scholarly journals PRODUKSI DAN PENENTUAN KONDISI OPTIMUM ENZIM XILANASE Bacillus amyloliquefaciens FUKUMOTO PADA SUBSTRAT XILAN JERAMI

2015 ◽  
Vol 2 (1) ◽  
pp. 74
Author(s):  
Widiyanti Sekatresna ◽  
Abdi Dharma ◽  
Periadnadi
Keyword(s):  
Enzyme Activity ◽  
Rice Straw ◽  
Incubation Time ◽  
Substrate Concentration ◽  
Bacillus Amyloliquefaciens ◽  
Specific Activity ◽  
Enzymatic Reaction ◽  
Optimal Conditions ◽  
Enzyme Specific Activity

 ABSTRACT The production and determination of  optimal condition of xylanase produced by Bacillus amyloliquefaciens on rice straw xylan were investigated in this study. The parameters to be observed were optimal conditions of pH, temperature, substrate concentration and incubation time. Xilanase activity was determined by measuring the amount of reducing sugar formed in the enzymatic reaction based on Somogyi Nelson method. Optimal conditions needed for the production of xylanase were at pH 7, temperature 27°C and six days of incubation time. While optimal conditions of xylanase action were reached at pH 8.2, temperature 45°C, substrate concentration 3.5%(w/w) and 15 minutes of incubation time with enzyme activity and enzyme specific activity of 1.285 U/mL and 0.738 U/mg respectively. As a comparison, xylanase was also produced on pure xylan  (birchwood), enzyme activity and enzyme specific activity obtained were 2.701 U/mL and 1.658 U/mg respectively. Cellulase content in enzyme produced on rice straw xilan showed the enzyme activity of 0.094 U/mL.  Keywords : xylanase, Bacillus amyloliquefaciens, rice straw xilan

scholarly journals PEMANFAATAN PERLIT YANG TELAH DIMODIFIKASI UNTUK AMOBILISASI ENZIM BROMELAIN

2015 ◽  
Vol 3 (1) ◽  
pp. 40
Author(s):  
Elida Mardiah
Keyword(s):  
Enzyme Activity ◽  
Protein Content ◽  
Incubation Time ◽  
Specific Activity ◽  
Native Enzyme ◽  
Enzymes Activity ◽  
Lowry Method ◽  
Enzyme Specific Activity

 ABSTRACT Amobilization of bromelaine enzyme extracted from ananas fruit (Ananas comusus) acetone has been done. Modified perlite in the amino silica phosphat (ASP) is used as matrix amobilization.  The protein content has determined by Lowry method, while enzyme activity were determined by Anson method caseine as substrate. It native enzyme specific activity was 0.1281 unit/mg with konsentration 20000 ppm, pH 7.0, incubation time 35 minutes, and  temperature 40°C. Amobil bromelaine specific activity was 0.7438 units/mg with substrate on 20000 ppm pH 7.0, incubation time 30 minutes and temperature 37°C. This bromelaine enzymes activity was increased six times than native enzim and showed the activity for several repeatation. Keywords: perlit, enzim bromelain, amobilization

scholarly journals Determination of Lipoxygenase Activity in Cereals Grains Using a Silver Nanoparticles Assay

2015 ◽  
Vol 2015 ◽  
pp. 1-5 ◽  
Author(s):  
Raybel Muñoz ◽  
Jose A. Rodriguez ◽  
M. Elena Páez-Hernández ◽  
Irais Sánchez-Ortega ◽  
Eva M. Santos
Keyword(s):  
Silver Nanoparticles ◽  
Enzyme Activity ◽  
Limit Of Detection ◽  
Xylenol Orange ◽  
Enzymatic Reaction ◽  
Lipoxygenase Activity ◽  
Cereal Grains ◽  
Optimal Conditions ◽  
Relative Standard

A spectrophotometric method based on the use of silver nanoparticles is presented for the determination of lipoxygenase activity in cereal grains. The method involves the synthesis of prism silver nanoparticles with a maximum absorption at 752 nm, followed by the abatement of the signal as a consequence of the oxidation produced by hydroperoxides generated in the enzymatic reaction. The quantification of the hydroperoxides produced by reaction of lipoxygenase with linoleic acid allows the determination of the enzyme activity in cereal grains. Under optimal conditions, the linear range of the calibration curve ranges from 1.0 to 5.0 μM, with a limit of detection of 0.34 μM. The method was validated comparing the results with those obtained by ferrous-xylenol orange method. A relative standard deviation < 5.0% was obtained in all cases and no significant differences were observed (p<0.05).

scholarly journals Effects of music playing on biological molecules

2018 ◽  
Vol 210 ◽  
pp. 05006 ◽  
Author(s):  
Catia Algieri ◽  
Claudio Guarnaccia ◽  
Vincenzo Barone ◽  
Maria Raffaella Gullo ◽  
Laura Donato
Keyword(s):  
Enzyme Activity ◽  
Detrimental Effect ◽  
Specific Activity ◽  
Time Lag ◽  
Enzymatic Reaction ◽  
Biological Molecules ◽  
National Council ◽  
Musical Piece ◽  
Tyrosinase Enzyme ◽  
Positive Effect

In this work the effect of two different musical pieces (called “Reminiscenza” and “Pioggia”) on the tyrosinase enzyme activity was investigated. The l-DOPA production by the enzymatic reaction was measured during the continuous playing of these musical pieces. Experiments were performed in the laboratories of the Institute of Membrane Technology (ITM) of the Italian National Council for Research (CNR). The results showed that a positive effect was exercised by the “Reminiscenza” piece, which determined an increase of the specific activity about of 30 % with respect to the value measured in the absence of sound. On the contrary, “Pioggia” piece had a detrimental effect on the enzymatic process. In particular, a time lag on the l-DOPA production, during the first minutes of the reaction, was detected. After this period, an increase of the reaction velocity occurred even if the enzyme activity was lower than the value obtained in the absence of music. These results show that the peculiar characteristics of a musical piece can exercise a positive or negative action on biological elements and open the way to further studies in this area.

Determination of serum aminotransferases: activation by pyridoxal-5'-phosphate in relation to substrate concentration.

1979 ◽  
Vol 25 (1) ◽  
pp. 55-59 ◽  
Author(s):  
J C Hafkenscheid ◽  
C C Dijt
Keyword(s):  
Enzymatic Activity ◽  
Serum Sample ◽  
Aspartate Aminotransferase ◽  
Substrate Concentration ◽  
Enzymatic Reaction ◽  
Reaction Medium ◽  
Aminotransferase Activity ◽  
Serum Aminotransferases ◽  
Stimulation Of

Abstract To investigate the activation of aspartate- and alanine aminotransferases by pyridoxal-5'-phosphate, we determined the enzymatic activity in serum in two different ways: (a) Preincubation of the serum alone or the serum with pyridoxal-5'-phosphate and starting the reaction by the addition of the serum sample or the serum sample + coenzyme, respectively. (b) Preincubation of the serum or the serum with pyridoxal-5'-phosphate in the reaction medium and starting the reaction by adding 2-oxoglutarate. There are only small differences in activities of both aminotransferases determined according to these two different methods. The stimulation by pyridoxal-5'-phosphate is also of the same order, when both methods are compared. Further, these enzymatic activities were measured with use of various concentrations of substrates. From our experiments we conclude that the degree of stimulation of the apoenzyme of the two enzymes is independent of which way the enzymatic reaction is carried out or the substrate concentration, except that aspartate aminotransferase activity is more stimulated by the coenzyme at higher 2-oxoglutarate concentrations.

scholarly journals Optimization of Cellulase Enzyme Production by Co-cultures of Fungi Isolated from Lignocellulosic Waste

2020 ◽  
Vol 6 (5) ◽  
pp. 19-26
Author(s):  
Francis John V ◽  
Dr. Soloman P A
Keyword(s):  
Moisture Content ◽  
Incubation Time ◽  
Substrate Concentration ◽  
Enzyme Production ◽  
Trichoderma Viride ◽  
Cellulase Production ◽  
Optimal Conditions ◽  
Lignocellulosic Waste ◽  
Cellulase Enzyme ◽  
Degree Of Degradation

Fruit wastes were incubated with the mixture of cellulolytic fungi Penicillium citrinum, Aspergillus oryzae, and Trichoderma viride to hydrolyze the cellulosic components and to increase the degree of degradation. . The batch experiments are statistically designed and performed using Box-Benhken method of Response Surface Methodology to investigate the influence of major parameters viz., incubation time, temperature, pH, moisture content and substrate concentration on cellulase enzyme production. Maximum cellulase production of 2.03 Units/ml (U/ml) was detected by the RSM method in a mixed culture containing fungi at a ratio of 1: 1: 1 under optimal conditions at an incubation time of 5.27 days, a temperature of 34.09 °C, pH 4.85, moisture content of 63.83% and a substrate concentration of 5.03%.

Distribution of the multiple molecular forms of glucose-6-phosphate dehydrogenase in different physiological states

1979 ◽  
Vol 57 (5) ◽  
pp. 396-401 ◽  
Author(s):  
Hsiao-Lin Chang ◽  
Darold Holten ◽  
Rom Karin
Keyword(s):  
Enzyme Activity ◽  
Mammary Gland ◽  
Rat Liver ◽  
Specific Activity ◽  
Molecular Forms ◽  
Polyacrylamide Gels ◽  
Multiple Molecular Forms ◽  
Pregnancy And Lactation ◽  
Enzyme Specific Activity ◽  
Glucose 6 Phosphate Dehydrogenase

The distribution of the multiple molecular forms of rat liver and mammary gland glucose-6-phosphate dehydrogenase was determined by electrophoresis on 5% polyacrylamide gels. In both of these organs, changes in the distribution of enzyme activity among the several forms was slight even when approximately 20- to 40-fold changes in enzyme specific activity were achieved by fasting-refeeding experiments (for liver) or during pregnancy and lactation (for mammary gland), it was concluded that the induction of glucose-6-phosphate dehydrogenase in these two organs occurs without any major redistribution among the multiple molecular forms of this enzyme.

scholarly journals Cloning and Expression of Levansucrase Gene of Bacillus velezensis BM-2 and Enzymatic Synthesis of Levan

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 317
Author(s):  
Min Xu ◽  
Lixia Zhang ◽  
Fangkun Zhao ◽  
Jingyue Wang ◽  
Bo Zhao ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Specific Activity ◽  
Enzymatic Reaction ◽  
Production Capacity ◽  
Cloning And Expression ◽  
Buffer System ◽  
Bacterial Strains ◽  
Bacillus Velezensis ◽  
Fusion Enzymes ◽  
Optimal Reaction Temperature

Levan is a versatile and valuable fructose homopolymer, and a few bacterial strains have been found to produce levan. Although levan products have numerous specific functions, their application and promotion were limited by the production capacity and production cost. Bacillus velezensis BM-2 is a levan-synthesizing strain, but its levan production is too low to apply. In this study, the levansucrase gene of B. velezensis BM-2 was cloned to plasmid pET-32a-Acma-zz, and the recombinant plasmids were transferred to Escherichia coli BL21. A transformed clone was selected to express and secrete the fusion enzymes with an Acma-tag efficiently. The expressed products were further purified by a self-developed separating material called bacterial enhancer matrix (BEM) particles. The purification efficiency was 93.4%, with a specific activity of 16.589 U/mL protein. The enzymatic reaction results indicated that the optimal reaction temperature is 50 °C, the optimal pH of the acetate buffer is 5.6, and the buffer system greatly influenced the enzyme activity. The enzyme activity was enhanced to 130% in the presence of 5 mM Ca2+, K+, Zn2+, and Mn2+, whereas it was almost abolished in the case of Cu2+ and Fe3+. The values of Km, kcat, and kcat/Km were 17.41 mM, 376.83 s−1, and 21.64 mM−1s−1, respectively. The enzyme amount of 20 U/g sucrose was added to the system containing 400 g/L sucrose, and the levan products with a concentration of 120 g/L reached after an incubation of 18 h, which was 8 times that of the yield before optimization. The results of molecular docking analysis indicated that the Asp86 might act as a nucleophilic catalytic residue for sucrose, Arg246 and Asp247 act as transition state stabilizer of transfructosylation, and Glu340 and Arg306 were recognized as general acid donors. They formed the catalytic-groups triad. The unique properties and catalytic activity of the levansucrase suggest that it deserves further research and might have good industrial application prospects.

scholarly journals PENGARUH EKSTRAK METANOL DAUN PEPAYA (Carica papaya L.) TERHADAP AKTIVITAS ENZIM LIPASE

KOVALEN ◽  
2017 ◽  
Vol 3 (3) ◽  
pp. 211
Author(s):  
Nurhaeni Nurhaeni ◽  
Ahmad Ridhay ◽  
Magfira Magfira
Keyword(s):  
Enzyme Activity ◽  
Lipase Activity ◽  
Incubation Time ◽  
Substrate Concentration ◽  
Goal Attainment ◽  
Carica Papaya ◽  
Methanol Extract ◽  
Ph Optimum ◽  
Lipase Enzyme ◽  
Optimum Ph

Has conducted research on the effects of methanol extract of leaves papaya (Carica papaya L.) Against Lipase Enzyme Activity. This study aimed to obtain information in a methanol extract inhibits lipase activity. The method used is Complete Random Design (RAL), with goal attainment is done by determining the incubation time lipase enzyme, pH optimum lipase enzyme, and maximum substrate concentration lipase enzyme. And determining the effect of the methanol extract to inhibit the lipase enzyme activity. The results showed that the best incubation time of lipase obtained by time of 120 minutes, the optimum pH 7 and the maximum substrate concentration of 4%. With the highest activity were obtained 16.94 mol /ml.menit, 13.33 mol / ml.menit, and 12.89 mol / ml.menit. The methanol extract of papaya leaves can inhibit the lipase enzyme activity the best concentration of 2% with the acquisition activity of 3.67 mol/ml.menit.Keyword: papaya, lipase, incubation time, optimum pH, substrate concentration.

Immobilization of chymotrypsin (E.C.3.4.21.1), subtilisin (E.C.3.4.21.14) and neutral proteinase from Bacillus subtilis by covalent binding to benzoquinone-activated pearl cellulose

1983 ◽  
Vol 48 (10) ◽  
pp. 2874-2878 ◽  
Author(s):  
Helena Škachová ◽  
Jiří Kučera
Keyword(s):  
Activation Energy ◽  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Substrate Concentration ◽  
Covalent Binding ◽  
Neutral Proteinase

Chymotrypsin (E.C.3.4.21.1), subtilisin (E.C.3.4.21.14), and a neutral proteinase from Bacillus subtilis were immobilized by covalent binding to benzoquinone-activated pearl cellulose. The yield of the immobilized protein was 55% in the case of chymotrypsin and 50% in the case of subtilisin and neutral proteinase from B. subtilis. The determination of activation energy at a low substrate concentration showed that the enzyme activity is limited by diffusion under these conditions. The activity yields are generally very good yet the activity of the enzymes immobilized is relatively low, most likely because of the presence of benzoquinone, as shown in experiments with the immobilization of chymotrypsin by the same technique on supports with different hydrophilicity.

Rat prostatic acid phosphatase: androgenic control of isoelectric focusing patterns

1983 ◽  
Vol 61 (7) ◽  
pp. 744-749 ◽  
Author(s):  
J. Downey ◽  
D. Mahan ◽  
T. G. Flynn ◽  
C. E. Bird ◽  
A. F. Clark
Keyword(s):  
Enzyme Activity ◽  
Acid Phosphatase ◽  
Isoelectric Focusing ◽  
Specific Activity ◽  
Electrophoretic Pattern ◽  
Prostatic Acid Phosphatase ◽  
Staining Intensity ◽  
Adult Rats ◽  
Enzyme Specific Activity ◽  
Ph Range

To further characterize the androgen dependence of prostatic acid phosphatase (AP), the isoelectric focusing patterns of enzyme activity have been examined for normal and castrated adult rats and for rats receiving androgen injections. Isoelectric focusing was performed in polyacrylamide gels over the pH range 4–8. Naphthyl phosphate was used as substrate for staining. For normal rats there was a single lysosomal band (isoelectric point (pI) = 7.35 ± 0.04), four closely migrating secretory bands (pI = 5.96–5.63), and an androgen-dependent band (pI = 6.37 ± 0.05) which as yet has not been identified as either lysosomal or secretory. Following castration the secretory bands decreased significantly in staining intensity, the androgen-dependent band disappeared, and two new lysosomal bands (pI's = 7.13 ± 0.03 and 7.00 ± 0.03) appeared. With androgen replacement the latter two bands disappeared, the androgen-dependent band reappeared, and the secretory bands increased in staining intensity but with the most anodic of the four appearing before the others. This suggests that it could be a precursor to the others. The isoelectric focusing patterns of AP activity appear to be a better method of assessing the androgen status of the prostate than are the previously used parameters, namely, enzyme specific activity, degree of inhibition by tartrate, and polyacrylamide gel electrophoretic pattern.

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