Products obtained from the biotransformation of artemisinin (
Abstract
Microbial-catalyzed biotransformations have considerable potential for the generation of an enormous variety of structurally diversified organic compounds, especially natural products with complex structures like triterpenoids, flavonoids, steroids, steroidal saponins, and sesquiterpenoids. They offer efficient and economical ways to produce semisynthetic analogues and novel lead molecules. Microorganisms such as bacteria and fungi could catalyze chemo-, regio-, and stereospecific hydroxylations of diverse substrates that are extremely difficult to produce by chemical routes. During recent years, considerable research has been performed on the microbial transformation of bioactive compounds, in order to obtain biologically active molecules with diverse structural features. In green chemistry, biotransformations are an important chemical methodology toward more sustainable industrial processes.
Keywords
- microorganisms
- fungi
- bacteria
- microbial transformation
- natural products
- enzymes
1. Introduction
Microbial transformation is regarded as an enzymatic reaction by using the metabolic activities of microorganisms to modify the chemical structures of bioactive substrates for finding the new chemical derivatives with the potent bioactivities and physical-chemical characteristics. It has a number of advantages over chemical synthesis such as higher
The use of microorganisms may be a highly efficient method of production of these compounds. The reactions involved in biotransformation of organic compounds by whole cells of various microorganisms include oxidation, reduction, hydroxylation, esterification, methylation, demethylation, isomerization, hydrolysis, glycosylation, and hydrogenation [4, 5].
Biotransformation may be carried out with isolated enzyme systems or with intact organism. Although isolated enzyme systems may be more specific and efficient for certain biotransformation, these reactions may involve isolating the enzyme system, and, for some classes of enzyme-catalyzed reaction, a recycling sequence may be required to regenerate the enzyme [6].
Fungi are playing a prominent role in the catalysis of organic compounds and in the production of commercially and industrially important compounds, because of their ability to catalyze novel reactions [7]. Fungi are commonly used in the industry for production of fermented beverages, foods, physiologically active substances, solvents, organic acids, polysaccharides, antibiotics, etc. Of the zygomycota,
The use of the microbial model offers a number of advantages over the use of animals in metabolism studies, mainly: (1) simple, easy, and can be prepared at low cost; (2) screening for a large number of strains is a simple repetitive process; (3) the large number of metabolites formed allows easier detection, isolation, and structural identification; (4) newer metabolites can be isolated; (5) utilized for synthetic reactions involving many steps; (6) useful in cases where
The objective of this review is to highlight the importance of microorganisms or enzymes isolated from them in the biotransformation process of natural products or xenobiotic compounds, according to green chemistry or white biotechnology.
2. Microbiological transformations of some selected natural products with different microorganisms
2.1 Sesquiterpene lactone
Artemisinin (
Microorganism | Products | Action | Reference |
---|---|---|---|
3β-hydroxy-4,12-epoxy-1-deoxyartemisinin Artemisinin G 3,13-epoxyartemisinin 4α-hydroxy-1-deoxyartemisinin | Epoxidation, hydroxylation C-3β site Endoperoxide function reduction Breakdown of heterocyclic rings Epoxidation C-3 and C-13 Hydroxylation C-4, endoperoxide function reduction | [10] | |
14-hydroxyartemisinin Artemisinin G 4α-hydroxydeoxyartemisinin Deoxyartemisinin | Hydroxylation of C-14 site Breakdown of heterocyclic rings Hydroxylation of C-4α site Endoperoxide function reduction | [11, 12] | |
7β-hydroxy-9α-artemisinin 4α-hydroxy-1-deoxoartemisinin 7β-hydroxyartemisinin 6β-hydroxyartemisinin 7α-hydroxyartemisinin 6β,7α-dihydroxyartemisinin | Hydroxylation C-7β site Epimerization C-9 Hydroxylation C-4α site Hydroxylation C-7β site Hydroxylation C-6β site Hydroxylation C-7α site Hydroxylation C-6β and C-7α sites | [13, 14] | |
9β-acetoxyartimisinin 9α-hydroxyartemisinin | Acetylation of C-9β site Hydroxylation of C-9α site | [15] | |
Deoxyartemisinin 1α-hydroxyartemisinin 10β-hydroxyartemisinin | Endoperoxide function reduction Hydroxylation of C-1 site | [16] | |
9-artemisitone 9α-hydroxyartemisinin 9β-hydroxyartemisinin 3α-hydroxyartemisinin | Oxidation of C-9 site Hydroxylation of C-9α site Hydroxylation of C-9β site Hydroxylation of C-3α site | [17] | |
Deoxyartemisinin | Endoperoxide function reduction | [11] |
2.2 Triterpene
Ursolic acid (3β-hydroxy-urs-12-en-28-oic acid, UA,
Microbial transformation of ursolic acid (
Biotransformation of UA by
The endophytic fungi
Microbial transformation of ursolic acid by
The gum resin
18β-glycyrrhetinic acid (
Ginsenoside Rb1 (
Triterpenoid | Microorganism | Reaction | Reference |
---|---|---|---|
Ginsenoside Rb1 ( | Deglycosylation at the C-3 and C-20 sites | [30] | |
Deglycosylation at the C-3 and C-20 sites | [30] | ||
Deglycosylation at the C-3 and C-20 sites | [30] | ||
Deglycosylation at the C-3 and C-20 sites | [31] | ||
Deglycosylation at the C-3 site | [32] | ||
Deglycosylation at the C-20 site, hydration Δ24(25) Formation of tertiary alcohol | [33] | ||
Deglycosylation at the C-3 and C-20 sites | [33] | ||
Oleanolic acid ( | Diverse hydroxylation at the C-1β, C-7β, C-13β sites | [4] | |
Dehydrogenation C-13 and C-18. oleanderolide formation | [4] | ||
Hydroxylation on C-21. Oxidation of the hydroxyl group in C-3 | [4] | ||
Hydroxylation in C-6β | [4] | ||
Hydroxylation in C-11α | [4] | ||
Oxidative ring A cleavage, hydroxylation at the C-21β sites | [34] | ||
Methyl esterification of the C-28 carboxyl group | [4] | ||
Hydroxylation of the C-7β, C-15α and C-30 sites Deshidrogenation Δ9(11) | [35] | ||
Betulinic acid ( | Dehydrogenation of the C-3 secondary alcohol group, hydroxylation at the C-6α and C-7β sites | [36] | |
Dehydrogenation of the C-3 secondary alcohol group, hydroxylation at the C-7β and C-15α sites | [37] | ||
Hydroxylation at the C-1β and C-7β sites | [4] | ||
Introduction of a β-glucopyranosyl at the C-28 carboxylic acid group | [38] | ||
Betulonic acid ( | Ketone α-hydroxylation at the C-2 site | [37] | |
Oxidative ring A cleavage, hydroxylation, decarboxylation | [39] | ||
Hydroxylations at the C-7β and (or) C-15β sites | [4, 40] |
Biotransformation of oleanolic acid (
A C-3 oxidized derivative of oleanolic acid
2.3 Steroidal saponins
Diosgenin [(25R)-spirost-5-en-3β-ol,
Fungi | Diosgenona ( | AD ( | ADD ( | Progesterone ( | 16-AD |
---|---|---|---|---|---|
++ | ++ | ++ | ++ | ||
++ | ++ | ||||
++ | ++ | ||||
++ | ++ | ++ |
Microbial transformation of
2.4 Steroids
Microorganisms are able to hydroxylate steroids in different positions C-1 to C-21. These represent the most widespread type of steroid bioconversion carried out by fungi. The commercialized microbial process in the steroid field was in the production of 11α-hydroxyprogesterone. This process was realized for the first time by Peterson and Murray (1952), which patented this process of 11α-hydroxylation of progesterone (
Industry, which is carried by different microorganisms, such as different species of
Microbial transformation of (20S)-20-hydroxymethylpregna-1,4-dien-3-one (
The 11α-, 11β-, 15α, and 16α-hydroxylations are currently established processes in the steroid industry mainly for the production of adrenal cortex hormones and their analogues. 11α-, 11β-, and 16α-hydroxylations are usually performed using
Hydroxylation sites | Microorganisms | Applications | Reference |
---|---|---|---|
C-7α | Production of bile acids and drugs for neuropsychiatry and immunology | [55, 56] | |
C-7β | Obtaining drugs for prostate cancer | [56, 57] | |
11β | Obtaining anti-inflammatory drugs, like hydrocortisone, prednisone acetate, dexamethasone | [56, 57, 58, 59, 60] | |
11α | Obtaining of anti-inflammatory, immunosuppressive, anti-allergic drugs, and production of contraceptive drugs | [56, 61] | |
14α | [56] | ||
15β | [56, 62] | ||
16α | [63, 64] |
Boldenone (
Fungi | Yeast | Bacteria | |
---|---|---|---|
The oxidation of 17β-hydroxyl group was observed along with hydroxylation of steroids at C5 (
2.5 Diterpene
Sclareolide (
2.6 Flavonoids
As most important phytochemicals in food, the dietary flavonoids exert a wide range of benefits for human health. Recent researches have explored diverse biological and pharmacological activities of natural flavonoids—antioxidant activity, anti-inflammatory activity, anti-Alzheimer’s disease, antibacterial activity, antifungal activity, anti-HIV activity, anticoagulant activity, antileishmanial activity, and anti-obesity activity [87, 88, 89, 90, 91]. Microbial biotransformation strategies for production of flavonoids have attracted considerable interest because they allow yielding novel flavonoids, which do not exist in nature.
The main reactions during microbial biotransformation are hydroxylation, dehydroxylation, O-methylation, O-demethylation, glycosylation, deglycosylation, dehydrogenation, hydrogenation, C ring cleavage of the benzo-γ-pyrone system, cyclization, and carbonyl reduction.
The microorganisms tend to hydroxylate flavanones at the C-5, 6, and 4′ positions; however, for prenylated flavanones, dihydroxylation often takes place on the Δ4(5) double bond on the prenyl group (the side chain of A ring), although cyclization of the prenyl group to dihydrofurane derivatives is rather common biotransformation pathway of prenylated flavonoids. Prenylated flavanones are a unique class of naturally occurring flavonoids characterized by the presence of a prenylated side chain (prenyl, geranyl) in the flavonoid skeleton [95]. The prenyl chain generally refers to the 3,3-dimethylallyl substituent (3,3-DMA), geranyl and lavandulyl. It is proposed that the prenyl-moiety makes the backbone compound more lipophilic, which leads to its high affinity with cell membranes. The prenylation brings the flavonoids with enhancement of antibacterial, anti-inflammatory, antioxidant, cytotoxicity, larvicidal, as well as estrogenic activities. Figure 16 demonstrated the microbial biotransformation of kurarinone (
Incubation of
Regioselective glycosylation of biologically active flavonoid aglycones catalyzed by microorganisms is an interesting and desired reaction, which significantly increases the water solubility of the compound and, therefore, may improve bioavailability of flavonoids.
Bavachinin (
The biotransformation of xanthohumol (
2″-(2″-hydroxyisopropyl)-dihydrofurano-[4″,5″:3′,4′]-4,2′-dihydroxy-6′-methoxychalcone (
Incubation of xanthohumol (
2.7 Enzymes isolated from microorganisms and their application
Enzymes are the most proficient catalysts, offering much more competitive processes than chemical catalysts. A number of enzyme-based processes have been commercialized for producing several valuable products. During the 1980s and 1990s, engineering of enzymes based on structural information allowed extension of their substrate ranges, enabling the synthesis of unusual intermediates. Accordingly, the use of enzymes has been expanded to the manufacture of pharmaceutical intermediates and fine chemicals [110]. Microorganisms and enzymes (biocatalysts) are highly enantio-, chemo-, and regioselective in a wide range of reaction conditions. Selectivity is extremely desirable in the synthesis of different synthesis products, since it offers advantages such as minimizing the side reactions that do not require protection and deprotection steps, which allows for shorter synthesis. Biocatalysis provides a technology that is environmentally safer, and it effectively reduces the level of waste and even eliminates the waste generation rather than remediation and disposal of wastes at the end of the process. In addition to, biocatalysts have many attractive features in the context of green chemistry and sustainable development. Various enzymes used in different industrial processes have been described in the literature. Table 6 indicates some enzymes, their source, and some applications [111, 112, 113].
Microbial enzymes | Microorganism | Application |
---|---|---|
α-Amylase | Baking, brewing, starch liquefaction Clarification of fruit juice Textile industry Paper industry | |
Glucoamylase | Beer production High glucose and high fructose syrups | |
Proteases | ||
Lactase (β-galactosidase) | Lactose intolerance reduction in people Prebiotic food ingredients | |
Lipase | Cheese flavor development Textile indutry Medicinal applications Use in cosmetics Use as biosensors Use in biodegradation | |
Phospholipases | Cheese flavor development | |
Esterases | Enhancement of flavor and fragrance in fruit juice | |
Xylanases | Clarification of fruit juice Beer quality improvement | |
Glucose oxidase | Food shelf life important Food flavor improvement | |
Laccase | Polyphenol removal from wine baking | |
Pectinases | Clarification of fruit juice | |
Catalase | Food preservation Removal of H2O2 from milk prior to cheese production | |
Peroxidase | Development of flavor, color and nutritional quality of food |
2.8 Extremophiles
A very interesting research area in biology and biotechnology is the of extremophile microorganisms. Extremophiles can be divided into group according to (i) temperature tolerance, (ii) salt concentration, (iii) pH range, or (iv) pressure conditions. Enzymes from extremophilic microorganisms offer versatile tools for sustainable developments in a variety of industrial applications as they show important environmental benefits due to their biodegradability, specific stability under extreme conditions, improved use of raw materials, and decreased amount of waste products. Although major advances have been made in the last decade, our knowledge of the physiology, metabolism, enzymology, and genetics of this fascinating group of extremophilic microorganisms and their related enzymes is still limited [114, 115, 116].
The outstanding properties of thermozymes are suited to industries that employ elevated temperatures, such as the pulp and paper, food, brewing, and feed processing industries. Thermophiles are often highly resistant to harsh conditions such as chemical denaturing agents, wide pH ranges, and/or nonaqueous solvents. Examples of such enzymes are cellulases, xylanases, pectinases, chitinases, amylases, pullulanases, proteases, lipases, glucose isomerases, alcohol dehydrogenases, and esterases. Thermophilic enzymes have played important roles not only at the industrial level but also in pharmaceutical applications requiring use of specific aldolases for the synthesis of enantiopure compounds (Table 7) [118].
Source | Enzyme | Activity | Bioprocess/industry | Reference |
---|---|---|---|---|
Aldolase | Stereoselective C-C bond formation | Pharmaceutical industry | [117] | |
Hydrogenase | Final stage of glucose oxidation by oxidative pentose phosphate cycle | Enhanced production of biohydrogen | [119] | |
Carboxylesterase | Carboxyl ester hydrolysis | Agriculture, food, and pharmaceutical industries | [120] | |
Acidic thermostable lipase | Degradation of palm oil | Treatment of palm oil-containing wastewater | [121] | |
Lipase | Hydrolysis of diver’s lipid substrates | Biofuel, cosmetics, or perfume production, leather and pulp industries | [122] | |
Microbial community from solid-state fermentation reactor | Protease | Degradation of hair waste from tannery | Leather industry | [123] |
Chitinase | Hydrolysis of β-(1, 4)-glycosidic bonds in chitin | Biomedical, pharmaceutical, food, and environmental | [124] | |
Endoxylanase | β-(1,4)-xylan cleavage | Biofuel production from lignocellulose | [125] | |
Pullulanase | Hydrolysis of α-(1, 6)-glucosidic linkages | Biofuel production | [126] |
3. Conclusion
Due to microorganisms’ abundant multienzyme systems, microbial transformation possesses advantages against chemosynthesis of environmental friendliness, mild reaction conditions, and high
The hydrolytic and reductive capabilities of microorganisms have been known and are currently used in preparative and industrial reactions. Various classes of bioactive organic compounds have been subjected to enzymatic transformation to obtain more active and less toxic substances or to elucidate their metabolic pathways.
For example, biotransformation-derived steroids are used for a wide range of pharmacotherapeutic purposes, such as anti-inflammatory, immunosuppressive, progestational, diuretic, anabolic, as neurosteroids, and as contraceptive. Researchers continue to discover more useful steroid compounds and to isolate microorganisms that can perform the structural transformations desired. New technologies such as genomics, metanogenomics, gene shuffling, and DNA evolution provide valuable tools for improving or adapting enzyme properties to the desired requirements.
An alternative may be extremophilic microorganisms such as biocatalysts for countless future industrial applications that are more environmentally friendly.
Acknowledgments
The authors thank Carrera de Biología, FES-Zaragoza, UNAM, Al Departamento de Química Orgánica, FES-Cuautitlán, UNAM.
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