Trypsin
Source: Swine (Bovine) pancreas
General description
Trypsin is a kind of serine proteolytic enzyme, with molecular weight of 23300 dalton, and is a single peptide chain composed of 223 amino acid residues. With rigorous specificity, the trypsin specifically acts on the peptide linkage constituted by the basic amino acid arginine and leucine. Enzyme easily autolyzes by itself, and its activation also reduces or loses gradually. It is easily soluble in the water, but insoluble in trichloromethane, ethanol, ether and glycerin, and the optimum PH is 8.0~9.0. When the PH is 1.8, it is hardly deactivated when boiled for a short time; if the salt is added into the hot solution, the protein will precipitate, and the enzyme action of filtrate cannot be seen, and Ca2+ plays the role in protecting and activating the trypsin.
The high purity Trypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration.
Specification
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Items
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Specification
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Method
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Appearance
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White or almose white lyophilized powder
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Solvent Transparentness
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Confroms
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USP30
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Loss on drying
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≤ 5.0%
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USP30
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Residue on Ignition
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≤2.5%
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USP30
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Microbial limits
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Confroms
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USP30
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Chymotrypsin
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≤50 USP units/mg powder
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USP30
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Assay
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Trypsin ≥ 2500USP units/mg powder
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USP30
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Storage
Sealed, Dark, at temperature 2-8℃
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