scholarly journals EXTRACTION AND PURIFICATION OF VEGETABLE PEROXIDASE: A REVIEW

2019 ◽  
Vol 16 (31) ◽  
pp. 692-703
Author(s):  
Aline HAAS ◽  
Cleiton VAZ ◽  
Aniela Pinto KEMPKA
Keyword(s):  
Enzymatic Activity ◽  
Specific Activity ◽  
Extraction Methods ◽  
Raw Material ◽  
Partial Purification ◽  
Buffer Solution ◽  
Degradation Of Dyes ◽  
Extraction And Purification ◽  
Wide Range ◽  
Purification Methods

Peroxidases are enzymes that catalyze the oxidation of various substrates, maintaining their enzymatic activity in wide ranges of pH and temperatures. These enzymes are used in processes for the degradation of dyes and phenolic compounds. Peroxidases are present in the tissues of several plants, and the search for new sources of this enzyme is necessary. This literature review aims to compile information about the extraction and/or purification of peroxidases contained in different plant tissues, presenting extraction methods, purification processes, enzymatic activities and their increments, according to the chemical and physical processes applied. Several plant sources can be raw material to obtain these enzymes, through different forms of extraction, where the processes of comminution predominate in the presence of buffer solution. For partial purification, are used precipitation with solvents (acetone and ethanol) and salts (ammonium sulfate) and centrifugation. For purification, chromatographic processes are used, in which molecular exclusion and affinity chromatography are prominent. It is concluded that there is a wide range of possibilities for obtaining the enzyme peroxidase from plants, with variability in the enzymatic activity when different extraction methods are applied. The purification methods used provide increases in the specific activity of the peroxidases.

scholarly journals Mycolysis of wood, its products and their use. IV. Component analysis of mycologically destroyed wood

2021 ◽  
Vol 25 ◽  
pp. 85-96
Author(s):  
G.N. Kononov ◽  
◽  
A.N. Verevkin ◽  
Yu.V. Serdyukova ◽  
V.D. Zaitsev ◽  
...  
Keyword(s):  
Brown Rot ◽  
Component Composition ◽  
Extraction Methods ◽  
Raw Material ◽  
White Rot ◽  
Birch Wood ◽  
Wide Range ◽  
Extractive Substances ◽  
Carbohydrate Components ◽  
Derivatives Of

The article is devoted to the study of the component composition of mycologically destroyed wood. As a result of wood mycolysis under the action of wood-destroying fungi enzymes, so-called «rot» is formed with a chemical composition different from healthy wood. It is noted that the «brown rot» of wood is enriched with lignin components of wood and «white rot» with carbohydrate components of wood. The results of analyses of ligno-carbohydrate complexes of spruce wood «brown rot», birch wood «white rot» and a group study of low-molecular compounds isolated by extraction methods with various solvents are presented. It is noted that the content of lignin in the sample of «brown rot» wood is four times higher than in the sample of «white rot». It is shown that birch wood with «white rot» is significantly enriched with cellulose. The chemical nature of some groups of extractive substances has been revealed. In the extracts of mycologically destroyed wood, substances of phenolic, alcoholic and quinone nature were found. The presence of derivatives of aromatic and aliphatic carbonyl and carboxyl compounds is noted. Among the products of mycolysis, carbohydrates, flavanoids and terpenoids have been identified. Based on the analysis, an assumption is made that mycologically destroyed wood contains a wide range of phenolic and carbohydrate compounds contained both in the original wood and in the spores and hyphae of wood-destroying fungi themselves. The idea is substantiated that the study of extractive substances of mycologically destroyed wood makes it possible to predict possible directions of the prospective use of this raw material for obtaining target products. This article is the fourth in the cycle «Wood mycolysis, its products and their use», the previous ones were published in the journal «Forestry Bulletin», 2020, v. 24, no. 2, 6; v. 25, no. 1.

scholarly journals Six Common Herbs with Distinctive Bioactive, Antioxidant Components. A Review of Their Separation Techniques

Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2920
Author(s):  
Antigoni Oreopoulou ◽  
Evanthia Choulitoudi ◽  
Dimitrios Tsimogiannis ◽  
Vassiliki Oreopoulou
Keyword(s):  
Raw Materials ◽  
Extraction Methods ◽  
Natural Antioxidant ◽  
Antioxidant Compounds ◽  
Extensive Literature ◽  
Green Solvents ◽  
Lemon Balm ◽  
Traditional Medicines ◽  
Extraction And Purification ◽  
Purification Methods

Rosemary, oregano, pink savory, lemon balm, St. John’s wort, and saffron are common herbs wildly grown and easily cultivated in many countries. All of them are rich in antioxidant compounds that exhibit several biological and health activities. They are commercialized as spices, traditional medicines, or raw materials for the production of essential oils. The whole herbs or the residues of their current use are potential sources for the recovery of natural antioxidant extracts. Finding effective and feasible extraction and purification methods is a major challenge for the industrial production of natural antioxidant extracts. In this respect, the present paper is an extensive literature review of the solvents and extraction methods that have been tested on these herbs. Green solvents and novel extraction methods that can be easily scaled up for industrial application are critically discussed.

THE PROTEOLYTIC ENZYMES OF MICROORGANISMS: IV. PARTIAL PURIFICATION AND SOME PROPERTIES OF EXTRACELLULAR PROTEASE FROM MORTIERELLA RENISPORA DIXON-STEWART

1952 ◽  
Vol 30 (6) ◽  
pp. 685-692 ◽  
Author(s):  
L. R. Wetter
Keyword(s):  
Culture Medium ◽  
Considerable Increase ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
Partial Purification ◽  
Ferrous Ions ◽  
Ph Optimum ◽  
Enzyme Preparations ◽  
Wide Range ◽  
Repeated Precipitation

A protease concentrate was obtained from the culture medium of Mortierella renispora Dixon-Stewart (PRL 26) by repeated precipitation with ammonium sulphate. The specific activity of the mold protease compared favorably with that of crystalline trypsin. The pH optimum was broad, with a maximum at a pH of 7.5 when hemoglobin was used as the substrate. A study of the pH stability characteristics showed that it was stable over a wide range (4.9 to 9.5) at 1 °C. and 25 °C. Ferrous ions caused a considerable increase in the activity of the enzyme preparations, other metals were ineffective as activators.

scholarly journals Review on Extraction and Application of Natural Dyes

2021 ◽  
Author(s):  
Md. Salauddin Sk ◽  
◽  
Rony Mia ◽  
Md. Anamul Haque ◽  
Al Mojnun Shamim ◽  
...  
Keyword(s):  
Extraction Process ◽  
Extraction Methods ◽  
Vital Role ◽  
Natural Dyes ◽  
Acid Extraction ◽  
Extraction And Purification ◽  
Wide Range ◽  
Different Types ◽  
Environment Characteristic ◽  
Extraction Processes

With the improvement of living standards, everybody is very much conscious about the environmental protection and health safety. Natural dyes have attracted more attention to the industry due to exhibiting better biodegradability and more compatibility with the environment. Characteristic colours that are gathered from common assets can be categorized as either plant, creature, mineral, or microbial colours and can be used for colouring a wide range of regular filaments. Late examination shows that it can likewise be utilized to colour a portion of the manufactured filaments too. Normal colours are not just utilized in the shading of material filaments, they are also utilized for food, prescriptions, handiwork articles, and leather preparing. Extraction and purification play a vital role in the processing of natural dyes. There are different types of extraction process currently available for these natural dyes, such as solvent extraction, aqueous extraction, enzymatic extraction and fermentation, extraction with microwave or ultrasonic energy, supercritical fluid extraction, and alkaline or acid extraction. All these extraction processes have their own advantages as well as some drawbacks depending on the parameters that need to be maintained during the extraction process. Appropriate extraction can be beneficial for specific types of such dyes. In this paper, the classification, characteristics, extraction methods, and the application of natural dyes are introduced in an organized manner.

scholarly journals Partial Purification and Characterization of Bacteriocin-Like Inhibitory Substances Produced by Streptomyces sp. Isolated from the Gut of Chanos chanos

2021 ◽  
Vol 2021 ◽  
pp. 1-12
Author(s):  
Muhammad A. Kurnianto ◽  
Harsi D. Kusumaningrum ◽  
Hanifah N. Lioe ◽  
Ekowati Chasanah
Keyword(s):  
Molecular Weight ◽  
Antibacterial Activity ◽  
Antimicrobial Agents ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
Proteinase K ◽  
Partial Purification ◽  
Chanos Chanos ◽  
Extracellular Metabolites ◽  
Wide Range

Bacteriocin-like inhibitory substances (BLIS) have sparked great interest because of their promising use in food as natural antimicrobial agents. In this work, six Streptomyces isolates obtained from the gut of Chanos chanos demonstrated their ability to produce extracellular metabolites with inhibitory activity against Salmonella enterica serovar Typhimurium, Escherichia coli, Listeria monocytogenes, and Staphylococcus aureus. Exposure of the extracellular metabolites to proteolytic enzymes (i.e., proteinase-K, trypsin, and pepsin) revealed high sensitivity and confirmed their proteinaceous nature. The metabolites were stable at high temperatures (up to 100°C for 30 min) and a wide range of pH (pH 2.0–7.0). Fractionation of the crude BLIS by filtration yielded three fractions based on molecular weight: <3 kDa, 3–10 kDa, and >10 kDa. Analysis of the antibacterial activity of these fractions showed increased specific activity, especially in the fraction with a molecular weight (MW) of <3 kDa, relative to the crude sample. The fraction with MW < 3   kDa had minimum inhibitory and bactericidal concentrations in ranges 0.04–0.62 mg·mL−1 and 0.08–1.25 mg·mL−1, respectively. This fraction also showed better temperature and pH stability compared with crude BLIS. Brine shrimp toxicity assay revealed that this fraction has moderate toxicity with a 50% lethal concentration of 226.975 μg·mL−1 (i.e., moderate toxicity) to Artemia salina. Identification of the peptide sequences of this fraction by liquid chromatography–tandem mass spectrometry yielded 130 proteins with retention times of 15.21–19.57 min. Eleven proteins with MWs of 1345.66–2908.35 Da and composed of less than 30 amino acid residues with high hydrophobicity (15.34–26.22 kcal·mol−1) appeared to be responsible for the antibacterial activity of the fraction. This study revealed the potential application of BLIS from Streptomyces, especially BLIS SCA-8, as antibacterial agents.

scholarly journals Polyol-pathway enzymes of human brain. Partial purification and properties of sorbitol dehydrogenase

1983 ◽  
Vol 211 (1) ◽  
pp. 81-90 ◽  
Author(s):  
M M O'Brien ◽  
P J Schofield ◽  
M R Edwards
Keyword(s):  
Human Brain ◽  
Thermal Inactivation ◽  
Specific Activity ◽  
Substrate Inhibition ◽  
Enzyme Mechanism ◽  
Reverse Reaction ◽  
Sorbitol Dehydrogenase ◽  
Partial Purification ◽  
Forward Reaction ◽  
Wide Range

Sorbitol dehydrogenase was isolated from human brain and purified 690-fold, giving a final specific activity of 11.1 units/mg of protein. The enzyme preparation was nearly homogeneous, but was unstable at most temperatures. It exhibited a broad pH optimum of 7.5-9.0 in the forward reaction (i.e. sorbitol leads to fructose), and of 7.0 in the reverse reaction (i.e. fructose leads to sorbitol). Substrate-specificity studies demonstrated that the enzyme had the capability to oxidize a wide range of polyols and that the enzyme had a higher affinity for substrates in the forward reaction than in the reverse reaction, e.g. Km for sorbitol was 0.45 mM, and that for fructose was 480 mM. However, the Vmax. was 10 times greater in the reverse reaction. At high concentrations of fructose (500 mM) the enzyme exhibited substrate inhibition in the reverse reaction. The enzyme mechanism was sequential, as determined by the kinetic patterns arising from varying the substrate concentrations. In addition, both fructose and NADH protected the enzyme against thermal inactivation. These findings, together with product-inhibition data, suggested that the mechanism is random rapid equilibrium with two dead-end complexes.

scholarly journals Partial purification, characterization and immobilization of a novel lipase from a native isolate of Lactobacillus fermentum

2021 ◽  
Author(s):  
Foruzan Fathi ◽  
Rouha Kasra-Kermanshahi ◽  
Zahra Moosavi-Nejad ◽  
Elahe Mobarak Qamsari
Keyword(s):  
Enzymatic Activity ◽  
Ammonium Sulfate ◽  
High Efficiency ◽  
Specific Activity ◽  
Lipolytic Activity ◽  
Physical Adsorption ◽  
Lactobacillus Fermentum ◽  
Partial Purification ◽  
Bacterial Strains ◽  
Chitosan Beads

Background and Objectives: Due to the widespread use of lipase enzymes in various industries, finding native lipase pro- ducing microorganisms is of great value and importance. In this study, screening of lipase-producing lactobacilli from native dairy products was performed. Materials and Methods: Qualitative evaluation of lipolytic activity of lipase-producing lactobacilli was performed in differ- ent media containing olive oil. A clear zone observation around the colonies indicated the lipolytic activity. The strain with the highest enzymatic activity was identified. Determination of optimal pH and temperature of lipase activity was measured by spectrophotometry using p-nitrophenyl acetate (ρ-NPA) substrate. Partial purification of lipase enzyme was performed using 20-90% saturation ammonium sulfate. Eventually, lipase was immobilized by physical adsorption on chitosan beads. Results: Among screened lipolytic bacterial strains, one sample (5c isolate) which showed the highest enzymatic activity (5329.18 U/ml) was close to Lactobacillus fermentum. During characterization, the enzyme showed maximum activity in Tris-HCl buffer with pH 7, while remaining active over a temperature range of 5°C to 40°C. The results of the quantitative assay demonstrated that the fraction precipitated in ammonium sulfate at 20% saturation has the highest amount of lipolytic activity, with a specific activity of 22.0425 ± 3.6 U/mg. Purification folds and yields were calculated as 8.73 and 44%, respec- tively. Eventually, the enzyme was immobilized by physical adsorption on chitosan beads with a yield of 56.21%. Conclusion: The high efficiency of enzyme immobilization on chitosan beads indicates the suitability of this method for long-term storage of new lipase from native 5c isolate.

scholarly journals EXTRACTION AND PURIFICATION OF BETA-GALACTOSIDASE FROM LOCAL ALMOND AND ITS USE FOR LACTOSE INTOLERANCE TREATMENT

2020 ◽  
Vol 51 (3) ◽  
pp. 767-776
Author(s):  
Al-easawi & et al.
Keyword(s):  
High Efficiency ◽  
Lactose Intolerance ◽  
Specific Activity ◽  
Gel Filtration ◽  
High Specific Activity ◽  
Exchange Chromatography ◽  
Partial Purification ◽  
Lactose Hydrolysis ◽  
Extraction And Purification ◽  
Beta Galactosidase

This study was aimed, extraction and purification of beta-Galactosidase from local almond(Amygdalus communis)  for lactose intolerance treatment. The best one among 10 methods method of the extraction was using sodium phosphate buffer at 0.2 molar. Which was  achieves the highest specific activity amounted to 3.66unit/mg protein. Then, partial purification of enzyme was done using five methods. The highest specific activity was obtained using the method of precipitation with ammonium sulphate at 30-70% since the specific activity was 15.85units/mg protein. Which represented the best way to precipitation the enzyme. Three iso enzymes were obtained. One of them was taken for its high specific activity(20.10units/mg protein) and ion exchange chromatography was used and followed by gel filtration technique using sephadex-100 column to increase purification. The specific activity was increased to 21.95units/mg protein. Lactose hydrolysis efficiency test was performed and the purified enzyme showed high efficiency in standard lactose hydrolysis test.          

Automation of Process Control in Chemical Plant

2015 ◽  
Vol 2 (1) ◽  
pp. 6-12
Author(s):  
Agus Sugiarta ◽  
Houtman P. Siregar ◽  
Dedy Loebis
Keyword(s):  
Process Control ◽  
Pid Control ◽  
Control Algorithm ◽  
Chemical Engineering ◽  
Chemical Plant ◽  
Raw Material ◽  
Flow Rates ◽  
Material Supply ◽  
Wide Range ◽  
Inherent Problem

Automation of process control in chemical plant is an inspiring application field of mechatronicengineering. In order to understand the complexity of the automation and its application requireknowledges of chemical engineering, mechatronic and other numerous interconnected studies.The background of this paper is an inherent problem of overheating due to lack of level controlsystem. The objective of this research is to control the dynamic process of desired level more tightlywhich is able to stabilize raw material supply into the chemical plant system.The chemical plant is operated within a wide range of feed compositions and flow rates whichmake the process control become difficult. This research uses modelling for efficiency reason andanalyzes the model by PID control algorithm along with its simulations by using Matlab.

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