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Aspergillus niger is a mold classified within the Nigri section of the Aspergillus genus. The Aspergillus genus consists of common molds found throughout the environment within soil and water, on vegetation, in fecal matter, on decomposing matter, and suspended in the air. Species within this genus often grow quickly and can sporulate within a few days of germination. A combination of characteristics unique to A. niger makes the microbe invaluable to the production of many acids, proteins and bioactive compounds. Characteristics including extensive metabolic diversity, high production yield, secretion capability, and the ability to conduct post-translational modifications are responsible for A. niger's robust production of secondary metabolites. A. niger's capability to withstand extremely acidic conditions makes it especially important to the industrial production of citric acid.
Cellulase is any of several enzymes produced chiefly by fungi, bacteria, and protozoans that catalyze cellulolysis, the decomposition of cellulose and of some related polysaccharides:
Endo-1,4-β-xylanase is any of a class of enzymes that degrade the linear polysaccharide xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls:
Aspergillus oryzae, also known as kōji mold, is a filamentous fungus used in East Asia to saccharify rice, sweet potato, and barley in the making of alcoholic beverages such as sake and shōchū, and also to ferment soybeans for making soy sauce and miso. However, in the production of fermented foods of soybeans such as soy sauce and miso, Aspergillus sojae is sometimes used instead of A. oryzae. Incidentally, in China and Korea, the fungi used for fermented foods for a long time in the production of traditional alcoholic beverages were not A. oryzae but fungi belonging to Rhizopus and Mucor. A. oryzae is also used for the production of rice vinegars. Barley kōji (麦麹) or rice kōji (米麹) are made by fermenting the grains with A. oryzae hyphae.
Naringin is a flavanone-7-O-glycoside between the flavanone naringenin and the disaccharide neohesperidose. The flavonoid naringin occurs naturally in citrus fruits, especially in grapefruit, where naringin is responsible for the fruit's bitter taste. In commercial grapefruit juice production, the enzyme naringinase can be used to remove the bitterness created by naringin. In humans naringin is metabolized to the aglycone naringenin by naringinase present in the gut.
A phytase is any type of phosphatase enzyme that catalyzes the hydrolysis of phytic acid – an indigestible, organic form of phosphorus that is found in many plant tissues, especially in grains and oil seeds – and releases a usable form of inorganic phosphorus. While phytases have been found to occur in animals, plants, fungi and bacteria, phytases have been most commonly detected and characterized from fungi.
Aspergillopepsin I is an enzyme. This enzyme catalyses the following chemical reaction
α-Glucosidase is a glucosidase located in the brush border of the small intestine that acts upon α(1→4) bonds:
Piceid is a stilbenoid glucoside and is a major resveratrol derivative in grape juices. It can be found in the bark of Picea sitchensis. It can also be isolated from Reynoutria japonica, the Japanese knotweed.
Pectin lyase is a polysaccharide enzyme with a complex structure that is present in plant cell walls. It has a significant role in pectin degradation and different biotechnological and industrial applications. It can be found in different organisms.
The enzyme feruloyl esterase (EC 3.1.1.73) catalyzes the reaction
In enzymology, a flavanone 7-O-beta-glucosyltransferase is an enzyme that catalyzes the chemical reaction
GBA2 is the gene that encodes the enzyme non-lysosomal glucosylceramidase in humans. It has glucosylceramidase activity.
Cytosolic beta-glucosidase, also known as cytosolic beta-glucosidase-like protein 1, is a beta-glucosidase enzyme that in humans is encoded by the GBA3 gene.
The enzyme pyrethroid hydrolase (EC 3.1.1.88, pyrethroid-hydrolyzing carboxylesterase, pyrethroid-hydrolysing esterase, pyrethroid-hydrolyzing esterase, pyrethroid-selective esterase, pyrethroid-cleaving enzyme, permethrinase, PytH, EstP; systematic name pyrethroid-ester hydrolase) catalyses the reaction
Arabinan endo-1,5-α-L-arabinanase is an enzyme with systematic name 5-α-L-arabinan 5-alpha-L-arabinanohydrolase. This enzyme catalyses the following chemical reaction
Mannosyl-oligosaccharide glucosidase (MOGS) (EC 3.2.1.106, processing α-glucosidase I,Glc3Man9NAc2 oligosaccharide glucosidase, trimming glucosidase I, GCS1) is an enzyme with systematic name mannosyl-oligosaccharide glucohydrolase. MOGS is a transmembrane protein found in the membrane of the endoplasmic reticulum of eukaryotic cells. Biologically, it functions within the N-glycosylation pathway.
Galactan endo-1,6-beta-galactosidase is an enzyme with systematic name endo-beta-(1->6)-galactanase. This enzyme catalyses the following chemical reaction
Prunin is a flavanone glycoside found in immature citrus fruits and in tomatoes. Its aglycone form is called naringenin.
Penicillium decumbens is an anamorph species of the genus of Penicillium which occurs widespread in nature, mainly in subtropical and tropical soil but it also occur in food. Analysis have shown that Penicillium decumbens has antibiotic activity Penicillium decumbens produces the cyclopentenone cyclopenicillone
References
- ↑ Puri, Munish; Kalra, Sukirti (2005). "Purification and characterization of naringinase from a newly isolated strain of Aspergillus niger 1344 for the transformation of flavonoids". World Journal of Microbiology and Biotechnology. 21 (5): 753. doi:10.1007/s11274-004-5488-7.
- ↑ Puri, M; Banerjee, UC (2000). "Production, purification, and characterization of the debittering enzyme naringinase". Biotechnology Advances. 18 (3): 207–17. doi:10.1016/S0734-9750(00)00034-3. PMID 14538108.
- ↑ Puri, Munish; Banerjee, Anirban; Banerjee, U.C. (2005). "Optimization of process parameters for the production of naringinase by Aspergillus niger MTCC 1344". Process Biochemistry. 40: 195. doi:10.1016/j.procbio.2003.12.009.