α-amylase

Salivary α-amylase has been used as a biomarker for stress that does not require a blood draw.

Because it can act anywhere on the substrate, α-amylase tends to be faster-acting than β-amylase.

Flavonoids also block several digestive enzymes, including α-amylase, trypsin and lipase.

Pentagalloyl glucose can precipitate proteins including human salivary α-amylase.

A biological detergent can contain α-amylase, a cellulase, a protease and a lipase.

In the human pancreas the digestion of starch is catalyzed by an α-amylase, as the salivary enzyme.

Currently, glucose syrup is mainly produced by first adding the enzyme α-amylase to a mixture of corn starch and water.

While the measurement is applicable to any amylase, in general it refers to the combined α-amylase and β-amylase used in brewing.

Commonly cyclodextrin glycosyltransferase (CGTase) is employed along with α-amylase.

They also secrete enzymes to enhance host digestive enzymes e.g. pancreatic α-amylase.

The digestive enzyme α-amylase is responsible for the breakdown of the starch molecule into maltotriose and maltose, which can be used as sources of energy.

Although found in many tissues, amylase is most prominent in pancreatic juice and saliva, each of which has its own isoform of human α-amylase.

Strains of S. oralis produce neuraminidase and an IgA protease and cannot bind α-amylase.

First starch is liquified either by heat treatment or using α-amylase, then CGTase is added for the enzymatic conversion.

The first step in the production of high-fructose corn syrup is the treatment of cornstarch with α-amylase, producing shorter chains of sugars called oligosaccharides.

Pancreatic α-amylase randomly cleaves the α(1-4) glycosidic linkages of amylose to yield dextrin, maltose, or maltotriose.

An α-amylase called "Termamyl", sourced from Bacillus licheniformis, is also used in some detergents, especially dishwashing and starch-removing detergents.

Gibberellins in the seed embryo are believed to signal starch hydrolysis through inducing the synthesis of the enzyme α-amylase in the aleurone cells.

By using β-amylase or fungal α-amylase, glucose syrups containing over 50% maltose, or even over 70% maltose (extra-high-maltose syrup) can be produced.

Studies of this process have indicated gibberellins cause higher levels of transcription of the gene coding for the α-amylase enzyme, to stimulate the synthesis of α-amylase.

Molecules smaller than the renal threshold (60-70 kDa) are readily excreted in the urine while the larger ones are metabolized by plasma α-amylase before the degradation products are renally excreted.

This enzyme can work with amylose and/or amylopectin, but only the interior α(1 4) glucose linkages of the amylopectin molecules as the α-amylase cannot hydrolyze the α(1 6) branching points.

By acting at random locations along the starch chain, α-amylase breaks down long-chain carbohydrates, ultimately yielding maltotriose and maltose from amylose, or maltose, glucose and "limit dextrin" from amylopectin.

In the model for gibberellin-induced production of α-amylase, it is demonstrated that gibberellins (denoted by GA) produced in the scutellum diffuse to the aleurone cells, where they stimulate the secretion α-amylase.

In that experiment, RosettaDock made a high-accuracy prediction for the docking between streptococcal pyogenic exotoxin A and a T cell-receptor β-chain, and a medium accuracy prediction for a complex between porcine α-amylase and a camelid antibody.