scholarly journals Industrial Enzymes and Metabolites from Actinobacteria in Food and Medicine Industry

10.5772/61286 ◽  
2016 ◽  
Author(s):  
María Valdés Ramírez ◽  
Liliana Calzadíaz
Keyword(s):  
Industrial Enzymes

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

2008 ◽  
Vol 59 (11) ◽  
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.

scholarly journals β-Galactosidase-Producing Isolates in Mucoromycota: Screening, Enzyme Production, and Applications for Functional Oligosaccharide Synthesis

2021 ◽  
Vol 7 (3) ◽  
pp. 229
Author(s):  
Bettina Volford ◽  
Mónika Varga ◽  
András Szekeres ◽  
Alexandra Kotogán ◽  
Gábor Nagy ◽  
...  
Keyword(s):  
Wheat Bran ◽  
Enzyme Production ◽  
Specific Activity ◽  
Prebiotic Synthesis ◽  
Crude Enzyme ◽  
Oligosaccharide Synthesis ◽  
Industrial Enzymes ◽  
Chromogenic Agar ◽  
Lichtheimia Ramosa ◽  
Excellent Source

β-Galactosidases of Mucoromycota are rarely studied, although this group of filamentous fungi is an excellent source of many industrial enzymes. In this study, 99 isolates from the genera Lichtheimia, Mortierella, Mucor, Rhizomucor, Rhizopus and Umbelopsis, were screened for their β-galactosidase activity using a chromogenic agar approach. Ten isolates from the best producers were selected, and the activity was further investigated in submerged (SmF) and solid-state (SSF) fermentation systems containing lactose and/or wheat bran substrates as enzyme production inducers. Wheat bran proved to be efficient for the enzyme production under both SmF and SSF conditions, giving maximum specific activity yields from 32 to 12,064 U/mg protein and from 783 to 22,720 U/mg protein, respectively. Oligosaccharide synthesis tests revealed the suitability of crude β-galactosidases from Lichtheimia ramosa Szeged Microbiological Collection (SZMC) 11360 and Rhizomucor pusillus SZMC 11025 to catalyze transgalactosylation reactions. In addition, the crude enzyme extracts had transfructosylation activity, resulting in the formation of fructo-oligosaccharide molecules in a sucrose-containing environment. The maximal oligosaccharide concentration varied between 0.0158 and 2.236 g/L depending on the crude enzyme and the initial material. Some oligosaccharide-enriched mixtures supported the growth of probiotics, indicating the potential of the studied enzyme extracts in future prebiotic synthesis processes.

Epoxy Sepabeads: A Novel Epoxy Support for Stabilization of Industrial Enzymes via Very Intense Multipoint Covalent Attachment

2002 ◽  
Vol 18 (3) ◽  
pp. 629-634 ◽  
Author(s):  
C. Mateo ◽  
O. Abian ◽  
G. Fernandez-Lorente ◽  
J. Pedroche ◽  
R. Fernandez-Lafuente ◽  
...  
Keyword(s):  
Covalent Attachment ◽  
Industrial Enzymes ◽  
Multipoint Covalent Attachment

scholarly journals Rational protein design for enhancing thermal stability of industrial enzymes

2020 ◽  
Vol 8 (1) ◽  
pp. 3-17
Author(s):  
Le Quang Anh Tuan
Keyword(s):  
High Temperature ◽  
Protein Engineering ◽  
Protein Design ◽  
Disulfide Bonds ◽  
Industrial Applications ◽  
Enzymatic Reactions ◽  
Industrial Enzymes ◽  
Effective Strategies ◽  
Environmental Treatment ◽  
Pharmaceutical Production

Enzymes possessing many excellent properties such as high selectivity, consuming less energy, and producing less side products or waste have been widely applied as biocatalysts in pharmaceutical production and many industries such as biofuel, biomaterials, biosensor, food, and environmental treatment. Although enzymes have shown its potential as biocatalysts for many industrial applications, natural enzymes were not originated for manufacturing process which requires harsh reaction conditions such as high temperature, alkaline pH, and organics solvents. It was reported that reduction of final conversion of several enzymatic reactions was declined at high temperature. Protein engineering to improve the enzymes’ thermostability is crucial to extend the use of the industrial enzymes and maximize effectiveness of the enzyme-based procesess. Various industrial enzymes with improved thermostability were produced through rational protein engineering using different strategies. This review is not aimed to cover all successful rational protein engineering studies. The review focuses on some effective strategies which have widely used to increase the thermostability of several industrial enzymes through introduction of disulfide bonds and introduction of proline.

scholarly journals An overview on current molecular tools for heterologous gene expression in Trichoderma

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Irene Tomico-Cuenca ◽  
Robert L. Mach ◽  
Astrid R. Mach-Aigner ◽  
Christian Derntl
Keyword(s):  
Gene Expression ◽  
Protein Expression ◽  
Protein Secretion ◽  
Heterologous Gene Expression ◽  
Heterologous Gene ◽  
Molecular Tools ◽  
Expression Systems ◽  
Industrial Enzymes ◽  
Nutrient Sources ◽  
Transformation Methods

AbstractFungi of the genus Trichoderma are routinely used as biocontrol agents and for the production of industrial enzymes. Trichoderma spp. are interesting hosts for heterologous gene expression because their saprotrophic and mycoparasitic lifestyles enable them to thrive on a large number of nutrient sources and some members of this genus are generally recognized as safe (GRAS status). In this review, we summarize and discuss several aspects involved in heterologous gene expression in Trichoderma, including transformation methods, genome editing strategies, native and synthetic expression systems and implications of protein secretion. This review focuses on the industrial workhorse Trichoderma reesei because this fungus is the best-studied member of this genus for protein expression and secretion. However, the discussed strategies and tools can be expected to be transferable to other Trichoderma species.

scholarly journals Biosynthesis of industrial enzymes by free and immobilized Alicyclobacillus in different matrices and the use of ultrafiltration in the enzymes concentration

Química Nova ◽  
2017 ◽  
Author(s):  
Suelen Pereira Ruiz ◽  
Juliana Harumi Miyoshi ◽  
Gabriela Gregolin Gimenez ◽  
Camila Ortiz Martinez ◽  
Benício Alves de Abreu Filho ◽  
...  
Keyword(s):  
Industrial Enzymes
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