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Urea carboxylase

Urea carboxylase (EC 6.3.4.6) is an enzyme that belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is urea:carbon-dioxide ligase. This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, biotin.

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Urease

Urease functionally, belong to the superfamily of amidohydrolases and phosphotriestreases.It is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia.In 1926, James B. Sumner, an assistant professor at Cornell University, showed that urease is a protein by examining its crystallized form.Urease is produced by numerous taxonomically diverse bacterial species, including normal flora and nonpathogens. Also, urease has been demonstrated as a potent virulence factor for some species.Ureases are nickel-dependent enzymes that catalyze the hydrolysis of urea into 2 molecules of ammonia and 1 of carbon dioxide.Urease is a highly efficient catalyst for the hydrolysis of urea with a rate approximately 10 14 times the rate of the noncatalyzed reaction. It has a long and distinguished history in the development of enzymology.

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Ureidoglycolate dehydrogenase

Ureidoglycolate dehydrogenase (EC 1.1.1.154) is an enzyme that belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-ureidoglycolate:NAD(P)+ oxidoreductase. This enzyme participates in purine metabolism.

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Uridine monophosphate synthetase

Uridine monophosphate synthetase (UMPS) (orotate phosphoribosyl transferase and orotidine-5'-decarboxylase) is the enzyme (EC 4.1.1.23) that catalyses the formation of uridine monophosphate (UMP), an energy-carrying molecule in many important biosynthetic pathways. In humans, the gene that codes for this enzyme is located on the long arm of chromosome 3 (3q13).

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Uroporphyrinogen III decarboxylase

Uroporphyrinogen decarboxylase, also known as UROD, is an enzyme which in humans is encoded by the UROD gene.This enzyme is responsible for catalyzing the conversion of uroporphyrinogen to coproporphyrinogen through the removal of four carboxymethyl side chains.

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VEMOZYMЕ GO

VEMOZYMЕ GO is a glucose oxidase preparation obtained by submerged fermentation of aspergillus niger and developed especially for bakery applications. VEMOZYMЕ GO catalyses the oxidation of glucose,as the result of this oxidation is gluconic acid and hydrogen peroxide.It is used to strengthen gluten in dough systems.VEMOZYMЕ GO improves dough strength and elasticity,works resistant bagainst the process of freezing and thawing.

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VEMOZYMЕ L

VEMOZYMЕ L is a lipolytic enzyme preparation produced by deep culture of a specially selected strain producer aspergillus niger. VEMOZYMЕ L is widely used for different food-grade applications mainly in bakery, where it improves crust and crumb structure, and prolongs bread shelf-life.

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VEMOZYMЕ PHL

VEMOZYMЕ PHL is a well-balanced mixture of specially selected lipases and phospholipases, designed especially for bakery applications. The main effect of Vemozymе PHL is replacement or considerable reduction of emulsifiers such as DATEM, SSL and CSL.

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VEMOZYMЕ X Plus

VEMOZYMЕ X Plus is a xylanase/hemicellulase enzyme. It improves wheat gluten network elasticity by acting on soluble and insoluble pentosans in the flour during dough processing. VEMOZYMЕ X Plus represents good alternative of dough conditioning emulsifiers and could be used alone or in combination with the latter.

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VERON 191

VERON 191 is a concentrated fungal xylanase obtains high baking volume and improved dough properties, recommended for use in combination with VERON M4.In particular, Veron 191 produces a stable, fluffy dough and voluminous loaves of bread with a soft, elastic crumb. This product is used as a processing aid in the first steps of the baking process

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