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Jaipur Bio Fertilizers
Jaipur Bio Fertilizers


Enzymes

Prominent & Leading Manufacturer from Jaipur, we offer phytase, b-galactosidase, cellulase, mannanase, protease and amylases.

Phytase

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Phytase
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Approx. Rs 10,000 / OrderGet Latest Price

Product Details:
Packaging Size1 kg
Packaging TypePouch
BrandSamridhi

Phytase is an enzyme that helps to break down phytate P (the main form of P in grains) allowing better absorption of grain P by poultry (and other monogastric animals such as swine) and reduces the need for addition of calcium phosphate supplements.

Phytases are digestive enzymes which release plant phosphorus from phytic acid.

Monogastric animals lack sufficient phytases to release the phosphorus. Adding extra phytases to the diet increases phytate breakdown and consequent utilization of plant phosphorus.

If more phosphorus is available naturally, then less of this substance has to be added to the diet. This greatly reduces feed costs.

If phosphorus in the diet is utilized more efficiently, then less of this substance is excreted. This reduces the impact of livestock production on the environment.

Our phytases deliver exceptional phosphorus release in combination with outstanding reliability and consistency. They enable improved performance and greater business sustainability.

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B-Galactosidase

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B-Galactosidase
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Approx. Rs 10,000 / OrderGet Latest Price

Product Details:
Minimum Order Quantity10000 Order
Packaging size1 kg
BrandSamridhi

Escherichia coli (E. coli) can produce the enzyme β-galactosidase which breaks lactose into galactose and glucose. However, the gene for β-galactosidase is normally switched off, except in the presence of lactose.

In this procedure, a sample of E. coli is treated with lactose, and then the β-galactosidase activity of this sample and an untreated sample are compared. ONPG (ortho-nitrophenyl-β-D-galactoside) is used as a substrate for the enzyme action which produces galactose and a compound which is yellow in alkaline conditions. The intensity (or optical density) of the yellow colour produced is a qualitative indicator or quantitative measure (with a colorimeter) of the β-galactosidase activity.

 

β-Galactosidase is an important enzyme since lactose cannot be utilized as either a carbon or an energy source until it has been broken down into its monosaccharide components.

Beta-galactosidase is a huge bacterial enzyme that performs several tiny tasks. Its first task is to perform an initial step in energy production: it breaks lactose, a common sugar in milk, into two pieces, glucose and galactose, so that they can be used in glycolysis. It also performs a similar side reaction: it can break lactose and then reconnect the pieces in a slightly different way to form allolactose. This cleavage reaction is important for the life of the bacterium, but it has also played a central role in many scientific discoveries.

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Cellulase

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Cellulase
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Cellulase refers to a group of enzymes which, acting together, hydrolyze cellulose.

Cellulose is a linear polysaccharide of glucose residues connected by β-1,4 linkages.
Like chitin it is not cross-linked. Native crystalline cellulose is insoluble and occurs as fibers of densely packed, hydrogen bonded, anhydroglucose chains of 15 to 10,000 glucose units. Its density and complexity make it very resistant to hydrolysis without preliminary chemical or mechanical degradation or swelling.

In nature cellulose is usually associated with other polysaccharides such as xylan or lignin. It is the skeletal basis of plant cell walls. Cellulose is the most abundant organic source of food, fuel and chemicals (Spano et al. 1975). However, its usefulness is dependent upon its hydrolysis to glucose.
Acid and high temperature degradation are unsatisfactory in that the resulting sugars are decomposed; enzymatic degradation (cellulase) is the most effective means of degrading cellulose into useful components. Although cellulases are distributed throughout the biosphere, they are most prevalent in fungal and microbial sources.

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Mannanase

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Mannanase
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Beta-Mannanase (endo-1, 4-ß-mannanase ) is made from a refined strain of Trichoderma reesei through liquid fermentation and extraction technology.
This product is a subcategory of hemi-cellulase, which can break the beta-1, 4 glycosidic bonds of mannan into mannan-oligosaccharides. The substrates are ß mannan, galactomannan, and galactose.

Mannanase are the major constituents of the hemicellulose fraction in softwoods and show widespread distribution in plant tissues.
The major mannan-degrading enzymes are β-mannanases, β-mannosidases and β-glucosidases. In addition to these, other enzymes such as α-galactosidases and acetyl mannan esterases, are required to remove the side chain substituents.
The mannanases are known to be produced by a variety of bacteria, fungi, actinomycetes, plants and animals. Microbial mannanases are mainly extracellular and can act in wide range of pH and temperature because of which they have found applications in pulp and paper, pharmaceutical, food, feed, oil and textile industries.

This review summarizes the studies on mannanases reported in recent years in terms of important microbial sources, production conditions, enzyme properties, heterologous expression and potential industrial applications.

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Protease

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Protease
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A protease (also called a peptidase or proteinase) is an enzyme that catalyzes proteolysis, the breakdown of proteins into smaller polypeptides or single amino acids. They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water breaks bonds. Proteases are involved in many biological functions, including digestion of eaten proteins, protein catabolism.

Without additional helping mechanisms, proteolysis would be very slow, taking hundreds of years. Proteases can be found in all forms of life and viruses. They have independently evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms

Protease is a group of enzymes that break the long chainlike molecules of proteins into shorter fragments and eventually into their components, amino acids. Proteolytic enzymes are present in bacteria, certain types of algae, some viruses, and plants they are most abundant, however, in animals.

There are different types of proteolytic enzymes, which are classified according to sites at which they catalyze the cleavage of proteins. The two major groups are the exopeptidases, which target the terminal ends of proteins, and the endopeptidases, which target sites within proteins. Endopeptidases employ various catalytic mechanisms; within this group are the aspartic endopeptidases, cysteine endopeptidases, glutamic endopeptidases, metalloendopeptidases, serine endopeptidases, and threonine endopeptidases. The term oligopeptidase is reserved for those enzymes that act specifically on peptides.

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Amylases

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Amylases
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Amylases are a class of enzymes that catalyze the hydrolysis of starch into sugars such as glucose and maltose.

Amylase is an enzyme that catalyses the hydrolysis of starch into sugars. Amylase is present in the saliva of humans and some other mammals, where it begins the chemical process of digestion. Foods that contain large amounts of starch but little sugar, such as rice and potatoes, may acquire a slightly sweet taste as they are chewed because amylase degrades some of their starch into sugar. The pancreas and salivary gland make amylase (alpha amylase) to hydrolyse dietary starch into disaccharides and trisaccharides which are converted by other enzymes to glucose to supply the body with energy. Plants and some bacteria also produce amylase.

There are three types of Amylase:

1) α-Amylase

2) β-Amylase

3) γ-Amylase

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Xylanases

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Xylanases are a group of glycoside hydrolase enzymes that degrade the linear polysaccharide xylan into xylose by catalyzing the hydrolysis of the glycosidic linkage (β-1,4) of xylosides.

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.

As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., mammals do not produce xylanases. However, the principal commercial source of xylanases is filamentous fungi.

Commercial applications for xylanase include the chlorine-free bleaching of wood pulp prior to the papermaking process, and the increased digestibility of silage.

Apart from its use in the pulp and paper industry, xylanases are also used as food additives to poultry; in wheat


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Lipase

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Lipase, any of a group of fat-splitting enzymes found in the blood, gastric juices, pancreatic secretions, intestinal juices, and adipose tissues. Lipases hydrolyze triglycerides (fats) into their component fatty acid and glycerol molecules.

Initial lipase digestion occurs in the lumen (interior) of the small intestine. Bile salts reduce the surface tension of the fat droplets so that the lipases can attack the triglyceride molecules. The fatty acid and glycerol molecules are then taken up into the epithelial cells that line the intestinal wall, where they are resynthesized into triglycerides for transport to muscles and adipose tissues. At these sites lipases in the bloodstream hydrolyze the triglycerides, and the resulting fatty acids and glycerol are taken up by the cells of these tissues. In the adipose tissues triglycerides are re-formed for storage until the energy needs of the animal increase under conditions of stress or exercise. Lipases in the cells of adipose tissues break down the triglycerides so that fatty acids can reenter the bloodstream for transport to energy-requiring tissues.

 


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