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重要文件

01824

Sigma-Aldrich

Acylase I, immobilized on Eupergit® C from Aspergillus sp.

≥50 U/g moist material

同義詞:

Aminoacylase, immobilized, Plexazym® AC

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About This Item

酶委員會編號:
MDL號碼:
分類程式碼代碼:
12352204
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形狀

beads

比活性

≥50 U/g moist material

儲存溫度

2-8°C

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一般說明

the immobilized acylase catalyzes the hydrolysis of N-acetyl-DL-amino acid to L-amino acid, the D-form is not attacked

單位定義

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol N-acetyl-L-methionine per minute at pH 8.0 and 25°C

重構

Standard procedure: a 10-20% substrate solution, pH 6-8, with an addition of CoCl2 (10-4 moles) at 33°C was used. Prior to use the polymer was washed with water (50 times bed volumes); when used in a fixed bed reactor, a velocity of flow of 3 bed volumes/h leads to a hydrolysis degree of 80%

分析報告

moist pearls (dried substance ~30%, pearl diameter 50-100 μm), covalent fixation of the acylase

其他說明

The immobilized acylase is used for the convenient resolution of amino acids via the selective deacetylation of N-acetyl-L-amino acids in DL-racemates[1][2][3][4]

法律資訊

Eupergit is a registered trademark of Röhm GmbH & Co. KG
Plexazym is a registered trademark of Röhm GmbH & Co. KG

儲存類別代碼

13 - Non Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable

個人防護裝備

Eyeshields, Gloves, type N95 (US)


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J. Tramper
Solid Phase Biochemistry, 393-393 (1983)
Preparation and properties of enzymes immobilized by copolymerization.
D Jaworek et al.
Methods in enzymology, 44, 195-120 (1976-01-01)
Optical resolution of racemic amino acids by aminoacylase.
T Sato et al.
Bioprocess technology, 16, 3-14 (1993-01-01)
W. Kuhlmann et al.
Chemie Ingenieur Technik, 52, 607-607 (1980)
Keya Cai et al.
Sheng wu gong cheng xue bao = Chinese journal of biotechnology, 24(2), 285-290 (2008-05-10)
Three model silkworms, highly resistant strain, highly susceptible strain and their near isogenic line were established by hybridization and backcross. The resistance of silkworm (Bombyx mori L.) to BmNPV was studied at proteomic level using two-dimensional gel electrophoresis and MALDI

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