Acetic acid bacteria (AAB) are a group of Gram-negative bacteria which oxidize sugars or ethanol and produce acetic acid during fermentation. The acetic acid bacteria consist of 10 genera in the family Acetobacteraceae. Several species of acetic acid bacteria are used in industry for production of certain foods and chemicals.
Mother of vinegar is a biofilm composed of a form of cellulose, yeast, and bacteria that sometimes develops on fermenting alcoholic liquids during the process that turns alcohol into acetic acid with the help of oxygen from the air and acetic acid bacteria (AAB). It is similar to the symbiotic culture of bacteria and yeast (SCOBY) mostly known from production of kombucha, but develops to a much lesser extent due to lesser availability of yeast, which is often no longer present in wine/cider at this stage, and a different population of bacteria. Mother of vinegar is often added to wine, cider, or other alcoholic liquids to produce vinegar at home, although only the bacteria is required, but historically has also been used in large scale production.
Pyrroloquinoline quinone (PQQ), also called methoxatin, is a redox cofactor and antioxidant. Produced by bacteria, it is found in soil and foods such as kiwifruit, as well as human breast milk. Enzymes using PQQ as a redox cofactor are called quinoproteins and play a variety of redox roles. Quinoprotein glucose dehydrogenase is used as a glucose sensor in bacteria. PQQ stimulates growth in bacteria. Eukaryote targets, including mammalian lactate dehydrogenase, are of more interest to health. It is suggested that PQQ taken as a dietary supplement could promote mitochondrial biogenesis via this pathway as well as PGC-1α.
Ethanol, an alcohol found in nature and in alcoholic drinks, is metabolized through a complex catabolic metabolic pathway. In humans, several enzymes are involved in processing ethanol first into acetaldehyde and further into acetic acid and acetyl-CoA. Once acetyl-CoA is formed, it becomes a substrate for the citric acid cycle ultimately producing cellular energy and releasing water and carbon dioxide. Due to differences in enzyme presence and availability, human adults and fetuses process ethanol through different pathways. Gene variation in these enzymes can lead to variation in catalytic efficiency between individuals. The liver is the major organ that metabolizes ethanol due to its high concentration of these enzymes.
Aldehyde dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the ALDH2 gene located on chromosome 12. This protein belongs to the aldehyde dehydrogenase family of enzymes. Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. Two major liver isoforms of aldehyde dehydrogenase, cytosolic and mitochondrial, can be distinguished by their electrophoretic mobilities, kinetic properties, and subcellular localizations.
In enzymology, a fructose 5-dehydrogenase (NADP+) (EC 1.1.1.124) is an enzyme that catalyzes the chemical reaction
In enzymology, a gluconate 5-dehydrogenase (EC 1.1.1.69) is an enzyme that catalyzes the chemical reaction
In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction
In enzymology, a choline dehydrogenase is an enzyme that catalyzes the chemical reaction
In enzymology, a glycerol dehydrogenase (acceptor) (EC 1.1.99.22) is an enzyme that catalyzes the chemical reaction
In enzymology, a quinoprotein glucose dehydrogenase is an enzyme that catalyzes the chemical reaction
In enzymology, an aldehyde dehydrogenase (NADP+) (EC 1.2.1.4) is an enzyme that catalyzes the chemical reaction
In enzymology, an aldehyde dehydrogenase (pyrroloquinoline-quinone) (EC 1.2.99.3) is an enzyme that catalyzes the chemical reaction
Alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase) is an enzyme with systematic name alcohol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction
Cyclic alcohol dehydrogenase (quinone) (EC 1.1.5.7, cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name cyclic alcohol:quinone oxidoreductase. This enzyme catalyses the following chemical reaction
Quinate dehydrogenase (quinone) (EC 1.1.5.8, NAD(P)+-independent quinate dehydrogenase, quinate:pyrroloquinoline-quinone 5-oxidoreductase) is an enzyme with systematic name quinate:quinol 3-oxidoreductase. This enzyme catalyses the following chemical reaction
Alcohol dehydrogenase (azurin) (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB) is an enzyme with systematic name alcohol:azurin oxidoreductase. This enzyme catalyses the following chemical reaction
Soluble quinoprotein glucose dehydrogenase is an enzyme with systematic name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction
Acetobacter aceti is a Gram-negative bacterium that moves using its peritrichous flagella. Louis Pasteur proved it to be the cause of conversion of ethanol to acetic acid in 1864. It is a benign microorganism which is present everywhere in the environment, existing in alcoholic ecological niches which include flowers, fruits, and honey bees, as well as in water and soil. It lives wherever sugar fermentation occurs. It grows best in temperatures that range from 25 to 30 degrees Celsius and in pH that ranges from 5.4 to 6.3. For a long time it has been used in the fermentation industry to produce acetic acid from alcohol. Acetobacter aceti is an obligate aerobe, which means that it requires oxygen to grow.
Asaia bogorensis is a species of acetic acid bacterium. It is Gram-negative, aerobic, rod-shaped and peritrichously flagellated. It was first isolated from specimens of Bauhinia purpurea and Plumbago auriculata. Its type strain is 71T. it is potentially pathogenic.
