preservation contributed to the development of mankind. They contributed in the areas of baking, cheese making, dairy processing, milling, cereals technology, juice and beverages processing, vegetable processing, oils and fats processing, and wine processing among others. Microorganisms are the earliest and foremost source of enzymes used in food processing, other sources are plant and animal tissues and organs. Advances in science and technology disclosed more potentials of enzymes and biotechnology open doors for commercial production of enzymes with charming properties. The development of enzyme immobilization techniques allows the reused of enzymes without affecting their properties, structure, or activities. Recent advances in genetic engineering and recombinant DNA technology permit the production of enzymes with exceptional properties. The current trends in the production of Extremozymes will open doors for using enzymes under extreme conditions of temperature, pH, and pressure. In food, processing enzymes can be used as ingredients, processing aid, or as a catalyst for both pre-and post-consumption catalysis. Enzymes improve the quality, shelf life, stability, and sensory properties of foods. They play important roles in food processing by lowering energy consumption, minimizing waste, producing desired products specifically required, and making foods more affordable, palatable, and available

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Genetic Manipulation by Recombinant DNA Technology

Molecular Biology ◽

10.1201/b22354-5 ◽

2018 ◽

pp. 219-274

Author(s):

Anjali Priyadarshini ◽

Prerna Pandey

Keyword(s):

Recombinant Dna ◽

Genetic Manipulation ◽

Recombinant Dna Technology ◽

Dna Technology

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Microbial insecticides in forestry

The Forestry Chronicle ◽

10.5558/tfc67473-5 ◽

1991 ◽

Vol 67 (5) ◽

pp. 473-480 ◽

Cited By ~ 4

Author(s):

J. C. Cunningham ◽

K. van Frankenhuyzen

Keyword(s):

Recombinant Dna ◽

Insect Pests ◽

Genetic Manipulation ◽

Microbial Control ◽

Control Agent ◽

Recombinant Dna Technology ◽

Pine Sawfly ◽

Foreign Genes ◽

Bacterium Bacillus ◽

European Pine Sawfly

Research has been conducted in Canada on bacteria, viruses, protozoa, fungi and nematodes for control of forest insect pests. Environmental concerns regarding the use of synthetic chemical pesticides have resulted in increased use of the only microbial control agent that is commercially available, the bacterium Bacillus thuringiensis (B.t.). There are currently 18 B.t. products registered for forestry use in Canada. The greatest use of B.t. has been for control of spruce budworm, Choristoneura Jumiferana, although it has been extensively used on several other species of defoliating lepidopterous pests.The use of other microbial control agents is insignificant compared to B.t. Three viral insecticides containing baculoviruses are registered in Canada, two for control of Douglas-fir tussock moth and one for control of redheaded pine sawfly. Registration petitions have been submitted for viral insecticides to control European pine sawfly and gypsy moth.The advent of recombinant DNA technology has opened the door to limitless possibilities for the genetic manipulation of microbial insecticides. Genetic engineering of B.t. toxin genes into other microorganisms and into plants has been accomplished. Foreign genes have been expressed in baculoviruses; most of these products have pharmaceutical applications unrelated to insect control, but this technology can be used to engineer viral insecticides for enhanced activity.

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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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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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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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