THE ENZYMATIC HYDROLYSIS PRODUCTS OF SARIN

The hydrolysis of the powerful cholinesterase inhibitor, sarin, by a rat serum enzyme leads almost exclusively to isopropyl methylphosphonic acid, neither methylphosphonic acid nor hydrogen methylphosphonofluoridate being formed. When isopropyl methylphosphonic acid is administered to the intact rat, it is excreted unchanged in the urine. It is inferred, therefore, that the metabolism of sarin by the intact rat would lead almost exclusively to isopropyl methylphosphonic acid.

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STEREOSPECIFICITY IN THE ENZYMATIC HYDROLYSIS OF TABUN AND ACETYL-β-METHYLCHOLINE CHLORIDE

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y55-116 ◽

1955 ◽

Vol 33 (1) ◽

pp. 963-969 ◽

Cited By ~ 1

Author(s):

F. C. G. Hoskin ◽

G. S. Trick

Keyword(s):

Enzymatic Hydrolysis ◽

Enzymatic Reaction ◽

Brain Homogenate ◽

Serum Enzyme ◽

Rat Serum ◽

Bicarbonate Buffer ◽

First Order ◽

Acetylcholine Chloride ◽

Hydrolysis Of ◽

Enzyme Source

The hydrolysis of the powerful cholinesterase inhibitor, tabun, at pH 7 to 7.5 by a rat serum enzyme in bicarbonate buffer involves two simultaneous first-order reactions. A fast, enzyme-catalyzed reaction destroys the toxic dextrorotatory isomer of tabun. The much slower hydrolysis of the levorotatory and apparently non-toxic isomer is probably a non-enzymatic reaction. The enzymatic hydrolysis of acetyl-dl-β-methylcholine chloride by a rat brain homogenate has been studied as a model reaction. Only one-half of the racemic compound is hydrolyzed in contrast to the complete hydrolysis of acetylcholine chloride by the same enzyme source. These results and the results of toxicity studies on the hydrolyzing solution indicate that true cholinesterase hydrolyzes only the dextrorotatory isomer of acetyl-dl-β-methylcholine chloride.

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STEREOSPECIFICITY IN THE ENZYMATIC HYDROLYSIS OF TABUN AND ACETYL-β-METHYLCHOLINE CHLORIDE

Canadian Journal of Biochemistry and Physiology ◽

10.1139/o55-116 ◽

1955 ◽

Vol 33 (6) ◽

pp. 963-969 ◽

Cited By ~ 33

Author(s):

F. C. G. Hoskin ◽

G. S. Trick

Keyword(s):

Enzymatic Hydrolysis ◽

Enzymatic Reaction ◽

Brain Homogenate ◽

Serum Enzyme ◽

Rat Serum ◽

Bicarbonate Buffer ◽

First Order ◽

Acetylcholine Chloride ◽

Hydrolysis Of ◽

Enzyme Source

The hydrolysis of the powerful cholinesterase inhibitor, tabun, at pH 7 to 7.5 by a rat serum enzyme in bicarbonate buffer involves two simultaneous first-order reactions. A fast, enzyme-catalyzed reaction destroys the toxic dextrorotatory isomer of tabun. The much slower hydrolysis of the levorotatory and apparently non-toxic isomer is probably a non-enzymatic reaction. The enzymatic hydrolysis of acetyl-dl-β-methylcholine chloride by a rat brain homogenate has been studied as a model reaction. Only one-half of the racemic compound is hydrolyzed in contrast to the complete hydrolysis of acetylcholine chloride by the same enzyme source. These results and the results of toxicity studies on the hydrolyzing solution indicate that true cholinesterase hydrolyzes only the dextrorotatory isomer of acetyl-dl-β-methylcholine chloride.

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EFFECTS OF ASCORBIC ACID AND FERUM IONS CONCENTRATION ON THE HYDROLYSIS OF GLUCOSINOLATE AND MYROSINASE ACTIVITY IN THE WATERCRESS (Nasturtium officinale sp.)

Jurnal Teknologi ◽

10.11113/jt.v78.5092 ◽

2016 ◽

Vol 78 (8) ◽

Cited By ~ 1

Author(s):

Syamimi Mohd Zul ◽

Noumie Surugau

Keyword(s):

Ascorbic Acid ◽

Enzymatic Hydrolysis ◽

Hydrolysis Product ◽

Carcinogenic Activity ◽

Nasturtium Officinale ◽

Hydrolysis Products ◽

Low Concentrations ◽

Health Promoting ◽

Hydrolysis Of ◽

Myrosinase Activity

Watercress (Nasturtium officinale sp.) from the Brassicae family contains phenethyl glucosinolates (gluconasturtiin) as the main glucosinolate (GLS). The enzymatic hydrolysis products by naturally-occuring myrosinase produced phenethyl isothicyanate (PEITC) which reported to possess anti-carcinogenic activity. Depending on several factors, its counterpart, phenethyl nitrile (PEN) can also be formed as hydrolysis product. This study investigated the effects of adding ascorbic acid and Fe2+ ions at different concentration on the hydrolysis of gluconasturtiin. Hydrolysis products were extracted using dichloromethane and analyzed semi-quantitatively by using GCMS. The results showed that PEITC increased at the low concentration of ascorbic acid (up to 0.06M). Similarly, addition of up to 0.06M Fe2+ ions increased PEITC; higher than 0.06M inhibits the formation of PEITC. Interestingly, similar trend for the production of PEN was detected. This study also investigated myrosinase activity both by exogenous and endogenous methods at different concentrations of ascorbic acid and Fe2+ ions using standard sinigrin as subsrat. Overall, the myrosinase activity was more active at the low concentrations of ascorbic acid. Also, the exogenous method is more efficient than endogenous. This study proved that the presence of reducing agents such as ascorbic acid and Fe2+ ions during the preparation of watercress as food would affect the production of the health-promoting PEITC.

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Enzymatic Hydrolysis of Marine Collagen and Fibrinogen Proteins in the Presence of Thrombin

Marine Drugs ◽

10.3390/md18040208 ◽

2020 ◽

Vol 18 (4) ◽

pp. 208 ◽

Cited By ~ 2

Author(s):

Ludmila L. Semenycheva ◽

Marfa N. Egorikhina ◽

Victoria O. Chasova ◽

Natalya B. Valetova ◽

Yulia L. Kuznetsova ◽

...

Keyword(s):

Molecular Weight ◽

Enzymatic Hydrolysis ◽

Main Part ◽

Room Temperature ◽

A Value ◽

Hydrolysis Products ◽

Native Collagen ◽

Before And After ◽

Molecular Fraction ◽

Hydrolysis Of

Enzymatic hydrolysis of native collagen and fibrinogen was carried out under comparable conditions at room temperature. The molecular weight parameters of proteins before and after hydrolysis by thrombin were monitored by gel-penetrating chromatography (GPC). An analysis of the experiment results shows that the molecular weight parameters of the initial fibrinogen (Fn) and cod collagen (CC) are very similar. High molecular CC decays within the first minute, forming two low molecular fractions. The main part (~80%) falls on the fraction with a value of Mw less than 10 kDa. The initial high molecular fraction of Fn with Mw ~320–340 kDa is not completely hydrolyzed even after three days of control. The presence of low molecular fractions with Mw ~17 and Mw ~10 kDa in the solution slightly increases within an hour and noticeably increases for three days. The destruction of macromolecules of high molecular collagen to hydrolysis products appears almost completely within the first minute mainly to the polymer with Mw ~10 kDa, and enzymatic hydrolysis of fibrinogen proceeds slower than that of collagen, but also mainly to the polymer with Mw ~10 kDa. Comparative photos of the surfaces of native collagen, fibrinogen and the scaffold based on them were obtained.

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Hidrolisis Enzimatis Minyak Kelapa Hidrolisis Enzimatis Minyak Kelapa dengan Lipase dari Rhyzomucor miehei / Enzymatic Hydrolysis of Coconut Oil using Lipase from Rhyzomucor mieheiLipase dari Rhizomucor miehei

Buletin Palma ◽

10.21082/bp.v17n1.2016.35-40 ◽

2017 ◽

Vol 17 (1) ◽

pp. 35

Author(s):

Steivie Karouw ◽

Linda Trivana ◽

Rindengan Barlina ◽

Budi Santosa

Keyword(s):

Fatty Acid ◽

Free Fatty Acid ◽

Enzymatic Hydrolysis ◽

Silica Gel ◽

Coconut Oil ◽

Rhizomucor Miehei ◽

Enzyme Concentration ◽

Hydrolysis Reaction ◽

Hydrolysis Products ◽

Hydrolysis Of

The objectives of the research was to find the temperature and time of enzymatic hydrolysis reaction of coconut oil by lipase from Rhizomucor miehei as biocatalyze which could produce the highest free fatty acids. Enzymatic hydrolysis reaction was held at various of reaction temperature (35, 40, 45 dan 50oC) and reaction duration (6, 12, 18 and 24 hours). Enzymatic hydrolysis reaction was carried out in waterbath shaker on pH of 7.0 and enzyme concentration of 2.5% based on substrate weight. The hydrolysis products were monitored using TLC using hexane:diethyl eter:acetic acid = 80:20:1 as developing solvent on silica gel F254, 20 cm x 20 cm aluminium plat. The results showed that hydrolyzed coconut oil contained 5 spots, they were identified as 1 spot of triglyceride at upper, 1 spot of free fatty acid, 2 spots of diglyceride at the middle and 1 spot monoglyceride at the bottom. The condition of enzymatic hydrolysis reaction produce the highest of free fatty acid (37.10%) at 50°C of temperature for 24 hours.ABSTRAK Penelitian ini bertujuan untuk mengetahui suhu dan lama reaksi yang dapat menghasilkan asam lemak bebas (ALB) paling banyak pada proses hidrolisis minyak kelapa menggunakan biokatalis lipase dari Rhizomucor miehei. Hidrolisis dilakukan pada variasi suhu reaksi (35, 40, 45 dan 50oC) dan lama reaksi (6, 12, 18 dan 24 jam). Reaksi hidrolisis dilakukan dalam shaker waterbath dengan pH 7,0 dan kosentrasi enzim 2,5% dari berat substrat. Hasil hidrolisis dianalisis dengan kromatografi lapis tipis (KLT) menggunakan larutan pengembang campuran pelarut heksan:dietil eter:asam asetat = 80:20:1 pada pelat silica gel F254, pelat aluminium 20 cm x 20 cm. Hasil penelitian menunjukkan bahwa hasil hidrolisis minyak kelapa teridentifikasi lima spot yaitu satu spot trigliserida pada bagian atas, 1 spot asam lemak bebas, dua spot digliserida dan satu spot monogliserida pada bagian bawah. Kondisi hidrolisis minyak kelapa dengan lipase dari R. miehei untuk menghasilkan asam lemak bebas tertinggi yaitu pada suhu 50°C selama 24 jam yaitu sebanyak 37,10%.

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