scholarly journals A novel Thermothelomyces heterothallicus PA2S4T fungus isolated from the soil induces chitinase production using orange peel flour

2021 ◽  
Vol 17 (9) ◽  
Author(s):  
Victoria Pommer ◽  
Paula Daniela Helfenstein Rother ◽  
Letícia Mara Rasbold ◽  
José Luis Da Conceição Silva ◽  
Alexandre Maller ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Carbon Sources ◽  
Orange Peel ◽  
Biotechnological Application ◽  
Optimum Ph ◽  
Chitinase Production ◽  
Stationary Conditions ◽  
Agricultural Industries ◽  
Optimum Ph And Temperature

Chitinases are enzymes capable of hydrolysing the β-1,4 bonds of chitin releasing chitooligosaccharides and N-acetylglucosamine and are widely used in food, pharmaceutical, and agricultural industries. Microorganisms are potential producers of this enzyme; however, there are no reports in the literature on the production of chitinase by fungi of the genus Thermothelomyces. Thus, this work aimed to investigate the production of extracellular chitinase using alternative carbon sources by the fungus isolated from soil, Thermothelomyces heterothallicus PA2S4T. The fungus was cultivated in a liquid medium supplemented with carbon sources and incubated at 40°C under stationary conditions for seven days. Orange peel flour was the best inducer for extracellular chitinase, with 82.3 U/mL of enzymatic activity. The highest production of chitinase was obtained on the tenth day, and the optimum pH and temperature for enzyme activity were 4.5 and 50ºC, respectively. Therefore, the fungus T. heterothallicus PA2S4T proved to be promising in the production of extracellular chitinase, which presents pH and temperature characteristics favourable to biotechnological application.

Cinnamate-4-Hydroxyiase in Polyporus hispidus

1973 ◽  
Vol 51 (6) ◽  
pp. 731-734 ◽  
Author(s):  
C. P. Vance ◽  
A. M. D. Nambudiri ◽  
G. H. N. Towers
Keyword(s):  
Enzyme Activity ◽  
Enzymatic Activity ◽  
Microsomal Fraction ◽  
Mitochondrial Fraction ◽  
Maximum Activity ◽  
Coumaric Acid ◽  
Free System ◽  
Optimum Ph ◽  
A Cell ◽  
Plant Enzyme

A cell-free system capable of hydroxylating cinnamic acid to p-coumaric acid has been isolated from 10-day-oid cultures of Polyporus hispidus. The enzyme requires NADPH and FAD for maximum activity. Enzyme activity appears to be localized in the microsomal fraction with slight activity occurring in the mitochondrial fraction. The optimum pH for enzymatic activity is 7.5. This is the first report on any properties of this enzyme in a fungus. The enzyme differs from the known plant enzyme in its FAD requirement.

scholarly journals Production of polygalacturonase by Aspergillus niger BC23 isolated from Irvingia gabonensis (African mango) fruit

2016 ◽  
Vol 70 (6) ◽  
pp. 717-724
Author(s):  
Nwokoro Ogbonnaya ◽  
Eze Chukwuemeka
Keyword(s):  
Enzyme Activity ◽  
Aspergillus Niger ◽  
Enzyme Production ◽  
Carbon Sources ◽  
Orange Peel ◽  
Relative Activity ◽  
Maximum Activity ◽  
Citrus Pectin ◽  
Enzyme Productivity ◽  
Irvingia Gabonensis

Polygalacturonase was produced from Aspergillus niger BC 23 which was isolated from spoiled Irvingia gabonensis fruit. The influence of carbon substrates on enzyme production showed that the medium containing sucrose produced a maximum enzyme yield of 38.5 U/mg protein after 72 h. Enzyme productivity in this medium was much higher than in the medium that contained only citrus pectin as the sole carbon source. Medium containing yeast extract as a nitrogen source caused the production of specific enzyme activity of 31.2 U/mg protein. Results on the effect of metal ions on enzyme activity showed that Ca2+ gave a percent relative activity of 214% in comparison to the native enzyme activity. The enzyme showed maximum activity in slight acid and neutral pH media with optimal activity at pH 4.0. Temperature activity profile of the enzyme showed best activity at a temperature of 35?C. Dried fruit peels were tested for their abilities to support enzyme production in a media devoid of citrus pectin. The best enzyme productivity of 102.3 U/mg protein was achieved after 72 h in the medium containing orange peel and this level was much higher than that achieved when pure carbon sources or citrus pectin alone were used for enzyme production.

scholarly journals Streptomyces misionensisPESB-25 Produces a Thermoacidophilic Endoglucanase Using Sugarcane Bagasse and Corn Steep Liquor as the Sole Organic Substrates

2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Marcella Novaes Franco-Cirigliano ◽  
Raquel de Carvalho Rezende ◽  
Mônica Pires Gravina-Oliveira ◽  
Pedro Henrique Freitas Pereira ◽  
Rodrigo Pires do Nascimento ◽  
...  
Keyword(s):  
Response Surface Methodology ◽  
Enzyme Activity ◽  
Sugarcane Bagasse ◽  
Corn Steep Liquor ◽  
Organic Substrates ◽  
Endoglucanase Activity ◽  
Optimum Ph ◽  
Molecular Masses ◽  
Steep Liquor ◽  
Optimum Ph And Temperature

Streptomyces misionensisstrain PESB-25 was screened and selected for its ability to secrete cellulases. Cells were grown in a liquid medium containing sugarcane bagasse (SCB) as carbon source and corn steep liquor (CSL) as nitrogen source, whose concentrations were optimized using response surface methodology (RSM). A peak of endoglucanase accumulation (1.01 U·mL−1) was observed in a medium with SCB 1.0% (w/v) and CSL 1.2% (w/v) within three days of cultivation.S. misionensisPESB-25 endoglucanase activity was thermoacidophilic with optimum pH and temperature range of 3.0 to 3.6 and 62° to 70°C, respectively. In these conditions, values of 1.54 U mL−1of endoglucanase activity were observed. Moreover, Mn2+was demonstrated to have a hyperactivating effect on the enzyme. In the presence of MnSO4(8 mM), the enzyme activity increased threefold, up to 4.34 U·mL−1. Mn2+also improved endoglucanase stability as the catalyst retained almost full activity upon incubation at 50°C for 4 h, while in the absence of Mn2+, enzyme activity decreased by 50% in this same period. Three protein bands with endoglucanase activity and apparent molecular masses of 12, 48.5 and 119.5 kDa were detected by zymogram.

Purification and Properties of an Enzyme Capable of Degrading the Polysaccharide of the Cyanobacterium, Nostoc commune

2002 ◽  
Vol 57 (11-12) ◽  
pp. 1042-1046 ◽  
Author(s):  
◽  
Shin’ichiro Kajiyama ◽  
Atsushi Okazawa ◽  
Ei-ichiro Fukusaki ◽  
Akio Kobayashi
Keyword(s):  
Enzyme Activity ◽  
Amino Acid ◽  
Nostoc Commune ◽  
Terminal Amino Acid ◽  
Degrading Enzyme ◽  
Purification And Properties ◽  
Optimum Ph ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence ◽  
Optimum Ph And Temperature

A novel Nostoc commune-polysaccharide (NPS)-degrading enzyme with a molecular mass of 128.5 kDa was purified from Paenibacillus glycanilyticus DS-1. The optimum pH and temperature of the enzyme activity were 5.5 and 35 °C, respectively. The enzyme completely degraded NPS to oligosaccharides, ranging from tetra to hexasaccharides and could degrade the xylan weakly whereas xanthan, gellan, cellulose, curdlan and p-nitrophenyl-β-ᴅ-xylopyranoside were not degraded. Homology analysis of the N-terminal amino acid sequence of the NPS-degrading enzyme against the PIR and SWISS-PROT databases indicated that the sequence was not homologous to any other polysaccharide-degrading enzyme.

scholarly journals Partial purification and biochemical characterization of amylase from Aeromonas caviaeNK1isolated from Industrial waste of India

2016 ◽  
Vol 7 (1) ◽  
pp. 85
Author(s):  
Kalyani Khanra ◽  
Indranil Choudhuri ◽  
Sudipta Panja ◽  
Nandan Bhattacharyya
Keyword(s):  
Enzyme Activity ◽  
Industrial Waste ◽  
Biochemical Characterization ◽  
Partial Purification ◽  
Ammonium Sulfate Precipitation ◽  
Operational Conditions ◽  
Industrial Utilization ◽  
Optimum Ph ◽  
Optimum Ph And Temperature

<p class="jbls">A partial purification and biochemical characterization of theamylase from <em>Aeromonascaviae</em>NK1 were carried out in this study. The extracellular extract was concentrated using ammonium sulfate precipitation and optimum operational conditions for the enzyme activity from the strain were evaluated. The optimum pH and temperature were observed 11.5 and37<sup>0</sup>C respectively. Ca<sup>2+</sup>, Mn<sup>2+</sup>, Mg<sup>2+</sup>, Zn<sup>2+</sup>, Pb<sup>2+</sup>, Co<sup>2+</sup> were found to have effect on amylase activity.Furthermore, the analysis of kinetic showed that the enzyme has 𝐾<sub>𝑚</sub> of 2.4mg/mL and 𝑉<sub>max</sub> of 21853.0𝜇mol/min/mg for starch. The results indicate that the enzyme reflects their potentiality towards industrial utilization.</p>

scholarly journals Trichoderma Reesei Cellulase Produced by Submerged Versus Solid State Fermentations

2012 ◽  
Vol 69 (2) ◽  
Author(s):  
Diana NEAGU ◽  
Jacqueline DESTAIN ◽  
Phillipe THONART ◽  
Carmen SOCACIU
Keyword(s):  
Solid State ◽  
Trichoderma Reesei ◽  
Wheat Bran ◽  
Solid State Fermentation ◽  
Enzyme Production ◽  
Carbon Sources ◽  
Production Yield ◽  
Trichoderma Sp ◽  
Optimum Ph ◽  
Optimum Ph And Temperature

The aim of this study was to produce and characterize a cellulase-rich fraction using submerged or solid state fermentation of Trichoderma reesei (QM 1914) strain. The carbon sources were the wheat bran or sawdust, the production yield of this enzyme production was higher in both fermentation types using sawdust substrate, and especially by solid state fermentation, after five days of fermentation. The optimum pH and temperature for the efficient crude enzyme production was established to be 5 and 60°C, respectively, but lost 50% of its activity after 30 minutes, when heated at 60°C. Comparatively with other fungi, the efficiency of Trichoderma sp. to synthesize cellulase rich extract was higher. 

scholarly journals Partial purification and characterization of an endo-α-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242

1992 ◽  
Vol 288 (2) ◽  
pp. 475-482 ◽  
Author(s):  
I Ishii-Karakasa ◽  
H Iwase ◽  
K Hotta ◽  
Y Tanaka ◽  
S Omura
Keyword(s):  
Enzyme Activity ◽  
Culture Medium ◽  
Gel Filtration ◽  
Partial Purification ◽  
Gastric Mucus ◽  
Purification And Characterization ◽  
Streptomyces Sp ◽  
Optimum Ph ◽  
New Type

For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberated from PGM were pyridylaminated, and the reducing terminal sugars of oligosaccharides larger than Gal beta 1-3GalNAc were analysed by h.p.1.c. The crude enzyme of endo-GalNAc-ase-S was prepared as an 80% (w/v) ammonium sulphate precipitate from the concentrated culture medium. The enzyme was partially purified by gel chromatofocusing and subsequent DEAE-Toyopearl chromatography. Endo-enzyme activity eluted around pI 4.8 on a gel chromatofocusing column and eluted with 0.19-0.25 M-NaCl on a DEAE-Toyopearl column. In the enzyme fraction obtained, no exo-glycosidases or proteases could be detected. The molecular mass of the enzyme was estimated as 105 kDa by gel filtration, and the optimum pH was 5.5. Endo-GalNAc-ase-S hydrolysed the O-glycosidic linkage between GalNAc and Ser (Thr) in 3H-labelled and unlabelled asialofetuin, liberating both the disaccharide (Gal beta 1-3GalNAc) and the tetrasaccharide [Gal beta 1-3 (Gal beta 1-4GlcNAc beta 1-6)GalNAc]. When endo-alpha-N-acetylgalactosaminidase from Alcaligenes sp. (endo-GalNac-ase-A) was incubated with 3H-labelled and unlabelled asialofetuin, only the disaccharide (Gal beta 1-3GalNAc) was liberated.

Effect of temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37

2021 ◽  
Vol 66 (1) ◽  
pp. 72-79
Author(s):  
Thuoc Doan Van ◽  
Hung Nguyen Phuc
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Animal Feed ◽  
Culture Conditions ◽  
Effect Of Temperature ◽  
Physical Parameters ◽  
Original Activity ◽  
Optimum Ph ◽  
Production Activity ◽  
Ph Range

The effect of physical parameters such as temperature and pH on the production, activity, and stability of α-amylase from Bacillus subtilis V37 was investigated. The results indicated that the optimum culture conditions for enzyme activity were pH 7.0 and 35 oC. The optimum pH and temperature for enzyme activity were 6.0 and 70 oC. The crude enzyme was found to be stable in the pH range of 5.0 to 7.0. The enzyme was stable for 1 h at a temperature from 30 to 80 oC; nearly 100% of enzyme activity remained at temperatures of 30 - 40 oC, and about 34% of original activity remained at a temperature of 80 oC. These features demonstrated that α-amylase from B. subtilis V37 can be applied in many areas such as the food, fermentation, and animal feed industries.

β-GLUCURONIDASE OF RABBIT POLYMORPHONUCLEAR LEUCOCYTES

1950 ◽  
Vol 28e (3) ◽  
pp. 69-79 ◽  
Author(s):  
R. J. Rossiter ◽  
Esther Wong
Keyword(s):  
Enzyme Activity ◽  
Blood Plasma ◽  
Substrate Concentration ◽  
Final Concentration ◽  
White Cell ◽  
Polymorphonuclear Leucocytes ◽  
Michaelis Constant ◽  
Glucuronidase Activity ◽  
Arsanilic Acid ◽  
Optimum Ph

Rabbit polymorphonuclear leucocytes contain an enzyme capable of hydrolyzing biosynthetic phenolphthalein mono-β-glucuronide. The concentration of the enzyme in the white cell is some 2000 times the concentration of the enzyme in the blood plasma. Under the conditions of study, the β-glucuronidase activity was proportional to the concentration of the enzyme. The effect of substrate concentration on the enzyme activity was studied and the Michaelis constant, Ks, determined. The course of the reaction was linear with time for the first 12 hr. and then fell off slightly during the next 12 hr. The optimum pH of the enzyme was 4.45 in either 0.2 M acetate or 0.2 M phthalate buffer. It was not inhibited by cyanide, azide, iodoacetate, fluoride, glycine, thiourea, urethane, arsanilic acid, acetophenone, o-cresol or m-cresol, in a final concentration of 0.01 M. The possible function of β-glucuronidase in rabbit polymorphonuclear leucocytes is discussed.

scholarly journals Immobilization of alpha-amylase produced by Bacillus circulans GRS 313

2003 ◽  
Vol 46 (2) ◽  
pp. 167-176 ◽  
Author(s):  
Gargi Dey ◽  
Singh Bhupinder ◽  
Rintu Banerjee
Keyword(s):  
Calcium Alginate ◽  
Immobilized Enzyme ◽  
Fold Increase ◽  
Alginate Beads ◽  
Hydrolysis Kinetics ◽  
Initial Activity ◽  
Reaction Conditions ◽  
Bead Size ◽  
Optimum Ph ◽  
Optimum Ph And Temperature

A maltooligosaccharide-forming amylase from B circulans GRS 313 was immobilized by entrapment in calcium alginate beads. The immobilized activity was affected by the size of the bead and bead size of 2mm was found to be most effective for hydrolysis. Kinetics constants, Km and Vmax were estimated and were found to be affected by the bead size. The catalytic activity of the enzyme was studied in presence of various starchy residues and metal ions. HgCl2, CuSO4 and FeCl3 caused inhibition of the enzyme. The reaction conditions, pH and temperature, was optimized using response surface methodology. At the optimum pH and temperature of 4.9 and 57ºC, the apparent activity was 25.6U/g of beads, resulting in almost 2-fold increase in activity. The immobilized enzyme showed a high operational stability by retaining almost 85% of the initial activity after seventh use.

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