qPCR Complete Pack List

Phenol monooxygenase (PMO), catalyze the hydroxylation of phenol by incorporating a single oxygen atom from molecular oxygen into the organic substrate, converting phenol into its o-diol derivatives, like catechol.

GP-PAH-RHDs are key enzymes in Gram-positive bacteria that start the degradation of polycyclic aromatic hydrocarbons (PAHs) such as naphthalene, phenanthrene, and benzo[a]pyrene. They serve as functional markers for identifying and studying PAH-degrading bacteria.

Biphenyl dioxygenase (bhpA) is an essential enzyme that initiates the degradation of biphenyl and structurally related compounds such as polychlorinated biphenyls (PCBs). Biphenyl dioxygenase belongs to the family of aromatic ring-hydroxylating dioxygenases (ARHDs), which catalyse the activation of aromatic rings through hydroxylation, enabling further breakdown of these persistent pollutants.

Alkane monooxygenase (AlmA) is an enzyme that catalyzes the initial oxidation of long-chain n-alkanes in bacteria like Acinetobacter and Alcanivorax. This process converts alkanes into primary alcohols, which are then further metabolised into fatty acids, making them available for use as an energy source. AlmA is crucial for the degradation of specific long-chain alkanes (C26-C38), as shown by the inability of bacteria to grow on these substrates when the almA gene is not present.

Biphenyl dioxygenase genes (BphA) are abundant in BTEXN contaminated environment and postively correlated with BTEXN concentrations.

GN-PAH-RHDs are key enzymes in Gram-negative bacteria that start the degradation of polycyclic aromatic hydrocarbons (PAHs) such as naphthalene, phenanthrene, and benzo[a]pyrene. They serve as functional markers for identifying and studying PAH-degrading bacteria.

Toluene monooxygenase (TMO) functions by hydroxylating toluene, using molecular oxygen (O2) and NADH to oxidize it to an alcohol or cresol.

Naphthalene dioxygenase is a multicomponent bacterial enzyme system that catalyzes the initial oxidation of aromatic compounds like naphthalene. Naphthalene dioxygenase (NDO) is a multi-component bacterial enzyme that catalyzes the conversion of naphthalene and other aromatic compounds into cis-dihydrodiols by adding both atoms of molecular oxygen to the substrate. This reaction is the first step in the metabolic degradation of naphthalene by bacterian.

Encodes alkane 1-monooxygenases, which initiate hydroxylation of medium-chain alkanes (C6-C22). These genes are widespread in Pseudomonas, Rhodococcus and other aerobes.

Toluene dioxygenase is an enzyme system, notably found in Pseudomonas putida, that converts toluene and other aromatic hydrocarbons to cis-dihydrodiols by adding two atoms of oxygen to the aromatic ring.

Catechol 2,3-dioxygenases are involved in the biodegradation of benzene, toluene, xylenes, phenol, and naphthalene through at least one catabolic pathway, and therefore play a key role in the metabolism of these compounds

Benzylsuccinate synthase (BSS) is the key enzyme of anaerobic toluene degradation and potentially other alkyl-substituted hydrocarbons such as Xylene.

Alkylsuccinate synthase is a complex enzyme that catalyses the initial step of anaerobic alkane degradation, where it adds an alkane to the double bond of fumarate. This process yields a (1-methylalkyl)succinate, which can then be further metabolised under anaerobic conditions by bacteria or methanogens. These enzymes, which use a glycyl radical, are found in various microorganisms, including nitrate- and sulfate-reducing bacteria, and play a crucial role in bioremediation of petroleum hydrocarbons.

Anaerobic benzene carboxylase (AbcAD) is a crucial enzyme for anaerobic aromatic hydrocarbon biodegradation, as its function indicates that an aromatic ring has been cleaved, a key step in the overall degradation process

Bacteria related to the Peptococcaceae have been shown to play an important role in anaerobic benzene degradation under denitrifying, iron-reducing, and sulfate-reducing conditions.

Ring-cleaving hydrolase (bamA) is a crucial enzyme for anaerobic aromatic hydrocarbon biodegradation, as its function indicates that an aromatic ring has been cleaved, a key step in the overall degradation process

Bioremediation processes (particularly in anaerobic environments) generally initiate the break down aromatic compounds by first converting them to benzoyl-CoA. Benzoyl-CoA reductase is the enzyme that reduces the aromatic ring of benzoyl-CoA, breaking its resonance and making it susceptible to further breakdown.

Nitrate reductase (napA) is a key denitrifying enzyme produced by heterotrophic denitrifying bacteria that catalyses the reduction of nitrate to nitrite. The napA gene serves as a reliable molecular target for quantifying the abundance of functional denitrifiers in environmental samples, helping assess the capacity and activity of denitrifying microbial communities relevant to bioremediation

Ammonia monooxygenase (AMO) enzymes (particularly the amoA subunit) are among the most reliable molecular markers for identifying and quantifying ammonia-oxidising archaea (AOA) in environmental samples. Ammonia oxidation is the first and rate-limiting step in nitrification, where AOB convert ammonia (NH3) into nitrite (NO2-) via hydroxylamine. This process is catalysed by ammonia monooxygenase (AMO). Hence, AOB quantification is a robust indicator of nitrification potential rather than general microbial presence. Note, the same amoA subunit is targeted to quantify Bacterial ammonia monooxygenase (AOB).

Ammonia monooxygenase (AMO) enzymes (particularly the amoA subunit) are among the most reliable molecular markers for identifying and quantifying ammonia-oxidising bacteria (AOB) in environmental samples. Ammonia oxidation is the first and rate-limiting step in nitrification, where AOB convert ammonia (NH3) into nitrite (NO2-) via hydroxylamine. This process is catalyzed by ammonia monooxygenase (AMO). Hence, AOB quantification is a robust indicator of nitrification potential rather than general microbial presence. Note, the same amoA subunit is targeted to quantify Archael ammonia monooxygenase (AOA).

bvcA is a functional gene of Dehalococcoides mccartyi strains with enzymes that catalyse reductive dechlorination of DCE and VC to ethene.  Dehalococcoides mccartyi in Micronovo's AusPCE culture mix carry the bvcA functional gene, enabling complete dechlorination of DCE and VC, ensuring bioremediation of PCE or TCE doesn't stall at DCE or VC.

Chloroform reductase (tmrA) gene copies for reductive dechlorination of chloroform to dichloromethane (DCM) and then acetate.

Chloroform reductase, encoded by the tmrA gene, is a specialized enzyme found in certain organohalide-respiring bacteria. It catalyses the reductive dechlorination of chloroform to dichloromethane (DCM), followed by further conversion to acetate under anaerobic conditions. Quantifying tmrA gene copies in environmental samples enables sensitive monitoring of key chloroform-degrading bacteria, helping assess bioremediation progress and optimize conditions for complete detoxification of chloroform and its breakdown products.

Micronovo's high performance AusCF Chloroform degrading culture utilises Chloroform reductase.

Micronovo’s AusCF high performance organo-halide respiring bacteria culture mix contains  Dehalobacter UNSWDHB that carry the tmrA gene. 

tceA is a functional gene carried by organohalide respiring bacteria with enzymes that catalyse reductive dechlorination of TCE to VC. Dehalococcoides mccartyi in Micronovo's AusPCE culture mix carry the tceA functional gene.

vcrA is a functional gene of Dehalococcoides mccartyi strains with enzymes that catalyses reductive dechlorination of VC to ethene.

Dehalococcoides mccartyi in Micronovo's AusPCE culture mix carry the vcrA functional gene, enabling complete dechlorination of VC and ensuring bioremediation of PCE or TCE doesn't stall at VC (a contaminant more toxic than the initial PCE and TCE contaminants).

1,2-dichloroethane reductive dehalogenase is the key enzyme for reductive dechlorination of 1,2-dichloroethane to ethene. Note, 1,2-dichloroethane is also know as 1,2-DCA, DCA and ethylene dichloride or EDC in Australia.

Reductive Dehalogenase A (RdhA) enzyme, is the catalytic subunit of reductive dehalogenases (RDases) responsible for PCB reductive dechlorination. These enzymes use a cobalamin (vitamin B12) cofactor and iron-sulfur clusters to remove chlorine atoms from highly chlorinated PCBs, converting them into less chlorinated forms under anaerobic conditions. AusPCE culture mix expresses RdhA to dechlorinate PCBs under anaerobic conditions.