Study on Enzymatic Characteristics of Chitin Deacetylase

2011 ◽  
Vol 236-238 ◽  
pp. 996-999 ◽  
Author(s):  
Jun Ang Liu ◽  
Yuan Hao He
Keyword(s):  
Inhibitory Effect ◽  
Enzymatic Properties ◽  
Optimum Temperature ◽  
Chitin Deacetylase ◽  
Activation Effect ◽  
High Productivity ◽  
Enzymatic Characteristics ◽  
Optimum Ph

Chitin deacetylase (CDA) catalyzes the conversion of chitin to chitosan by the deacetylation of N-acetyl-D-glucosamine residues. The results of the fundamental enzymatic properties of chitin deacetylase producing from the high productivity chitin deacetylase strain Z7 show that, the optimum temperature of strain Z7 was 40°C, the optimum pH was 6.5, under the concentration of 1mmol/L, Mg2+, K+, Ca2+and Fe2+had activation effect, of which the strongest activation effect was Mg2+. Pb2+, Cu2+and Mn2+had inhibitory effect, of which the strongest inhibitory effect was Mn2+.

Isolation and Identification of Strains with High Chitin Deacetylase Activity

2012 ◽  
Vol 457-458 ◽  
pp. 476-479
Author(s):  
Jing Xuan Gou ◽  
Wen Bin Dong ◽  
Qiao Zeng ◽  
Jing Jing Zhang
Keyword(s):  
Food Industry ◽  
Analysis Data ◽  
Soil Samples ◽  
Optimum Temperature ◽  
Isolation And Identification ◽  
Chitin Deacetylase ◽  
Physiological And Biochemical Characteristics ◽  
Optimum Ph ◽  
Physiological And Biochemical ◽  
Rdna Analysis

Chitosan is an aboundant biopolymer like cellose. To bioprocess them with chitin deacetylase (CDA), the products will be used in medicine and food industry. [In order to get new strains with significant ability of (CDA) Twenty eight strains producing CDA were isolated and screened out from the soil samples by color reaction in plate medium. The strain F2-7-3 was screened out from these strains for the highest CDA activity, which can reach more than 250U/mL. The paranitroacetanilide was used as the substrate, the optimum temperature for enzyme activity was determined to be 50°C and the optimum pH was 7.0. It was studied by method of morphological, physiological and biochemical characteristics and 16S rDNA analysis. Data shows that the strain was Rhodococcus sp.

scholarly journals SEMI PURIFIKASI DAN KARAKTERISASI ENZIM PROTEASE Bacillus sp.

2007 ◽  
Vol 13 (1) ◽  
pp. 51-56 ◽  
Author(s):  
Elidar Naiola ◽  
Nunuk Widhyastuti
Keyword(s):  
Metal Ions ◽  
Gel Filtration ◽  
Liquid Waste ◽  
Enzyme Reaction ◽  
Inhibitory Effect ◽  
Crude Enzyme ◽  
Bacillus Sp ◽  
Optimum Temperature ◽  
Optimum Ph ◽  
Specific Activities

The aim of the research was to find the partial purified of enzyme protease from Bacillus sp. The crude enzyme of protease was produce in rice brand medium (100 gram of rice brand in a liter tofu liquid waste). The enzyme was semi-purified by the procedure of precipitation using ethanol in different percentages of saturation, gel filtration using Sephadex G 100 and Ion Exchanged Chromatography using DEAE Sephadex A50. Specific activities of the enzyme during purification were 5.71 U/mg (crude enzyme); 6.75 U/mg (ethanol precipitations); 37.16 U/mg (gel filtration) and 43.02 U/mg (Ion Exchanged Chromatography). The optimum temperature for enzyme reaction was 45–50 °C, while the optimum pH was 7.0–8.0. Protease was relatively stable after heating until 37–50 °C for 60 minutes. Metal ions had different effects to the enzyme. CaCl2, FeCl3, MnCl2, ZnCl2 and MgCl2 increased enzyme activity, CdCl2 and HgCl2 gave an inhibitory effect, and another of metal ions had no effects to the enzyme.

Preparation of Genipin by Hydrolysis of Geniposide with Co-Immobilized Enzyme

2011 ◽  
Vol 236-238 ◽  
pp. 1793-1798 ◽  
Author(s):  
Hua Zheng Liang ◽  
He Chen ◽  
Jian Feng Wang ◽  
Yu Lan He
Keyword(s):  
High Performance ◽  
Immobilized Enzyme ◽  
Low Cost ◽  
Enzymatic Properties ◽  
High Yield ◽  
Cross Linking ◽  
Optimum Temperature ◽  
Environmental Friendly ◽  
Optimum Ph ◽  
Hydrolysis Of

Co-immobilize enzyme by cross-linking and embedding, optimize conditions for immobilizing, determinate the enzymatic properties of co-immobilized enzyme and study the methods for preparation of genipin using co-immobilized enzyme to hydrolyze geniposide. Optimized immobilizing conditions include glutaraldehyde concentration being 0.15%, cross-linking temperature being 20°C, cross-linking time being 2 hours, the activity of co-immobilized β-glucosidase and cell reaches to 65.33U/mg and the enzyme activity recovery being 52.63%. Enzymatic properties of co-immobilized enzyme are following: optimum temperature is 55°C and optimum pH is 5.0. The transformation experiments are carried out with co-immobilized enzyme. The results show that half-life of co-immobilized enzyme reaches around 40 days, higher than the normal immobilized enzyme. The conversion rate of geniposide is above 95% after 8 hours. The genipin is isolated, purified and recrystallized to reach more than 98% of purity by High Performance Liquid Chromatography. Advantages to prepare genipin using co-immobilized enzyme include low cost, high yield, environmental friendly and easy to manufacturing.

Screening of the Bacterium for Chlorobenzene Degradation and its Enzymatic Properties

2012 ◽  
Vol 610-613 ◽  
pp. 404-408
Author(s):  
Xian Niu ◽  
Cheng Ding ◽  
Jin Long Yan ◽  
Bai Ren Yang
Keyword(s):  
Enzyme Purification ◽  
Extracellular Enzymes ◽  
Ph Value ◽  
Morphological Characteristics ◽  
Enzymatic Properties ◽  
Purification Process ◽  
Optimum Temperature ◽  
16S Rdna Sequence ◽  
Sds Page ◽  
Optimum Ph

A dominant bacterium (LW13) for the degradation of chlorobenzene was selected from maturity sludge in a novel combined bio-filter polluted by chlorobenzene gas. Based on the morphological characteristics observation, physio-biochemical characteristics and 16S rDNA sequence homology analysis, strain LW13 was identified as Lysinibacillus fusiformis. Crude enzyme from the fermentation was extracted and their enzymatic properties were also investigated. Results showed that the degradation enzyme produced by the bacteria belong to extracellular enzymes. The purity of the enzyme was determined by SDS-PAGE gel electrophoresis and the molecular weight was found to be 52 kDa. The optimum pH value was about 8.0 with the optimum temperature of 45° C. Throughout the purification process, 85-fold of enzyme purification was achieved with the recovery of 20.69%.

Immobilization and Characterization of Tannase and its Haze-removing

2009 ◽  
Vol 15 (6) ◽  
pp. 545-552 ◽  
Author(s):  
Erzheng Su ◽  
Tao Xia ◽  
Liping Gao ◽  
Qianying Dai ◽  
Zhengzhu Zhang
Keyword(s):  
Kinetic Parameter ◽  
High Activity ◽  
Green Tea ◽  
Storage Stability ◽  
Residual Activity ◽  
Black Tea ◽  
Optimum Temperature ◽  
Oolong Tea ◽  
Optimum Ph

Tannase was effectively immobilized on alginate by the method of crosslinking-entrapment-crosslinking with a high activity recovery of 76.6%. The properties of immobilized tannase were investigated. Its optimum temperature was determined to be 35 ° C, decreasing 10 °C compared with that of free enzyme, whereas the optimum pH of 5.0 did not change. The thermal and pH stabilities of immobilized tannase increased to some degree. The kinetic parameter, Km, for immobilized tannase was estimated to be 11.6 × 10-4 mol/L. Fe2+ and Mn2+ could activate the activity of immobilized tannase. The immobilized tannase was also applied to treat the tea beverage to investigate its haze-removing effect. The content of non-estern catechins in green tea, black tea and oolong tea increased by 52.17%, 12.94% and 8.83%, respectively. The content of estern catechins in green tea, oolong tea and black tea decreased by 20.0%, 16.68% and 5.04%, respectively. The anti-sediment effect of green tea infusion treated with immobilized tannase was significantly increased. The storage stability and reusability of the immobilized tannase were improved greatly, with 72.5% activity retention after stored for 42 days and 86.9% residual activity after repeatedly used for 30 times.

Charakterisierung und Kinetik des in der Rattenplacenta vorkommenden mikrosomalen Enzyms, das den Wasserstoff-Transfer von Oestradiol auf Androstendion katalysiert / Characterization and Kinetics of the Microsomal Enzyme of Rat Placenta which Functions as a “Transhydrogenase” between Estradiol-17β and Androstenedione

1971 ◽  
Vol 26 (7) ◽  
pp. 710-719 ◽  
Author(s):  
Kunhard Pollow ◽  
Barbara Pollow
Keyword(s):  
Hydrogen Transfer ◽  
Microsomal Fraction ◽  
Close Relation ◽  
Inhibitory Effect ◽  
Magnesium Ions ◽  
Michaelis Constant ◽  
Temperature Optimum ◽  
Optimum Ph ◽  
Kinetics Of ◽  
Estradiol 17Β

The microsomal fraction of rat placenta contains a 17β-hydroxysteroid-oxidoreductase which transfers hydrogen from position 17 of estradiol to androstenedione. This hydrogen transfer is dependent on NAD, NADP as cofactor is without effect. The optimum pH is at 6,9. In the presence of NAD the Michaelis constant for estradiol is 4,17 · 10-5м at pH 7,4. In the presence of androstenedione in the incubation medium the Km-value for estradiol is decreased, which indicates an increased affinity for the enzyme. The temperature optimum of the enzyme is 38 °C. Addition of SH-blocking agents inhibited the enzyme activity. Zinc and magnesium ions had an inhibitory effect on the “transhydrogenase” and B-NADPT specifically labelled from [1-T]-glucose showed that the non-effect of NADP on transhydrogenation from estradiol to androstenedione resulting in reduction of position 17 is not due to different stereospecifity.The results show a close relation between the oxidative metabolism of estradiol and the reduction of androstenedione, indicating that estradiol-17β, as the preferred hydrogen-donating substrate, is an essential component of the androstenedione-hydrogenating system in the microsomal fraction of rat placenta.

scholarly journals Properties of a new fungal b-galactosidase with potential application in the dairy industry

1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  
Keyword(s):  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Transferase Activity ◽  
Optimum Temperature ◽  
Milk Whey ◽  
Beneficial Effects ◽  
Optimum Ph ◽  
Semi Solid ◽  
Good Productivity ◽  
Hydrolysis Of

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.

scholarly journals Characterization of Biosynthetic Enzymes for Ectoine as a Compatible Solute in a Moderately Halophilic Eubacterium, Halomonas elongata

1999 ◽  
Vol 181 (1) ◽  
pp. 91-99 ◽  
Author(s):  
Hisayo Ono ◽  
Kazuhisa Sawada ◽  
Nonpanga Khunajakr ◽  
Tao Tao ◽  
Mihoko Yamamoto ◽  
...  
Keyword(s):  
Molecular Mass ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Apparent Molecular Mass ◽  
Optimum Temperature ◽  
Sds Page ◽  
Halomonas Elongata ◽  
Optimum Ph

ABSTRACT 1,4,5,6-Tetrahydro-2-methyl-4-pyrimidinecarboxylic acid (ectoine) is an excellent osmoprotectant. The biosynthetic pathway of ectoine from aspartic β-semialdehyde (ASA), in Halomonas elongata, was elucidated by purification and characterization of each enzyme involved. 2,4-Diaminobutyrate (DABA) aminotransferase catalyzed reversively the first step of the pathway, conversion of ASA to DABA by transamination with l-glutamate. This enzyme required pyridoxal 5′-phosphate and potassium ions for its activity and stability. The gel filtration estimated an apparent molecular mass of 260 kDa, whereas molecular mass measured by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) was 44 kDa. This enzyme exhibited an optimum pH of 8.6 and an optimum temperature of 25°C and had Km s of 9.1 mM forl-glutamate and 4.5 mM for dl-ASA. DABA acetyltransferase catalyzed acetylation of DABA to γ-N-acetyl-α,γ-diaminobutyric acid (ADABA) with acetyl coenzyme A and exhibited an optimum pH of 8.2 and an optimum temperature of 20°C in the presence of 0.4 M NaCl. The molecular mass was 45 kDa by gel filtration. Ectoine synthase catalyzed circularization of ADABA to ectoine and exhibited an optimum pH of 8.5 to 9.0 and an optimum temperature of 15°C in the presence of 0.5 M NaCl. This enzyme had an apparent molecular mass of 19 kDa by SDS-PAGE and a Km of 8.4 mM in the presence of 0.77 M NaCl. DABA acetyltransferase and ectoine synthase were stabilized in the presence of NaCl (>2 M) and DABA (100 mM) at temperatures below 30°C.

scholarly journals Immobilization of Isolated Lipase From Moldy Copra(Aspergillus Oryzae)

2011 ◽  
Vol 8 (2) ◽  
pp. 896-902
Author(s):  
Seniwati Dali ◽  
A. B. D. Rauf Patong ◽  
M. Noor Jalaluddin ◽  
Pirman ◽  
Baharuddin Hamzah
Keyword(s):  
Thermal Stability ◽  
Aspergillus Oryzae ◽  
Immobilized Lipase ◽  
Optimum Temperature ◽  
Adsorption Method ◽  
Ph Optimum ◽  
Optimum Ph ◽  
Recovery Technique ◽  
Free Lipase

Enzyme immobilization is a recovery technique that has been studied in several years, using support as a media to help enzyme dissolutions to the reaction substrate. Immobilization method used in this study was adsorption method, using specific lipase fromAspergillus oryzae. Lipase was partially purified from the culture supernatant ofAspergillus oryzae. Enzyme was immobilized by adsorbed on silica gel. Studies on free and immobilized lipase systems for determination of optimum pH, optimum temperature, thermal stability and reusability were carried out. The results showed that free lipase had optimum pH 8,2 and optimum temperature 35 °C while the immobilized lipase had optimum 8,2 and optimum temperature 45 °C. The thermal stability of the immobilized lipase, relative to that of the free lipase, was markedly increased. The immobilized lipase can be reused for at least six times.

scholarly journals Preparation of Cross-Linked Enzyme Aggregates (CLEAs) of an Inulosucrase Mutant for the Enzymatic Synthesis of Inulin-Type Fructooligosaccharides

Catalysts ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 641 ◽  
Author(s):  
Thanapon Charoenwongpaiboon ◽  
Rath Pichyangkura ◽  
Robert A. Field ◽  
Manchumas Hengsakul Prousoontorn
Keyword(s):  
Enzymatic Synthesis ◽  
Biochemical Characterization ◽  
Lactobacillus Reuteri ◽  
Soluble Enzyme ◽  
Optimum Temperature ◽  
Optimum Conditions ◽  
Product Specificity ◽  
Product Characterization ◽  
Optimum Ph ◽  
Probiotic Activity

Fructooligosaccharides are well-known carbohydrate molecules that exhibit good probiotic activity and are widely used as sweeteners. Inulin-type fructooligosaccharides (IFOs) can be synthesized from sucrose using inulosucrase. In this study, cross-linked enzyme aggregates (CLEAs) of Lactobacillus reuteri 121 inulosucrase (R483A-LrInu) were prepared and used as a biocatalyst for IFOs production. Under optimum conditions, R483A-LrInu CLEAs retained 42% of original inulosucrase activity. Biochemical characterization demonstrated that the optimum pH of inulosucrase changed from 5 to 4 after immobilization, while the optimum temperature was unchanged. Furthermore, the pH stability and thermostability of the R483A-LrInu CLEAs was significantly improved. IFOs product characterization indicated that the product specificity of the enzyme was impacted by CLEA generation, producing a narrower range of IFOs than the soluble enzyme. In addition, the R483A-LrInu CLEAs showed operational stability in the batch synthesis of IFOs.

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