Industrial applications of actinobacterial enzymes
Biocatalysis offers green and clean solutions to chemical processes and is emerging as an effective alternative to chemical technology. The chemical processes are now carried out by biocatalysts (enzymes) which are essential components of all biological systems. However, the utility of enzymes is not naive to us, as they have been a vital part of our lives from immemorial times. Their use in fermentation processes like wine and beer manufacture, vinegar production, and bread making has been practised for several decades. However, a commercial breakthrough happened during the middle of the 20th century with the first commercial protease production. Since then, due to the development of newer industries, the enzyme industry has not only seen a remarkable growth but has also matured with a technology-oriented perspective. Commercially available enzymes are derived from plants, animals, and microorganisms. However, a major fraction of enzymes are chiefly derived from microbes due to their ease of growth, nutritional requirements, and low-cost downstream processing. In addition, enzymes with new physical and physiological characteristics like high productivity, specificity, stability at extreme conditions, low cost of production, and tolerance to inhibitors are always the most sought after properties from an industrial standpoint. To meet the increasing demand of robust, high-turnover, economical, and easily available biocatalysts, research is always channelized for novelty in enzyme or its source or for improvement of existing enzymes by engineering at gene and protein levels. The novel actinobacteria and their industrially important enzymes will assist effective productivity and fulfill the requirements of industries.
- extra-cellular enzymes
Among the microorganisms, actinobacteria are of special interest since they are known to produce chemically diverse compounds with a wide range of biological activities. Actinobacteria, the filamentous Gram positive bacteria are primarily saprophytes of the soils, where they contribute notably to the turnover of complex biopolymers such as lignocellulose, hemicellulose, pectin, keratin, and chitin. Undoubtedly, they are also well known as a rich source of antibiotics, enzymes, and other bioactive molecules, and are of considerable importance in pharmaceutical and other industries .
The ever-increasing requirement for enzymatic preparations is being met by such classical sources as animal and higher plant tissues, and that has stimulated the search for similar enzymes from the microbial world. The value of microorganisms, including actinobacteria, in the production of enzymes is enhanced by their relatively high yields, cost-efficiency, and susceptibility to genetic manipulation . At present, enzymes of microbial origin are widely used in food processing, detergent manufacturing, the textile and pharmaceutical industries, medical therapy, bioorganic chemistry, and molecular biology. The wide use of enzymes reflects their characteristic specificity of action as biocatalysts. However, enzymes of identical substrate profile produced by different microorganisms may significantly vary in the optimal conditions of their productivity. For this reason, it is necessary to obtain microorganisms which produce enzymes with required substrate specificity, at particular temperature and pH ranges demanded by the production process. The biochemical heterogeneity, ecological diversity, and exceptional capacity of actinobacteria for secondary metabolites production make them an obvious target for enzymes displaying new activities and/or specificities. For many years, actinobacteria are best known as the source of majority of antibiotics. More recently, they have been found to be a promising source of a wide range of industrially important enzymes. Keeping this in mind and recognizing the significance of actinobacteria, especially
2. Significance of actinobacterial enzymes
Actinobacteria are one of the ubiquitous dominant groups of Gram positive bacteria. Actinobacteria have been commercially exploited for the production of pharmaceuticals, neutraceuticals, enzymes, antitumor agents, enzyme inhibitors, and so forth . These bioactive compounds are of high commercial value, and hence actinobacteria are regularly screened for the production of novel bioactive compounds. A wide array of enzymes applied in biotechnological industries and biomedical fields have been reported from various genera of actinobacteria. Since there is vital information available due to the advent of genome and protein sequencing data, actinobacteria has been continuously screened for the production of proteases, cellulases, chitinases, amylases, xylanases, and other enzymes. The industrial applications of several actinobacterial enzymes are given in Table 1.
|Detergent (laundry and dish wash)||Protease||Protein stain removal|
|Amylase||Starch stain removal|
|Lipase||Lipid stain removal|
|Cellulase||Cleaning, color clarification, anti-redeposition (cotton)|
|Mannanase||Mannanan stain removal (reappearing stains)|
|Starch and fuel||Amylase||Starch liquefaction and saccharification|
|Glucose isomerase||Glucose to fructose conversion|
|Xylanase||Viscosity reduction (fuel and starch)|
|Food (including dairy)||Protease||Milk clotting, infant formulas (low allergenic), flavor|
|Lactase||Lactose removal (milk)|
|Pectin methyl esterase||Firming fruit-based products|
|Transglutaminase||Modify visco-elastic properties|
|Baking||Amylase||Bread softness and volume, flour adjustment dough conditioning|
|Xylanase||Dough stability and conditioning (|
|Lipase||Dough stability and conditioning (|
|Glucose oxidase||Dough strengthening|
|Transglutaminase||Laminated dough strengths|
|Animal feed||Phytase||Phytate digestibility – phosphorus release|
|Amylase||Juice treatment, low calorie beer|
|Acetolactate decarboxylase||Maturation (beer)|
|Laccase||Clarification (juice), flavor (beer), cork stopper treatment|
|Textile||Cellulase||Denim finishing, cotton softening|
|Peroxidase||Excess dye removal|
|Pulp and paper||Lipase||Pitch control, contaminant control|
|Amylase||Starch-coating, de-inking, drainage improvement|
|Cellulase||De-inking, drainage improvement, fiber modification|
|Fats and oils||Lipase||Transesterification|
|Phospholipase||De-gumming, lyso-lecithin production|
|Organic synthesis||Lipase||Resolution of chiral alcohols and amides|
|Acylase||Synthesis of semisynthetic penicillin|
|Nitrilase||Synthesis of enantiopure carboxylic acids|
|Personal care||Amyloglucosidase||Antimicrobial (combined with glucose oxidase)|
|Glucose oxidase||Bleaching, antimicrobial|
|Aminoacylase||Regulation of urea cycle|
3. Types of actinobacterial enzymes
Aminoacylase (N-acylamino-acid amidohydrolase) catalyzes the hydrolysis of acylated D- or L-amino acids to D- or L-amino acids and an appropriate carboxylic acid: N-acetyl-(D) or (L)-amino acid> carboxylic acid+(D)-or (L)-amino acid (Figure 1). Aminoacylases are interesting and ever-increasing enzymes due to the growing demand in the pharmaceutical industry for optically active amino acids. In enzymology, an aminoacylase is an enzyme that catalyzes the following chemical reaction:
This enzyme belonged to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. This enzyme mainly concerns D-amino acids, both natural and synthetic, such as D-phenylglycine and its derivatives which are used for the production of semisynthetic penicillins and cephalosporins. Phenylglycine obtained synthetically as a racemic mixture can be split into enantiomers by chemical or enzymatic reactions. The latter are usually applied because they are simpler and more efficient. Two methods have been proposed for the isolation of pure enantiomers of D-amino acids using enzymatic hydrolysis of racemic mixtures of their N-acetylated derivatives. In the first method, a stereospecific enzymatic hydrolysis of N-acetyl-DL-amino acids has been used to obtain a mixture of D-amino acid and unaffected N-acetyl-L-amino acid which has to be racemized before its reuse in the process, while in the second method enzymatic cleavage of N-acetyl-L-amino acid, a component of the racemic mixture, results in a mixture of L-amino acid and non-hydrolyzed N-acetyl-D-amino acid. D-amino acid is obtained from the latter as a result of chemical deacylation of the N-acetylated derivative. The second method of obtaining D-amino acids is the one applied in practice. D-aminoacylases are uncommon in microorganisms, though Szwajcer
Amylase comprises a group of industrial enzymes having approximately 25% of the global enzyme market. Specifically, an extracellular amylase with the ability to digest raw starch has found important applications in bioconversion of starches and starch-based substrates. The level of alpha amylase activity in various fluids of human body is of clinical importance, e.g., in diabetes, pancreatitis, and cancer research, while plant and microbial alpha amylases are used as industrial enzymes. Starch-degrading amylolytic enzymes are of great significance in biotechnological applications ranging from food, fermentation, and textile to paper industries (Table_1). Although amylases can be derived from several sources, such as plants, animals, and microorganisms, the enzymes from microbial sources are generally used to meet industrial demands and have made significant contribution to the production of foods and beverages in the last three decades. The microbial amylases have almost completely replaced the starch hydrolyzing chemicals in starch processing industry.
Like most microorganisms, actinobacteria can also survive in both mesophilic and thermophilic conditions; they have the ability to degrade starch by hydrolysis . The occurrence of amylases in actinobacteria has been a well-known phenomenon since it was established that several representatives of the genera
|α-amylase||60||7.0||Chao-Hsun and Wen-Hsiung, 2007|
|Cellulase||50||6.5||Hung-Der and Kuo-Shu, 2003|
|Lipase||50||9.0-10.0 (4-10)||Abrami |
|Xylanase||60-80||7.0 (6-8)||McCarthy |
β-N-acetyl-D-glucosaminidase (2-acetamido-2-deoxy-β-D-glucoside) is frequently encountered in microorganisms, higher plants, and mammalian tissues. This enzyme splits hydrolytically chitobiose, N,N'-diacetylchitobiose moieties of asparagines-linked oligosaccharides of various glycoprotein and hydrolyzes N-acetyl-β-D-galactosaminidases, yielding oligosaccharide chains from glycoproteins . Thus, it has been found to be very useful for the structural determination of the carbohydrate moiety of several glycoproteins and for studying their biochemical functions and biosynthesis . Generally, actinobacteria producing enzymes are synthesized at extracellular region including endo-β-N-acetyl-D-glucosaminidase H  and endo-β-N-acetyl-glucosaminidase L  isolated from
3.4. 1, 3-α and 1, 3-β Glucanase
Endo-l, 3-α-D-glucanases (1, 3-α-D-glucan glucanohydrolase) hydrolyzes fragments of polysaccharides that contain consecutive 1, 3-linked α-D-glucosyl residues. Consequently, 1,3- α -D-glucanases are useful in detection of 1,3- α -D-linkages sequences in dextran as well as provide a route for 1,3-α-D-glucans study in fungal cell walls [37; 38]. These enzymes are produced by fungi and bacteria and are quite common among actinobacteria. Therefore, these enzymes may be useful as protective agents for odontological purposes. The presence of mutan-hydrolyzing enzymes was detected in
Cellulose, which forms almost half of the dry weight of the earth’s biomass, is an unbranched polymer consisting of D-glucose units linked by 1,4-β glycosidic bonds. This macromolecule has a complex crystalline structure, is insoluble in water, and is quite resistant to depolymerizing enzymes and chemical reagents. Under natural conditions, cellulose is almost always combined with hemicellulose and lignin , which makes its degradation by microorganisms even more difficult.
Investigations on the mechanism of cellulose degradation and its possible applications have been carried out for many years . Recently, the enzymatic hydrolysis of cellulose for D-glucose production has aroused an ever-increasing interest [48; 49]. Cellulose-degrading enzymes are excreted by microorganisms into the surrounding environment and as with most enzymes-degrading biopolymers they constitute a multicomponent lytic complex that acts synergistically on the cellulose. The cellulolytic system consists of three major components: 1,4-β glucan glucanohydrolase acting as endoglucanase, l,4-β-D-glucan cellobiohydrolase displaying exoglucanase activity, and β-glucosidase, which splits cellobiose. The enzymatic system of cellulases operates synergistically, i.e., endoglucanases make random scissions of the cellulose chain yielding glucose and oligosaccharides; exoglucanases attack the nonreducing end of cellulose forming cellobiose; and finally cellobiases hydrolyze cellobiose to glucose . Members of several mesophilic and thermophilic actinobacteria have been studied for their ability to degrade cellulose.
Proteases, generally classified into exopeptidases (cleave off peptide bonds from the ends of the protein chain) and endopeptidases (cleave peptide bonds within the protein) (Figure 2.), are the major industrial enzymes and fulfill more than 65% of the global market need . These enzymes are extensively used in the food, pharmaceutical, leather, and textile industries [64; 65]. Among the extremophilic sources, thermostable proteases have been reported from certain haloalkaliphilic bacteria and actinobacteria [66; 67]. With the increasing demand of the enzymes, there will be an ever-increasing need for stable biocatalysts capable of withstanding extreme conditions of operation. Proteases generally activate a nucleophile, which will in turn attack the carbon of the peptide bond. The electrons in the carbon-oxygen double bond migrate onto the oxygen as the nucleophile attaches itself. This tetrahedral intermediate is a highly energetic intermediate, and the protease will stabilize this intermediate. The intermediate will then decompose, usually releasing the two peptide fragments.
The ability to produce a variety of proteolytic enzyme is a well-known phenomenon in mesophilic actinobacteria;
Chitin, a polymer occurring in crustaceans, fungi, and insects, is a fibrillar 1,4 linked 2-acetamido-2-deoxy-β-D-glucan with acetyl groups attached to nitrogen to various extents. It is found in three polymeric forms with various degrees of crystallinity. Fully deacetylated chitin is known as chitosane . Enzymatic hydrolysis of chitin, liberating free N-acetyl-D-glucosamine, is caused by the chitinolytic complex which consists of chitinase (polyβ-1,4- (2-acetamido-2-deoxy)-D-glucose glycanohydrolase) and chitobiase (β-N-acetyl-D-glucosaminidase) (Figure 3.). As a result of the action of chitinase complex, chitobiose and chitotrose are released. Chitinases are specific to linear polymers of N-acetylglucosamine, but they do not split chitobiose. They hydrolyze chitin to chitobiose and to a lesser extent to chitotriose .
Chitinolytic complexes commonly occur in bacteria, fungi, and especially in actinobacteria. The chitinase have been isolated from culture filtrates of
Cholesterol esterase, which converts cholesterol esters into free cholesterol, is used in clinical tests for determining the cholesterol level in blood serum . Until now, little is known about the properties of cholesterol esterases. These enzymes differ not only in their optimum pH for production but also in their substrate specificity. For example, cholesterol esterase isolated from
Phospholipases, the enzymes capable of selective cleavage of ester bonds in glycerophosphatides, occur widely in both animal and plant kingdoms. Because of their high specificity, they are used for the analysis of phospholipid components of biological membranes as well as for clinical diagnostic tests. Phospholipases are classified into four groups, A, B, C, and D (Table 3). Serum choline phospholipids are hydrolyzed by phospholipase-D and the amount of liberated choline can be estimated quantitatively. Phospholipase-D from streptomycetes has been found useful for the determination of serum choline-phospholipids and in clinical diagnostic tests [83; 84].
|Phospholipase - A2||7.0||Okawa and Yamaguchi (1976a)|
|Phospholipase - B||9.0||Walker and Walker (1975)|
|Phospholipase - C||7.5||Verma and Khuller (1983)|
|Phospholipase - D||8.0||Imamura and Horiuti (1979)|
Xylan, a hemicellulose, is composed of l,4-β-linked D-xylose units that form a linear backbone to which 4-O-methyl-D-glucuronic acid and L-arabinose are attached as side chains (Figure 4). This polymer, which occurs together with cellulose, is degraded by xylanases. Xylanases can be found in large amounts in both microorganisms as well as several invertebrates . Together with other carbohydrases, xylanases play an important role in the degradation of terrestrial biomass . Like cellulases they occur in microorganisms in the form of extracellular complexes, which consist of endo and exoxylanases that differ in substrate specificity. Xylanases produced by mesophilic actinobacteria belong to the endotype (l,4-β-D-xylan xylanohydrolase). They have been isolated and purified from several species of streptomycetes, such as
N-acetylmuramidase, an enzyme resembling lysozyme in action, cleaves the N-acetyl-muramyl-β,4-N-acetylglucosamine bonds of the polysaccharide chain of peptidoglycan, liberating free-reducing groups of N-acetylmuramic acid. N-acetylmuramidase (mucopeptide N-acetylmuramoyl-hydrolases) belongs to the group of bacteriostatic enzymes comprising glycosidases that hydrolyze peptidoglycan (murein), which is basic component of the bacterial cell wall. Murein, composed of glycan strands consisting of alternating acetylated amino sugars, N-acetylglucosamine and N-acetylmuramic acid linked by β (1-4) glycosidic bonds mutually cross-linked by peptide chains, forms a mono- or multilayer net covered with lipopolysaccharides, phospholipids, and lipoproteins. The peptide moiety of murein is composed of short chains of unbranched aliphatic amino acids and/or amino acids that form stem peptides linked to the carboxyl group of N-acetylmuramic acid and cross-linked by interpeptide bridges . Peptidoglycans, especially available high in Gram-positive bacteria, are highly diversified. The determination of the primary structure of peptidoglycans has revealed differences between the bacteria and it provides significant taxonomic tools . The enzyme was isolated from
Neuraminidase (acylneuraminyl hydrolase) splits 2,3-, 2,6-, and 2,8- and 2,9-glucosidic linkages which join terminal nonreducing N- or O-acetylated neuraminyl residues present in oligosaccharides and glycoprotein. Neuraminidases or sialidases occur widely in bacteria, viruses, animal tissues, and biological fluids . These enzymes, isolated from various sources and differing in their substrate specificity, are applied in a wide area of biological and immunological research, particularly in cell surface and clinical studies [23; 102]. In actinobacteria, neuraminidases have been found in representatives of the genera
3.13. Peptide hydrolase
Proteolytic enzymes of microbial origin were classified by Morihara , on the basis of their catalytic mechanism, into serine, thiol, metallo, and acid proteases according to the general systematic scheme introduced by Hartley . The ability to produce a variety of proteolytic enzymes is a well-known phenomenon in mesophilic actinobacteria . There is also an increasing interest in proteases derived from thermophilic actinobacteria including members of the genera
Pronase like enzymes are produced not only by
The important application of the L-asparaginase enzyme is in the treatment of acute lymphoblastic leukemia, Hodgkin’s disease, acute myelocytic leukemia, acute myelomonocytic leukemia, acute and chronic lymphocytic leukemia, lymphosarcoma treatment, reticulosarbom, and melanosarcoma . L-asparaginase broadly distribute among the plants, animals, and microorganisms. The microbes are a better source of L-asparaginase, because they can be cultured easily and the extraction and purification of enzyme from them is also convenient, facilitating large-scale production . L-asparaginase has been arousing considerable interest as it displays an antineoplastic activity against a variety of murine neoplasms. As an antineoplastic agent, L-asparaginase from
3.15. Penicillin amidase
Penicillin amidase (penicillin amidohydrolase) is an enzyme that hydrolyzes penicillins to 6-aminopenicillanic acid (6-APA) and carboxylic acid. The cleavage of penicillin into 6-APA and side chain is a reaction in which the penicillin nucleus, the basis for the production of semisynthetic penicillins, is obtained. Penicillin amidases in the form of immobilized preparations are applied in the production of 6-APA on an industrial scale . Penicillin acylases are classified into three groups on the basis of their substrate specificity: the first group includes the enzymes that hydrolyze phenoxymethyl-penicillin (penicillin V); the second, those that act on benzylpenicillin (penicillin G); and the enzymes of the third group display specificity with respect to D-a-amino-benzylpenicillin, ampicillin . The penicillin hydrolysis reaction procedes in an alkaline medium and at lower pH values and is reversible. This property was exploited to synthesize semisynthetic penicillins and cephalosporins by the application of penicillin amidase preparations  occur in bacteria and actinobacteria and to a minor extent in yeasts and moulds [129-131]. The majority of those found in actinobacteria such as
Enzymes are considered as a potential biocatalyst for many biological reactions. Particularly, the microbial enzymes have extensive uses in industries and medicines. The microbial enzymes are also more active and stable than plant and animal enzymes. In addition, the microorganisms, particularly actinobacteria, represent an alternative efficient source of enzymes because they can be cultured in large quantities by fermentation and owing to their biochemical diversity and susceptibility to gene manipulation. Industries are looking for new microbial strains in order to produce different enzymes to fulfill the current enzyme requirements. Hence, the actinobacteria as biofactory of potential enzyme as well as secondary metabolites production, fulfill the requirements of several industrial enzymes. In a world with a rapid increasing of population and approaching exhaustion of many natural resources, enzyme technology offers a great potential for many industries to help meet the challenges they will face in the years to come.
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