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Enzyme purification fold
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The enzymatic synthesis of fructooligosaccharides (FOS) was carried out using a partially purified -fructofuranosidase from the commercial enzyme preparation Viscozyme L. Partial purification of -fructofuranosidase from Viscozyme L was done by batch adsorption using ion-exchange resin DEAESepharose, showing a 6-fold increase in specific activity.
5p
vihermione
06-01-2023
11
2
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Rosmarinic acid is a water-soluble ester of caffeic acid and 3,4-dihydroxyphenyllactic acids, and is mainly found in plant species including Boraginaceae and Lamiaceae. In this research, we determined the inhibition property of rosmarinic acid on carbonic anhydrase isoenzymes I and II (hCA I and II) purified from human erythrocytes by using Sepharose-4B affinity column chromatography. hCA I and II isoenzymes were obtained with a yield of 57.9% and 67.2% and 76.5- and 509.3-fold purification of each isoenzyme, respectively.
9p
langthannam
29-12-2021
9
0
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Thioredoxin reductase (E.C 1.6.4.5.; TrxR) is an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. In this study, mitochondrial TrxR enzyme was purified from rainbow trout mitochondria. Thanks to the 2 consecutive procedures (preparation of homogenate and 2’,5’-ADP Sepharose 4B affinity chromatography), the enzyme, having the specific activity of 11.9 EU mg protein-1, was purified with a yield of 2.38% and 672-fold. The purity of the enzyme was monitored and the molecular weight of its subunits was calculated as 70 kDa by SDS-PAGE.
10p
langthannam
29-12-2021
10
0
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A carboxymethylcellulose (CMC)-degrading bacterium was isolated from soil, identified as Bacillus methylotrophicus according to the physiological properties and analyses of 16S rRNA and a partial sequence of the gyrase A (gyrA) gene, and named as B. methylotrophicus Y37. The CMCase enzyme was purified to homogeneity by 20.4-fold with 21.73% recovery using single-step hydrophobic interaction chromatography and biochemically characterized. CMCase showed a molecular weight of approximately 50 kDa as determined by SDS-PAGE.
14p
langthannam
29-12-2021
9
0
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The thioredoxin system, found in all living creatures, consists of thioredoxin protein (Trx), thioredoxin reductase enzyme (TrxR), and NADPH. In this study, turkey liver mitochondrial TrxR enzyme with 3.07 EU × mg −1 specific activity was purified 990-fold in a yield of 2.05% using 2’,5’-ADP Sepharose 4B affinity chromatography. The purity of the enzyme was measured and the molecular weight of its subunits was determined to be 45.5 kDa by SDSPAGE. The molecular mass of the enzyme’s natural state was found to be 88 kDa using Sephadex-G 150 gel filtration chromatography.
13p
langthannam
29-12-2021
10
0
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Recombinant production of amebic cysteine proteases using Escherichia coli cells as the bacterial system has become a challenging effort, with protein insolubility being the most common issue.
7p
vihamax2711
21-04-2020
11
0
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Acidic and alkaline proteases from visceral waste of Labeo rohita (Hamilton, 1822) were isolated, partially purified by ammonium sulphate precipitation followed by dialysis, their kinetics and characteristics studied. The purification fold increased from 1.24 to 2.49 and 1.19 to 1.55 in acidic and alkaline protease respectively along the purification steps.
17p
chauchaungayxua4
18-03-2020
11
1
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Microbial phytases are of immense importance due to their application in food/feed industry by enhancing the availability of essential minerals such as phosphorous, iron, calcium etc. required for normal human physiology and also have commercial and environment significance. Therefore, in present study an attempt was made to enhance the production of phytase from isolated probiotic Pediococcus acidilactici BNS5B by employing both one variable at a time approach and statistically based design of experiments such as Plackett-Burman and Response Surface Methodology.
22p
caygaocaolon3
09-03-2020
28
1
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The use of enzymes in a free form is very uneconomical because the enzymes generally cannot be recovered at the end of the reaction. These drawbacks can be overcome by immobilization of the enzyme thereby rendering it more stable and easy to recover and recycle. It is a very effective alternative for gripping the problems of instability, repetitive use and reduction in the cost of enzyme. The aim of this research was to obtain the optimum condition of the making of immobilized amylase beads using a different natural matrix. The result obtain that amylase producing isolate i.e.
7p
nguathienthan2
19-12-2019
7
1
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Purification and characterization of a cyanide-degrading nitrilase from Trichoderma harzianum VSL291
An intracellular nitrilase (Nit1) with cyanide-degrading activity was isolated from Trichoderma harzianum VSL291, cultivated on benzonitrile as the sole carbon source. Nit1 was purified to homogeneity by ion exchange and gel filtration chromatography with a recovery of 7.15% and a fold of 22.5.
10p
vikimsa
22-02-2019
21
1
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An extracellular endoglucanase (EG) from Aspergillus niger VTCC-F021 was purified 2.09-fold to homogeneity with a yield of 18.4%. The enzyme had a molecular mass of 31 kDa and a specific activity of 14.122 U/mg protein.
8p
vivant2711
01-02-2019
21
3
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A novel extracellular endoglucanase from a basidiomycete strain Peniophora sp. NDVN01 was purified 2.8-fold to homogeneity through ammonium sulfate precipitation and gel filtration with Bio-Gel P-100 and Sephadex G-75. The endoglucanase had a specific activity of 163.8 U/mg protein and a molecular mass of 32 kDa.
8p
sony2711
01-02-2019
20
1
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An extracellular lipase, LipA, extracted fromAcinetobacter sp. RAG-1 grown on hexadecane was purified and proper-ties of the enzyme investigated. The enzyme is released into the growth medium during the transition to stationary phase. The lipase was harvested from cells grown to sta-tionary phase, and purified with 22% yield and 10-fold purification. The protein demonstrates little affinity for anionexchange resins,withcontaminatingproteins removed by passing crude supernatants over a Mono Q column....
9p
tumor12
22-04-2013
45
1
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Geraniol dehydrogenase (GeDH), which plays an important role in the bio-synthesis of neral, an alarm pheromone, was purified from the astigmatid miteCarpoglyphus lactis. The enzyme was obtained in an apparently homo-geneous and active form after 1879-fold purification through seven steps of chromatography.
11p
media19
06-03-2013
39
3
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