scholarly journals Utilization of Crude Intracellular Chitinase Enzyme from Providencia stuartii for Glucosamine Production from Shrimp Shells

REAKTOR ◽  
2019 ◽  
Vol 19 (2) ◽  
pp. 62-67
Author(s):  
Hardoko Hardoko ◽  
Titri Siratantri Mastuti ◽  
Desy Puspasari ◽  
Yuniwaty Halim
Keyword(s):  
Optimum Condition ◽  
Substrate Concentration ◽  
Intracellular Enzyme ◽  
Fermentation Time ◽  
Shrimp Shells ◽  
Optimum Ph ◽  
Chitin Hydrolysis ◽  
Providencia Stuartii ◽  
Optimum Ph And Temperature

Chitin hydrolysis using enzyme is one of the methods to produce glucosamine in shorter time compared to using microbial cells, but the ability to produce glucosamine at enzyme’s optimum condition is influenced by substrate concentration and fermentation time. The objective of this research was to determine the optimum substrate concentration and fermentation time of shrimp shells’ chitin to produce glucosamine at the optimum pH and temperature of crude intracellular chitinase enzyme from Providencia stuartii. Method used was experimental method, started by extraction of intracellular enzyme from P. stuartii, followed by determination of optimum pH and temperature of enzyme. The optimum condition was used for experiment of shrimp shells’ chitin fermentation with treatments of chitin substrate concentration (0.5; 1.0; 1.5; 2.0%) and fermentation time (2, 4, 6 and 24 hours). Results showed that optimum enzyme activity occurred at pH of 5.0 and temperature of 40oC, which was about 6.03 U/ml. Concentration of chitin substrate and fermentation time influenced the amount of glucosamine obtained. Fermentation of shrimp shells’ chitin using crude intracellular enzyme was optimum at 1.0% substrate concentration and 6 hours fermentation time, which produced glucosamine about 1680.06±58.49 ppm. Keywords: intracellular chitinase enzyme, glucosamine, shrimp shells’ chitin, P. stuartii

scholarly journals Production of N-acetylglucosamine from shrimp shells’ chitin using intracellular chitinase from Mucor circinelloides

Food Research ◽  
2020 ◽  
Vol 4 (5) ◽  
pp. 1582-1587
Author(s):  
Yuniwaty Halim ◽  
Fransiska ◽  
Hardoko ◽  
R. Handayani
Keyword(s):  
Incubation Period ◽  
Substrate Concentration ◽  
Chitinase Activity ◽  
Mucor Circinelloides ◽  
Optimum Temperature ◽  
Shrimp Shells ◽  
Incubation Periods ◽  
Optimum Ph ◽  
Substrate Concentrations ◽  
Optimum Ph And Temperature

Chitin is a natural biopolymer found in shrimp shells and can be processed into Nacetylglucosamine which is extensively used as a dietary supplement to treat osteoarthritis, back pain and knee pain. This research was conducted to determine the optimum pH, temperature, substrate concentration and incubation period to produce Nacetylglucosamine using crude and semi pure intracellular chitinase extracted from Mucor circinelloides. Chitinase activity was measured to determine optimum pH and temperature by using various pHs (3, 4, 5, 6, 7, 8 and 9) and temperatures (30oC, 40oC, 50oC, 60oC, 70oC and 80oC). Different substrate concentrations (0.5%, 1.0%, 1.5% and 2.0%) and incubation periods (2, 4, 6 and 24 hrs) were used to determine the optimum condition to produce N-acetylglucosamine. Results showed that crude intracellular chitinase had an optimum pH of 5 with chitinase activity of 4.16±0.07 U/mL and optimum temperature of 60oC with chitinase activity of 4.22±0.07 U/mL. The optimum substrate concentration obtained was 0.5% and the optimum incubation period obtained was 6 hrs with about 961.67±9.13 ppm N-acetylglucosamine produced. Semi pure intracellular chitinase had an optimum pH of 4 with chitinase activity of 4.75±0.09 U/mL and optimum temperature of 50oC with chitinase activity of 5.03±0.08 U/mL. The optimum substrate concentration obtained was 1.5% and the optimum incubation period obtained was 4 hrs with about 1150.56±12.55 ppm N-acetylglucosamine produced.

A new method for the adaptive determination of optimum pH and temperature

1989 ◽  
Vol 33 (11) ◽  
pp. 1419-1424 ◽  
Author(s):  
Jeff. L Harmon ◽  
Gerasimos Lyberatos ◽  
Spyros A. Svoronos
Keyword(s):  
New Method ◽  
Optimum Ph ◽  
Optimum Ph And Temperature

Study on the Optimum Condition for Immobilization and Properties of Laccase on Coordinated Chitosan-Cu2+

2013 ◽  
Vol 864-867 ◽  
pp. 1262-1265 ◽  
Author(s):  
Bo Yang ◽  
Xu Ming Wang
Keyword(s):  
Optimum Condition ◽  
Heat Resistance ◽  
High Activity ◽  
Storage Stability ◽  
Optimal Conditions ◽  
Immobilized Laccase ◽  
Complex Time ◽  
Optimum Ph ◽  
Polymeric Coordination ◽  
Optimum Ph And Temperature

Coordinated chitosan-Cu2+ as a carrier, the laccase was immobilized on it by polymeric coordination method. In this study, the optimal conditions for immobilization and properties of laccase were investigated. The optimal conditions for immobilization were: CuSO4 (0.05 mol/L), complex time (7 h), laccase concentration (250 U/mL), immobilization time (8 h). Under this condition, the activity of immobilized laccase can reach 820 U/g. In comparison with the free laccase, the optimum pH and temperature of immobilized laccase have a little change, while the heat resistance and pH stability were improved. After the immobilized laccase was stored in the refrigerator at 4 °C for 25 days, the activity of it remained 69.5 % of the original, it illustrates the immobilized laccase has a good storage stability. The laccase immobilized with chitosan-Cu2+ has high activity and has potential to use in industry as a biocatalyst.

A new method for the adaptive determination of optimum pH and temperature

1989 ◽  
Vol 34 (7) ◽  
pp. 1022-1022
Author(s):  
Jeff. L. Harmon ◽  
Gerasimos Lyberatos ◽  
Spyros A. Svoronos
Keyword(s):  
New Method ◽  
Optimum Ph ◽  
Optimum Ph And Temperature

scholarly journals Determination of Optimal Fermentation Condition for N-acetylglucosamine Production Using Mucor circinelloides Extracellular Chitinase

2019 ◽  
Vol 21 (2) ◽  
pp. 105
Author(s):  
Yuniwaty Halim ◽  
Hardoko Hardoko ◽  
Reinald Febryanto Pengalila
Keyword(s):  
Enzyme Activity ◽  
Experimental Method ◽  
Substrate Concentration ◽  
Chitinase Activity ◽  
Mucor Circinelloides ◽  
Fermentation Condition ◽  
Optimal Temperature ◽  
Fermentation Time ◽  
Optimal Ph

This research aimed to determine the best fermentation condition, consists of pH, temperature, fermentation time and substrate concentration, in N-acetylglucosamine production from shrimp shells using crude extracellular chitinase obtained from Mucor circinelloides mould. The method used was experimental method with fermentation treatment of different pH (5, 6, 7, 8 and 9) and temperature (30, 40, 50, 60, 70 and 80°C). The optimal pH and temperature of fermentation obtained was used to determine the maximum substrate concentration (0.5, 1, 1.5 and 2%) and fermentation time (2, 4, 6 and 24 hours) to produce the highest concentration of N-acetylglucosamine. The optimal pH for fermentation was 8, with chitinase activity of 4.38±0.06 U/ml, while the optimal temperature was 50°C with enzyme activity of 5.42±0.06 U/ml. Substrate concentration and fermentation time affected the N-acetylglucosamine production. The optimal fermentation condition was obtained with substrate concentration of 1.5% and fermentation time of 2 hours resulted to N-acetyl Glucosamine concentration of 2195.83±15.14 ppm.

scholarly journals PEMBUATAN DEKSTRIN DARI PATI UBI KAYU MENGGUNAKAN ENZIM AMILASE DARI AZOSPIRILLUM sp. JG3 DAN KARAKTERISASINYA

Molekul ◽  
2010 ◽  
Vol 5 (1) ◽  
pp. 15 ◽  
Author(s):  
Dian Riana Ningsih ◽  
Ari Asnani ◽  
Amin Fatoni
Keyword(s):  
Moisture Content ◽  
Optimum Condition ◽  
Water Content ◽  
Substrate Concentration ◽  
Manihot Esculenta ◽  
Cassava Starch ◽  
Ash Content

Amylase enzyme is used to hydrolyze starch into simpler molecules such as dextrin. Amylase can be isolated fromAzospirillum sp. JG3 bacteria. The purpose of this study was to characterize dextrins from cassava starch (Manihot esculenta) is catalyzed by the enzyme amylase from Azospirillum sp. JG3 bacteria. Stages of this study are: determination of optimum substrat and to analyze the chemical and physical dextrins including moisture content, ash content, dexstrosa equivalent (DE) and the yield obtained. The result of this research showed that optimum condition hydrolysis starch of cassava that using amylase from Azospirillium sp. JG3 bacteria was acquired at substrate concentration 3% and the results of analysis obtained dextrins include yield of 96.67%, water content of 9.39%, 0.25% ash content and dexstrosa equivalent (DE) of 16.55.

Respirometry for determination of the influents SS-concentration

1996 ◽  
Vol 33 (1) ◽  
pp. 311-323 ◽  
Author(s):  
A. Witteborg ◽  
A. van der Last ◽  
R. Hamming ◽  
I. Hemmers
Keyword(s):  
Experimental Design ◽  
Activated Sludge ◽  
Substrate Concentration ◽  
Full Scale ◽  
Activated Sludge Process ◽  
Respiration Rates ◽  
On Line ◽  
Large Measurement ◽  
Set Up

A method is presented for determining influent readily biodegradable substrate concentration (SS). The method is based on three different respiration rates, which can be measured with a continuous respiration meter which is operated in a cyclic way. Within the respiration meter nitrification is inhibited through the addition of ATU. Simulations were used to develop the respirometry set-up and decide upon the experimental design. The method was tested as part of a large measurement programme executed at a full-scale plant. The proposed respirometry set-up has been shown to be suitable for a semi-on-line determination of an influent SS which is fully based on the IAWQ #1 vision of the activated sludge process. The YH and the KS play a major role in the principle, and should be measured directly from the process.

Alkaline phosphatase. I. Kinetics and inhibition by levamisole of purified isoenzymes from humans.

1976 ◽  
Vol 22 (7) ◽  
pp. 972-976 ◽  
Author(s):  
H Van Belle
Keyword(s):  
Alkaline Phosphatase ◽  
Substrate Concentration ◽  
Human Liver ◽  
Alkaline Phosphatases ◽  
Mechanism Of Inhibition ◽  
Optimum Ph ◽  
Alkaline Phosphatase Isoenzymes

Abstract I studied the kinetics and sensitivity toward inhibition by levamisole and R 8231 of the most important human alkaline phosphatase isoenzymes. N-Ethylaminoethanol proved superior to the now widely used diethanolamine buffer, especially for the enzymes from the intestine and placenta, behaving as an uncompetitive activator. The optimum pH largely depends on the substrate concentration. The addition of Mg2+ has no effect on the activities. The meaning of Km-values for alkaline phosphatases is questioned. Isoenzymes from human liver, bone, kidney, and spleen are strongly inhibited by levamisole or R 8231 at concentrations that barely affect the enzymes from intestine or placenta. The inhibition is stereospecific, uncompetitive, and not changed by Mg2+. Inhibition is counteracted by increasing concentrations of N-ethylaminoethanol. The mechanism of inhibition is suggested to be formation of a complex with the phosphoenzyme.

scholarly journals The determination of binding parameters when the total and free substrate concentrations are not approximately equal

1979 ◽  
Vol 179 (3) ◽  
pp. 697-700 ◽  
Author(s):  
N Gains
Keyword(s):  
Substrate Concentration ◽  
Graphical Method ◽  
Enzyme Concentration ◽  
Binding Parameters ◽  
Free Concentration ◽  
Equilibrium Binding ◽  
Substrate Concentrations

By using a standard graphical method values of Km and V may be found that are independent of the conditions and assumptions that the total substrate concentration approximates to its free concentration and that Km is much larger than the enzyme concentration. The procedure is also applicable to the determination of equilibrium binding parameters of a ligand to a macromolecule.

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