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BIOTOUCH catalase

BIOTOUCH catalase removes hydrogen peroxide from both the fabric and the processed liquor after bleaching. The use of BIOTOUCH catalase creates an environmentally friendly process with decreased water consumption and a shorter process time. This enzymatic bleach cleanup can be peformed in batch process equipment like jets, jiggers or winches. BIOTOUCH catalase works well across a broad temperature range and remains effective even at high peroxide concentrations.

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Batezyme AC

Batezyme AC is a fungal Aspergillus acid protease leather bating enzymes to be used in leather beam house processes for bating of hides and skins already pickled or tanned by either chrome or vegetable synthetic method. Batezyme AC also has application in tanneries processing long stored, picked wet blue or vegetable synthetic crust stock requiring further bating treatment as well as bating of partially chrome tanned leather for manufacturing good quality garment leather.

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Benzaldehyde dehydrogenase

Benzaldehyde dehydrogenase (NADP+) (EC 1.2.1.7) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is benzaldehyde:NADP+ oxidoreductase.This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene degradation.

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Benzamidine Hydrochloride

Benzamidine hydrochloride is used as a ligand in protein crystallography to prevent proteases from degrading a protein of interest.

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Berberine reductase

Berberine reductase (EC 1.5.1.31) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-tetrahydroberberine:NADP+ oxidoreductase.

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Beta adrenergic receptor kinase

Beta adrenergic receptor kinase (BARK) is a serine/threonine intracellular kinase. It is activated by PKA and its target is the beta adrenergic receptor. It is one method by which the cell will desensitize itself from epinephrine overstimulation.

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Beta amyloid

Amyloid beta (Aβ or Abeta) is a peptide of 36–43 amino acids that appears to be the main constituent of amyloid plaques in the brains of Alzheimer's disease patients. Aβ is formed after sequential cleavage of the amyloid precursor protein (APP), a transmembrane glycoprotein of undetermined function. APP can be processed by α-, β- and γ-secretases; Aβ protein is generated by successive action of the β and γ secretases.

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Beta-2-Microglobulin

Beta-2-Microglobulin is a component of MHC class I molecules, which are present on all nucleated cells (excludes red blood cells). It associates not only with the alpha chain of MHC class I molecules, but also with class I-like molecules such as CD1 and Qa. Beta-2-Microglobulin is expressed by the nucleated cells of the body and on many tumor lines.Human Beta-2-Microglobulin is a low molecular weight protein (MW 11600) consisting of a single polypeptide chain of 99 amino acids.It is identical to the small chain of the HLA-A, -B, and -C major histocompatibility complex antigens.In structure and amino acid sequence. Beta-2-Microglobulin resembles the CH3 region of IgG, though it is antigenically distinct. is eliminated via the kidneys. After filtration through the glomeruli. Beta-2-Microglobulin is reabsorbed and catabolized by the proximal tubular cells through endocytosis.It is found at low levels in the serum and urine of normal individuals.

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Beta-Lactamase

Beta-lactamases catalyses the opening and hydrolysis of the beta-lactam ring of beta-lactam antibiotics such as penicillins and cephalosporins.Beta-lactam antibiotics are typically used to treat a broad spectrum of Gram-positive and Gram-negative bacteria.

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Beta-galactoside transacetylase

β-galactoside transacetylase is an enzyme that transfers an acetyl group from acetyl-CoA to β-galactosides. Coded by the gene (lacA) in the lac operon of Escherichia coli. Its precise function as part of the lac operon is not understood currently.

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