scholarly journals ANALYSING THE BIOCATALYTIC ASPECT OF AMYLASE FROM PLANT AND MICROBIAL SOURCES FOR INDUSTRIAL APPLICATION

2020 ◽  
pp. 85-87
Author(s):  
DIGUMARTHY NIHARIKA ◽  
DIPTI SONI JAIPURIAR ◽  
VIRENDRA VAISHNAV
Keyword(s):  
Bacillus Subtilis ◽  
Enzymatic Activity ◽  
Enzyme Assay ◽  
Exchange Chromatography ◽  
Sds Page ◽  
Wide Range ◽  
Green Pea ◽  
Pharmaceutical Industries ◽  
Plant Sources ◽  
Important Enzyme

Objective: Biocatalysts have a wide role in industries and amylases are one of the best enzymes used in various industries as they stay stable physically and chemically even under environmental or physical stress. Extraction of amylase from plant sources like chickpea and green pea and also the microbial source of Bacillus subtilis. Methods: Enzymatic activity was determined by enzyme assay and purified through the following steps such as salt precipitation, dialysis, Ion-exchange chromatography and characterized using SDS PAGE. Results: Enzymatic activity of amylase produced by bacillus subtilis was determined the highest (4600 U/ml) activity and molecular weight 48.9kDa was recorded. Conclusion: Amylase is a highly important enzyme that breaks down the starch molecules into simple sugars. It has potential in a wide range of industrial processes such as food, fermentation and pharmaceutical industries. All the sources used in this study proves that the bacteria have the highest concentration of enzyme in the form of protein.

scholarly journals Proteinaceous Protease Inhibitor from Lawsonia Inermis: Purification, Characterization and Antibacterial Activity

2013 ◽  
Vol 8 (10) ◽  
pp. 1934578X1300801 ◽  
Author(s):  
Arvind Dabhade ◽  
Priti Patel ◽  
Ulhas Patil
Keyword(s):  
Antibacterial Activity ◽  
Protease Inhibitor ◽  
Deae Cellulose ◽  
Gel Permeation Chromatography ◽  
Apparent Molecular Weight ◽  
Exchange Chromatography ◽  
Lawsonia Inermis ◽  
Sds Page ◽  
Wide Range ◽  
And Staphylococcus Aureus

A thermo-stable, proteinaceous protease inhibitor (LPI) from Lawsonia inermis is reported. The LPI was purified from Lawsonia inermis seeds by subsequent ammonium sulfate precipitation, ion exchange chromatography (DEAE-Cellulose) and gel permeation chromatography (Sephadex-50). The purified protease inhibitor is effective against a wide range of proteases viz. papain, trypsin, pepsin and metallo-protease. The apparent molecular weight of the protease inhibitor is 19 kDa, determined by SDS-PAGE electrophoresis. The protease inhibitor was found to be stable at 70 °C for 30 min. It was also examined for antibacterial activity against Pseudomonas aeruginosa MTCC 7926 and Staphylococcus aureus NCIM 2079; the IC50 values of the purified LPI were 11.4 μg/mL and 16.6 μg/mL respectively.

scholarly journals Characterization of Thermostable Amylase From Halophilic Lactobacillus Plantarum TS1

2021 ◽  
Author(s):  
Sania Riaz ◽  
Anum Fareed ◽  
Habiba Zaffar ◽  
Shafique Ur Rehman ◽  
Muhammad Jamil ◽  
...  
Keyword(s):  
Lactobacillus Plantarum ◽  
Saline Soil ◽  
Salt Range ◽  
Sds Page ◽  
Wide Range ◽  
Two Temperatures ◽  
Harsh Conditions ◽  
Thermostable Amylase ◽  
Important Enzyme

Abstract Amylase is an important enzyme use extensively in various industrial processes. It is mainly involved in the catalysis of starch that requires harsh conditions; therefore, it is required to isolate amylases with unique properties that makes it more applicable. Extremophiles are the major resource of such enzymes; therefore, amylase positive strains were isolated from the saline soil where the temperature is also exceptionally high. Five amylase positive strains were isolated from the Karak salt range, Kohat Pakistan and were identified by phylogenetic analysis. DNS based assay was employed to compare the activities of different amylases obtained from five strains while using the starch as a substrate. The amylase obtained from Lactobacillus plantarum TS1 was found to be more efficient, which was purified and characterized. The SDS-PAGE of purified amylase showed a single band with an estimated size of 10 kDa. The kinetic parameters were measured at two temperatures i.e. at 37 °C and 50 °C. The Kcat as well as the Kcat/KM were found to be high when temperature increased from 37 °C to 50 °C. Amylase was active at wide range of temperature as well as pH and work efficiently in the presence of salts and various organic solvents.

scholarly journals Extraction, purification, and activity of protease from the leaves of Moringa oleifera

F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 1151 ◽  
Author(s):  
Swarnali Banik ◽  
Shrutidhara Biswas ◽  
Srabani Karmakar
Keyword(s):  
Enzymatic Activity ◽  
Moringa Oleifera ◽  
Proteolytic Enzymes ◽  
Maximal Activity ◽  
Essential Amino Acids ◽  
Industrial Applications ◽  
Exchange Chromatography ◽  
Wide Range ◽  
Geographically Distributed ◽  
Aqueous Leaf Extract

Background: Proteases cleave proteins, thereby providing essential amino acids for protein synthesis, and degrade misfolded and damaged proteins to maintain homeostasis. Proteases also serve as signaling molecules, therapeutic agents and find wide applications in biotechnology and pharmaceutical industry.  Plant-derived proteases are suitable for many biomedical applications due to their easy availability and activity over a wide range of pH, temperature, and substrates. Moringa oleifera Lam (Moringaceae) is a very common food plant with medicinal property and geographically distributed in tropical countries. Here, we isolate proteases from the leaves of Moringa oleifera and characterize its enzymatic activity. Methods: Proteases were isolated from the aqueous leaf extract of Moringa oleifera by ammonium sulfate precipitation and purified by ion exchange chromatography. Subsequently, the enzyme kinetics was determined using casein as a substrate and calibrated over different pH and temperature range for maximal activity. Results: We obtained purified fraction of the protease having a molecular weight of 51 kDa. We observed that for the maximal caseinolytic activity of the protease, a pH of 8 and temperature of 37ºC was found to be most effective. Conclusion: The plant-derived proteolytic enzymes are finding increasing clinical and industrial applications. We could extract, purify and characterize the enzymatic activity of proteases from the leaves of Moringa oleifera. Further molecular characterization, substrate specificity and activity of the extracted protease are required for determining its suitability as a proteolytic enzyme for various applications.

scholarly journals High-mannose type N-glycan binding specificity of a novel lectin from the red alga (Betaphycus gelatinus)

2020 ◽  
Vol 17 (4) ◽  
pp. 709-718
Author(s):  
Le Dinh Hung ◽  
Le Thi Doan Thuc
Keyword(s):  
Divalent Cations ◽  
Kappaphycus Alvarezii ◽  
Gel Filtration ◽  
Red Alga ◽  
Exchange Chromatography ◽  
Sds Page ◽  
Wide Range ◽  
Anti Cancer ◽  
High Mannose ◽  
Solieria Filiformis

The red alga, Betaphycus gelatinus is one of carrageenan sources in the world. The lectin from the red alga B. gelatinus was isolated by a combination of aqueous ethanol extraction, ethanol precipitation, ion-exchange chromatography and gel filtration chromatography and was designated as BGL after the specific name of alga. Lectin gave a single band with molecular mass of about 19,000 Da in both non-reducing and reducing SDS-PAGE conditions, therefore lectin exists in monomer form. The hemagglutination activities of BGL were stable over a wide range of pH from 3 to 10, temperature up 60 oC and not affected by either the presence of EDTA or addition of divalent cations, indicating that lectin requires no metal for biological activity. The hemagglutination activities of BGL were not inhibited by monosaccharides and glycoproteins, D-glucose, D-mannose, D-galactose, D-xylose, N-acetyl-galactosamine, N-acetyl-glucosamine, N-acetyl-neuraminic acid, N-acety-D-mannosamine, transferrin and fetuin, but strongly inhibited by glycoproteins bearing high-mannose type N-glycan, such as yeast mannan and porcine thyroglobulin. Lectin BGL is specific for N-glycans and may recognize terminal (α1–3) or (α1–6)-linked mannose residues in structure Man(α1-6)[Man(α1-3)]Man(α1-6)[Man(α1-3)]Man(β1-4)GlcNAc(β1-4)GlcNAc of N-glycans. High-mannose type N-glycan binding specificities of this lectin highly resemble with those of the anti-cancer, anti-virus and anti-bacteria lectins from the red algae, carrageenophytes, including Eucheuma serra (ESA-2), Eucheuma denticulatum (EDA-2), Kappaphycus striatum (KSA-2), Kappaphycus alvarezii (KAA-1 and KAA-2) and Solieria filiformis (SfL1 and SfL2). The red alga B. gelatinus could promise to be a good source of valuable lectins for application in biochemistry and biomedicine.

Aspergillus sydowii Strain SCAU066 and Aspergillus versicolor Isolate BAB-6580: Potential Source of Xylanolytic, Cellulolytic and Amylolytic Enzymes

2020 ◽  
Vol 14 (2) ◽  
pp. 15
Author(s):  
Zaidah Zainal ariffin
Keyword(s):  
Extracellular Enzymes ◽  
Biologically Active ◽  
Aspergillus Versicolor ◽  
Aspergillus Sydowii ◽  
Aspergillus Tamarii ◽  
Alternative Source ◽  
Amylolytic Enzymes ◽  
Potato Dextrose Broth ◽  
Wide Range ◽  
Pharmaceutical Industries

Fungi is known to produce a wide range of biologically active metabolites and enzymes. Enzymes produced by fungi are utilized in food and pharmaceutical industries because of their rich enzymatic profile. Filamentous fungi are particularly interesting due to their high production of extracellular enzymes which has a large industrial potential. The aim of this study is to isolate potential soil fungi species that are able to produce functional enzymes for industries. Five Aspergillus species were successfully isolated from antibiotic overexposed soil (GPS coordinate of N3.093219 E101.40269) by standard microbiological method. The isolated fungi were identified via morphological observations and molecular tools; polymerase chain reactions, ITS 1 (5’- TCC GTA GGT GAA CCT GCG G3’) forward primer and ITS 4 (5’-TCC TCC GCT TAT TGA TAT GC-3’) reverse primer. The isolated fungi were identified as Aspergillus sydowii strain SCAU066, Aspergillus tamarii isolate TN-7, Aspergillus candidus strain KUFA 0062, Aspergillus versicolor isolate BAB-6580, and Aspergillus protuberus strain KAS 6024. Supernatant obtained via submerged fermentation of the isolated fungi in potato dextrose broth (PDB) and extracted via centrifugation was loaded onto specific media to screen for the production of xylanolytic, cellulolytic and amylolytic enzymes. The present findings indicate that Aspergillus sydowii strain SCAU066 and Aspergillus versicolor isolate BAB-6580 have great potential as an alternative source of xylanolytic, cellulolytic and amylolytic enzymes.

Enzymatic activity of strains of bacteria Bacillus subtilis isolated from frozen soils

2020 ◽  
Vol 1 (1) ◽  
pp. 73-79
Author(s):  
M.P. Scriabina ◽  
◽  
A.M. Stepanova ◽  
N.P. Tarabukina ◽  
M.P. Neustroev ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Enzymatic Activity ◽  
Frozen Soils

1,4-Diazepines: A Review on Synthesis, Reactions and Biological Significance

2019 ◽  
Vol 16 (5) ◽  
pp. 709-729 ◽  
Author(s):  
Muhammad A. Rashid ◽  
Aisha Ashraf ◽  
Sahibzada S. Rehman ◽  
Shaukat A. Shahid ◽  
Adeel Mahmood ◽  
...  
Keyword(s):  
Biological Activities ◽  
Biological Significance ◽  
Biological Evaluation ◽  
Wide Range ◽  
Pharmaceutical Industries ◽  
Biological Aspects ◽  
Synthetic Routes ◽  
Biological Attributes ◽  
Synthesis Reactions ◽  
Potential Use

Background:1,4-Diazepines are two nitrogen containing seven membered heterocyclic compounds and associated with a wide range of biological activities. Due to its medicinal importance, scientists are actively involved in the synthesis, reactions and biological evaluation of 1,4-diazepines since number of decades.Objective:The primary purpose of this review is to discuss the synthetic schemes and reactivity of 1,4- diazepines. This article also describes biological aspects of 1,4-diazepine derivatives, that can be usefully exploited for the pharmaceutical sector.Conclusion:This review summarizes the abundant literature on synthetic routes, chemical reactions and biological attributes of 1,4-diazepine derivatives. We concluded that 1,4-diazepines have significant importance due to their biological activities like antipsychotic, anxiolytic, anthelmintic, anticonvulsant, antibacterial, antifungal and anticancer. 1,4-diazepine derivatives with significant biological activities could be explored for potential use in the pharmaceutical industries.

Chain-breaking/Preventive Antioxidant, Urate-lowering, and Anti-inflammatory Effects of Pure Curcumin

2020 ◽  
Vol 17 (1) ◽  
pp. 66-74
Author(s):  
Seghira Bisset ◽  
Widad Sobhi ◽  
Chawki Bensouici ◽  
Abdelhalim Khenchouche
Keyword(s):  
Uric Acid ◽  
Xanthine Oxidase ◽  
Acid Production ◽  
Biological Activities ◽  
Antioxidant Effect ◽  
Metal Chelating ◽  
Wide Range ◽  
Chain Breaking ◽  
Pharmaceutical Industries ◽  
Anti Inflammatory

Background: Several researches have shown that therapeutic compounds or phytochemicals from natural sources are important in the food as it is valuable in pharmaceutical industries due to their fewer side effects and potent against various diseases. Curcumin, a major polyphenol derived from turmeric spice, which used in many foods, has a wide range of biological activities, with quite a safety. Objective: The goal of this study was to investigate the antioxidant, urate-lowering, and antiinflammatory effects of pure curcumin. Methods: The antioxidant activity was evaluated for chain-breaking antioxidant effect (radicalscavenging and reducing abilities assays) and for preventive antioxidant effect with metal chelating assay, the urate-lowering was assayed on aspectrophotometer by measuring the inhibition of uric acid production by xanthine oxidase (XO) enzyme, and the anti-inflammatory effect was estimated using in vitro albumin denaturation inhibition. Results: Curcumin showed a significant and good chain-breaking antioxidant effect, both in free radical- scavenging assays (Galvinoxyl radical, ABTS, and hydroxyl radical), and in reducing abilities methods (reducing power, Cupric ion reducing antioxidant capacity and O-phenanthroline assays). In preventive antioxidant effect, assessed with the metal chelating assay, curcumin showed significant effect but with high concentration compared with standard. In the xanthine/xanthine oxidase system, curcumin significantly inhibited uric acid production (IC50=0.71 ± 0.06 mg/mL). Regarding antiinflammatory activity, curcumin showed significant inhibition of albumin denaturation with an IC50 value of 1181.69 ± 1.11μg/mL. Conclusion: These results indicated that curcumin showed promising antioxidant, anti-gout and antiinflammatory properties and might be used as potential, natural drugs against oxidative and inflammation- related diseases.

PRODUCTION OF CYTASES ACTIVE ON BARLEY GUM BY BACTERIA OF THE GENUS BACILLUS

1953 ◽  
Vol 31 (1) ◽  
pp. 28-32 ◽  
Author(s):  
A. C. Blackwood
Keyword(s):  
Bacillus Subtilis ◽  
Enzymatic Activity ◽  
Nitrogen Source ◽  
Freeze Drying ◽  
Shake Flask ◽  
Sole Nitrogen Source ◽  
Genus Bacillus ◽  
Original Activity ◽  
Bacterial Cultures ◽  
Bacillus Genus

One hundred and fourteen bacterial cultures representing most of the species in the Bacillus genus were tested for the production of extracellular barley gum cytase. Assays were made on shake-flask cultures grown on a medium containing glucose and yeast extract. Although all the organisms had some enzymatic activity, certain strains of Bacillus subtilis gave the best yields of cytase. On a medium with asparagine as the sole nitrogen source even higher yields were obtained. The crude cytase preparations were stable and after freeze-drying most of the original activity remained.

scholarly journals Not Just Transporters: Alternative Functions of ABC Transporters in Bacillus subtilis and Listeria monocytogenes

2021 ◽  
Vol 9 (1) ◽  
pp. 163
Author(s):  
Jeanine Rismondo ◽  
Lisa Maria Schulz
Keyword(s):  
Bacillus Subtilis ◽  
Listeria Monocytogenes ◽  
Abc Transporters ◽  
Organic Molecules ◽  
Atp Hydrolysis ◽  
The Past ◽  
Wide Range ◽  
Regulatory Functions ◽  
Complex Organic ◽  
Detoxification Mechanisms

ATP-binding cassette (ABC) transporters are usually involved in the translocation of their cognate substrates, which is driven by ATP hydrolysis. Typically, these transporters are required for the import or export of a wide range of substrates such as sugars, ions and complex organic molecules. ABC exporters can also be involved in the export of toxic compounds such as antibiotics. However, recent studies revealed alternative detoxification mechanisms of ABC transporters. For instance, the ABC transporter BceAB of Bacillus subtilis seems to confer resistance to bacitracin via target protection. In addition, several transporters with functions other than substrate export or import have been identified in the past. Here, we provide an overview of recent findings on ABC transporters of the Gram-positive organisms B. subtilis and Listeria monocytogenes with transport or regulatory functions affecting antibiotic resistance, cell wall biosynthesis, cell division and sporulation.

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