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BIOTECHNOLOGY - MICR 421


Ch 12. Synthesis of Commercial Products by Recombinant Microorganisms

Restriction Endonucleases

Vitamins and Amino Acids

Dyes

Antibiotics

Biopolymers



Production of Restriction Endonucleases

Figs. 12.1, 12.2, 12.3

Widely used for recombinant DNA technology

Several hundred are known from a variety of different bacterial species
(Components of the restriction-modification system)

Aerobes, anaerobes, phototrophs, thermophiles

Each has different growth requirements

Commercial production of many enzymes by one organism (recombinant E. coli) allows fermentation conditions to be standardized

Growth media composition and pH

Temperature and aeration

Fermentor design

Clone both genes of RM system (restriction enzyme and methylase)

Methylase protects E. coli host's DNA from cleavage by the restriction enzyme

Methylase gene should be expressed before the restriction enzyme

The restriction enzyme should have a leader peptide so that it will be transported from the cytoplasm to the periplasm

This separates the enzyme from the host's chromosome to further protect it from being cleaved


Cloning and Commercial Production of Restriction Enzymes


Target genes encode both th methylase and the restriction enzyme

I. Create genomic DNA library

1. Digest genomic DNA of organism that produces the desired restriction enzyme

2. Insert into cloning vector

3. Transform E. coli strain that doesn't produce its own restriction enzyme

 

II. Screen library

4. Infect libary w/ bacteriophage l

5. Isolate colonies

-Cells w/ cloned restriction enzyme gene are resistant to lysis by l

-Screen for expression of modification enzyme

 

III. Transfer genes to expression vector for large-scale commercial production


Commercial Production of Indigo from Tryptophan by Recombinant E. coli

See Figs. 12.8 aand 12.9

Large market for indigo as a dye for blue jeans

Chemical synthesis produces toxic wastes

 

nahA genes of Pseudomonas encodes naphthalene dioxygenase

Cloning of nahA and expression in E. coli results in production of indigo

1. E. coli tryptophanase converts trp to indole

2. Naphthalene dioxygenase transforms indole to an unstable intermediate

(indole and naphthalene have similar chemical structures)

3. Intermediate dehydrates, producing indoxyl

4. Indoxyl oxidizes, producing indigo

 

Produces fewer toxic wastes than chemical synthesis

Not yet economically competitive with chemical process, however


Production of Amino Acids

800,000 tons produced/year worth $5 billion

See Table 12.1

Sources

1. Hydrolysis of proteins

2. Microbial fermentation

Mainly by nonrecombinant Gram positive bacteria

Ex.

Corynebacterium glutamicum

Brevibacterium spp.


Increasing Tryptophan Production

Fig. 12.10

Corynebacterium glutamicum

Traditional industrial bacterium for production of amino acids by fermentation

Rate-limiting step of Trp biosynthesis is catalyzed by antharnilate synthetase

trpE encodes anthranilate synthetase

Gene dosage of trpE was increased in C. glutamicum

1. C. glutamicum DNA library was created using C. glutamicum-E.
coli
shuttle vector

2. Library was screend by complementation of a C. glutamicum
mutant that needed anthranilic acid for growth

o Suggests that vector contains trpE

3. Vector transferred to C. glutamicum for expression


Eosinophilia Myalgia Syndrome

1989 Eosinophilia myalgia epidemic in U.S.

1500 cases --28 deaths

high blood eosinophil counts

muscle pain

 

Associated with ingestion of large amounts of trp as dietary supplement

Trp manufacturer traced to Showa Denko KK of Japan

Changed fermentation process in 1988

1. Wild type => genetically engineered strain

-overproduced phosphoribosylpyrophosphate

-a trp precursor, increased trp biosynthesis

 

2. Product purification (downstream processing)

-reduced amount of activated charcoal

 

Several byproducts were produced which weren't removed by purification and contaminated product

Ex. 1,1'-ethylidene-bis[L-tryptophan] which is converted to 1,2,3,4-tetrahydro-b-carboline 3-carboxylic acid by the acidic pH of the stomach

May have triggered an autoimmune reaction


Antibiotics

  • 100,000 tons produced/year. $5,000,000,000
  • By mid-1990's over 6,000 described
  • Only 1-2% are useful and commercialized

    High costs of development and clinical testing

    Many have toxic side-effects

    To treat infections by resistant strains

    None are known for some pathogens

    1. Modify existing antibiotics

    Reduce side effects

    Broaden spectrum of activity

    Increase stability

    2. Engineer producer strains with increased yields

    3. Lower production costs

     

    Cloning Genes Encoding Enzymes of Antibiotic Biosynthetic Pathways

    -Biosynthesis may involve 10-30 different enzyme-catalyzed reactions with as many genes

    -May be close to each other on chromosome, or

    -May be scattered around the chromosome

    One approach

    1. Create DNA library using wild-type antibiotic-producing organism

    2. Transform mutants of the same organism that have defects in antibiotic biosynthetic pathway

    3. Screen colonies for complementation of the mutations by cloned genes that reestablish the ability to synthesize the antibiotic

    4. Screen for additional genes of the pathway

    Use DNA isolated from the initial positive clones and to synthesize labeled DNA probes

    -can use random primer method (Ch. 4) or

    -sequence cloned DNA and design complementray probes that will hybridize to 5' and 3' ends of the cloned DNA

    Rescreen library for colonies that hybridize to labeled probes

    Positive colonies may contain cloned genes encoding enzymes that catalyze additional steps of biosynthetic pathway if the genes are located nearby (upstream or downstream) on the chromosome

    (May require several rounds of probe design and screening to get all genes for a complete pathway)

     

    To construct a recombinant strain with increased antibiotic production:

    Assemble all genes on one vector and optimize expression to increase amount of antibiotic produced, or

    Overexpress cloned genes for the enzymes that encode rate-limiting or slow steps of the pathway

     

    Engineering Antibiotics with Altered Chemical Structures

    May give antibiotic new or improved properties

    Genes encoding enzymes for biosynthetic pathways of two related antibiotics can be combined in one organism

    Intermediate products of one pathway may be transformed by enzymes of the introduced pathway, resulting in altered antibiotic stuctures

    Exs. (See Fig. 12.17)

    All biosynthetic genes were cloned and inserted into plasmids pIJ2315 and pIJ2303

    Transformed with pIJ2315

    -Produced Mederrhodine A, new antibiotic

    Transformed with pIJ2303

    Produced Dihydrogranatirhodine, new antibiotic


    Production of Industrial Polymers

    Ex. Xanthum gum

    High molecular weight biopolymer (Fig. 12.24)

    Synthesized by Xanthomonas campestris

    Most important bacterial polymer used by industry

    High viscosity, stable to heat and pH extremes

    Many uses:

    Thickener of processed foods, paints and well drilling mud

     

    Xanthan Gum from Whey Waste

    Whey: Waste product of cheese manufacturing

    Disposal is a problem and costly

    Contains high conc. of lactose, ~3.5-4%

     

    Xanthomonas campestris grows on glucose but not lactose

    1. lacZY genes cloned from E. coli (Fig. 12.25)

    lacZ encodes b-galactosidase

    lactose --> glucose + galactose

    lacY encodes lactose permease

    transports lactose into cell

     

    2. Inserted into broad host range plasmid with a constitutive promoter from X. campestris bacteriophage

    Introduced into X. campestris

    Grows on lactose present in whey and produces xanthan gum (Table 12.5)

    Former waste product converted to marketable product

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