scholarly journals Multipotential Alkaline Protease From a Novel Pyxidicoccus sp. 252: Ecofriendly Replacement to Various Chemical Processes

2021 ◽  
Vol 12 ◽  
Author(s):  
Sonia Sharma ◽  
Shiv Kumar ◽  
Rajinder Kaur ◽  
Ramandeep Kaur
Keyword(s):  
Hydrogen Peroxide ◽  
Alkaline Protease ◽  
Ethylenediaminetetraacetic Acid ◽  
Tween 20 ◽  
16S Rrna Sequence ◽  
Temperature Range ◽  
Chitin Extraction ◽  
16S Rrna Sequence Analysis ◽  
Ph Range ◽  
Triton X

A newly isolated alkaline protease-producing myxobacterium was isolated from soil. The strain was identified as Pyxidicoccus sp. S252 on the basis of 16S rRNA sequence analysis. The extracellular alkaline proteases produced by isolate S252 (PyCP) was optimally active in the pH range of 11.0–12.0 and temperature range of 40–50°C The zymogram of PyCP showed six caseinolytic protease bands. The proteases were stable in the pH range of 8.0–10.0 and temperature range of 40–50°C. The activity of PyCP was enhanced in the presence of Na+, Mg2+, Cu2+, Tween-20, and hydrogen peroxide (H2O2) (hydrogen peroxide), whereas in Triton X-100, glycerol, ethylenediaminetetraacetic acid (EDTA), and Co2+, it was stable. PyCP showed a potential in various applications. The addition of PyCP in the commercial detergent enhanced the wash performance of the detergent by efficiently removing the stains of tomato ketchup and coffee. PyCP efficiently hydrolyzed the gelatin layer on X-ray film to release the embedded silver. PyCP also showed potent dehairing of goat skin and also efficiently deproteinized sea shell waste indicating its application in chitin extraction. Thus, the results of the present study indicate that Pyxidicoccus sp. S252 proteases have the potential to be used as an ecofriendly replacement of chemicals in several industrial processes.

Thermostable alkaline protease from newly isolated Vibrio sp.: extraction, purification and characterisation

Biologia ◽  
2012 ◽  
Vol 67 (4) ◽  
Author(s):  
Ponnambalam Subhashini ◽  
Neelamegam Annamalai ◽  
Ayyappan Saravanakumar ◽  
Thangavel Balasubramanian
Keyword(s):  
Enzyme Activity ◽  
Organic Solvents ◽  
Alkaline Protease ◽  
Mangrove Sediments ◽  
Sds Page ◽  
Vellar Estuary ◽  
Commercial Detergents ◽  
The Stability ◽  
Ph Range ◽  
Triton X

AbstractAn extracellular alkaline protease-producing Vibrio sp. was isolated from mangrove sediments of Vellar estuary. A 9.36-fold purification was achieved by a three-step purification procedure and the molecular weight of the enzyme was determined as 33 kDa by SDS-PAGE. The enzyme was active in a broad range of pH (6.0–11.0) and temperature (30–70°C), the optimum being at pH 9.0 and temperature 55°C. The enzyme was stable at alkaline pH range of 9–11 and up to a temperature of 60°C, after incubation for 1 h. Metals like Co2+, Hg2+, Ni2+ and Cu2+ inhibited the enzyme activity, whereas Fe2+, Ca2+ and Mn2+ were found to enhance the activity. The protease was found to be highly stable in the presence of oxidizing agents like H2O2, detergents such as SDS and Triton-X-100 and also some of the commonly used commercial detergents. The organic solvents like xylene, isopropanol, hexane and benzene were found to enhance as well as stabilize the enzyme activity. The extracellular production of the enzyme, the pH and thermal stability, and the stability in presence of oxidants, surfactants, commercial detergents and organic solvents, altogether suggest that it can be used as a laundry additive.

Kinetic of oxidation of methyl orange by vanadium(V) under conditions VO2+ and decavanadates coexist: Catalysis by Triton X-100 micellar medium

2019 ◽  
Author(s):  
Chem Int
Keyword(s):  
Methyl Orange ◽  
Solution Ph ◽  
Vanadium Concentration ◽  
Limiting Behavior ◽  
First Order ◽  
First Order Kinetics ◽  
Ph Range ◽  
Kinetic Pattern ◽  
Triton X ◽  
Kinetics Of

The kinetics of oxidation of methyl orange by vanadium(V) {V(V)} has been investigated in the pH range 2.3-3.79. In this pH range V(V) exists both in the form of decavanadates and VO2+. The kinetic results are distinctly different from the results obtained for the same reaction in highly acidic solution (pH < 1) where V(V) exists only in the form of VO2+. The reaction obeys first order kinetics with respect to methyl orange but the rate has very little dependence on total vanadium concentration. The reaction is accelerated by H+ ion but the dependence of rate on [H+] is less than that corresponding to first order dependence. The equilibrium between decavanadates and VO2+ explains the different kinetic pattern observed in this pH range. The reaction is markedly accelerated by Triton X-100 micelles. The rate-[surfactant] profile shows a limiting behavior indicative of a unimolecular pathway in the micellar pseudophase.

scholarly journals Pseudomonas eucalypticola sp. nov., a producer of antifungal agents isolated from Eucalyptus dunnii leaves

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Yujing Liu ◽  
Zhang Song ◽  
Hualong Zeng ◽  
Meng Lu ◽  
Weiyao Zhu ◽  
...  
Keyword(s):  
Dna Hybridization ◽  
Antifungal Agents ◽  
Novel Species ◽  
Phytopathogenic Fungi ◽  
Strictly Aerobic ◽  
Rrna Sequence ◽  
16S Rrna Sequence ◽  
Eucalyptus Dunnii ◽  
16S Rrna Sequence Analysis

AbstractPseudomonas are ubiquitously occurring microorganisms and are known for their ability to produce antimicrobials. An endophytic bacterial strain NP-1 T, isolated from Eucalyptus dunnii leaves, exhibits antifungal properties against five tested phytopathogenic fungi. The strain is a Gram-negative rod-shaped bacterium containing a single polar flagellum. It is strictly aerobic, grows at 4–37 °C, 2–5% NaCl, and pH 3–7. The 16S rRNA sequence analysis showed that NP-1 T belongs to the Pseudomonas genus. Phylogenetic analysis based on four concatenated partial genes (16S rDNA, gyrB, rpoB and rpoD) and the phylogenomic tree indicated that NP-1 T belongs to Pseudomonas fluorescens lineage but is distinct from any known Pseudomonas species. The G + C mol % of NP-1 T genome is 63.96, and the differences between NP-1 T and related species are larger than 1. The digital DNA-DNA hybridization and tetranucleotide signatures are 23.8 and 0.97, which clearly separates strain NP-1 T from its closest neighbours, Pseudomonas coleopterorum and Pseudomonas rhizosphaerae. Its phenotypic and chemotaxonomic features confirmed its differentiation from related taxa. The results from this polyphasic approach support the classification of NP-1 T as a novel species of Pseudomonas, and the name of Pseudomonas eucalypticola is thus proposed for this strain, whose type is NP-1 T (= CCTCC M2018494T = JCM 33572 T).

scholarly journals Marisediminicola antarctica gen. nov., sp. nov., an actinobacterium isolated from the Antarctic

2010 ◽  
Vol 60 (11) ◽  
pp. 2535-2539 ◽  
Author(s):  
Hui-Rong Li ◽  
Yong Yu ◽  
Wei Luo ◽  
Yin-Xin Zeng
Keyword(s):  
Sequence Similarity ◽  
Phylogenetic Analyses ◽  
Intertidal Sediment ◽  
Rrna Gene ◽  
Optimum Growth ◽  
Temperature Range ◽  
Zhongshan Station ◽  
Diamino Acid ◽  
Ph Range ◽  
The Antarctic

Strain ZS314T was isolated from a sandy intertidal sediment sample collected from the coastal area off the Chinese Antarctic Zhongshan Station, east Antarctica (6 ° 22′ 13″ S 7 ° 21′ 41″ E). The cells were Gram-positive, motile, short rods. The temperature range for growth was 0–26 °C and the pH for growth ranged from 5 to 10, with optimum growth occurring within the temperature range 18–23 °C and pH range 6.0–8.0. Growth occurred in the presence of 0–6 % (w/v) NaCl, with optimum growth occurring in the presence of 2–4 % (w/v) NaCl. Strain ZS314T had MK-10 as the major menaquinone and anteiso-C15 : 0, iso-C16 : 0 and anteiso-C17 : 0 as major fatty acids. The cell-wall peptidoglycan type was B2β with ornithine as the diagnostic diamino acid. The major polar lipids were diphosphatidylglycerol and phosphatidylglycerol. The genomic DNA G+C content was approximately 67 mol%. Phylogenetic analysis based on 16S rRNA gene sequence similarity showed that strain ZS314T represents a new lineage in the family Microbacteriaceae. On the basis of the phylogenetic analyses and phenotypic characteristics, a new genus, namely Marisediminicola gen. nov., is proposed, harbouring the novel species Marisediminicola antarctica sp. nov. with the type strain ZS314T (=DSM 22350T =CCTCC AB 209077T).

The efficiency of various detergents for extraction and stabilization of acetylcholinesterase from bovine erythrocytes

1987 ◽  
Vol 65 (1) ◽  
pp. 8-18 ◽  
Author(s):  
Rex K. M. Wong ◽  
Christine P. Nichol ◽  
M. Chandra Sekar ◽  
Basil D. Roufogalis
Keyword(s):  
Chain Length ◽  
Membrane Lipids ◽  
Acetylcholinesterase Activity ◽  
Exchange Chromatography ◽  
Erythrocyte Membranes ◽  
Tween 20 ◽  
Bovine Erythrocyte ◽  
Critical Micelle Concentrations ◽  
Triton X ◽  
Nonionic Detergents

The efficiency of several nonionic detergents and a homologous series of zwitterionic detergents for the extraction of acetylcholinesterase (EC 3.1.1.7) from bovine erythrocyte membranes was examined. Of the nonionic detergents examined, the polyoxyethylene-based Tweens were the least effective solubilizing agents. Within this series, increasing the length of the saturated fatty acid chain progressively decreased the efficiency of enzyme recovery, while unsaturation in the side chain reversed this trend. In the Lubrol detergents, where the chain length of the alcohol group is variable, an increase in the length of the polyoxyethylene glycol group decreased the recovery of acetylcholinesterase in the solubilized state, without affecting the efficiency of extraction of total erythrocyte protein. As with the other nonionic detergents examined, Triton X-100 and octy1 β-D-glucoside were maximally effective in solubilizing acetylcholinesterase activity at concentrations greater than their respective critical micelle concentrations. In the sulfobetaine (N-alkyldimethylaminopropane sulphonate) zwitterionic detergent series, the longer alkyl chain zwittergents Z 316 and Z 314 were more efficient than the shorter chain length members of the series (Z 310 and Z 312). In contrast to the higher chain length compounds, short chain analogs were maximally effective at or below their critical micelle concentrations. After purification by ion-exchange chromatography and affinity chromatography, the enzyme extracted with the various detergents gave sedimentation coefficients between 6.8S and 7.6S, consistent with a dimeric structure. Acetylcholinesterase could also be efficiently released by 0.2 mM EDTA or 0.5 M NaCl from bovine erythrocyte membranes previously depleted of 70–80% of the membrane lipids by butanol. Nonlinear Arrhenius plots of enzyme activity were found whether acetylcholinesterase was solubilized with Tween 20, Lubrol PX, or Triton X-100. The present work confirms that bovine erythrocyte acetylcholinesterase requires detergents to solubilize it from membranes and that its activity depends on the structure of the amphiphiles used to solubilize the enzyme.

scholarly journals Mucin biosynthesis. Properties of a bovine tracheal mucin β-6-N-acetylglucosaminyltransferase

1985 ◽  
Vol 227 (2) ◽  
pp. 405-412 ◽  
Author(s):  
P W Cheng ◽  
W E Wingert ◽  
M R Little ◽  
R Wei
Keyword(s):  
Enzyme Activity ◽  
Freezing Point ◽  
Cetylpyridinium Chloride ◽  
Sodium Dodecyl ◽  
Sodium Deoxycholate ◽  
Gas Chromatography Mass Spectrometry ◽  
Tween 20 ◽  
Group A ◽  
Michaelis Constants ◽  
Triton X

We have characterized a bovine tracheal mucin beta-6-N-acetylglucosaminyltransferase that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the C-6 of the N-acetylgalactosamine residue of galactosyl-β 1→3-N-acetylgalactosamine. Optimal enzyme activity was obtained between pH 7.5-8.5, at 5mM-MnCl2, and at 0.06-0.08% (v/v) Triton X-100 (or Nonidet P-40), or 0.5-5.0% (v/v) Tween 20. Ba2+, Mg2+ and Ca2+ could partially replace Mn2+, but Co2+, Fe2+, Cd2+ and Zn2+ could not. Sodium dodecyl sulphate, cetylpyridinium chloride, sodium deoxycholate, octyl beta-D-glucoside, digitonin and alkyl alcohols were less effective in enhancing enzyme activity, and dimethyl sulphoxide was ineffective. The apparent Michaelis constants were 1.25 mM for UDP-N-acetylglucosamine, 0.94-3.34 mM for freezing-point-depressing glycoprotein and 0.19 mM for periodate-treated blood-group-A porcine submaxillary mucin. Asialo ovine submaxillary mucin could not serve as the glycosyl acceptor. The structure of the 14C-labelled oligosaccharide obtained by alkaline-borohydride treatment of the product was identified as Gal beta 1→3(Glc-NAc beta 1→6)N-acetylgalactosaminitol by beta-hexosaminidase treatment, gas chromatography-mass spectrometry and 1H-n.m.r. (270 MHz) analysis. The enzyme is important in the regulation of mucin oligosaccharide biosynthesis.

Isolation and characterization of phosphate solubilizing bacteria from the rhizospheric soil of Ponthenpuzha forest, Pathanamthitta (District), Kerala

2021 ◽  
Vol 16 (8) ◽  
pp. 110-117
Author(s):  
Kannan Abhirami ◽  
K. Jayakumar
Keyword(s):  
Bacterial Isolate ◽  
Phosphate Solubilizing Bacteria ◽  
Cymbopogon Citratus ◽  
16S Rrna Sequence ◽  
Isolation And Characterization ◽  
16S Rrna Sequence Analysis ◽  
Phosphate Solubilizing ◽  
Level Identification

Phosphorous is considered as a major parameter for crop yield. Its availability to plant is independent of its abundance. For the plants to utilize phosphorous, it is to be converted to absorbable form. Here, the part rendered by phosphate solubilizing bacteria is significant for it plays a crucial role in the formation of plant usable phosphate from organic forms. In the present work, an effort had been made to isolate and identify phosphate solubilising bacterial isolate from the rhizhospheric soils of various plants in Ponthenpuzha forest. One of the isolate from Cymbopogon citrates responded positively to Pikovskaya’s medium by producing a halo zone during in vitro culture. Colony features and 16S rRNA sequence analysis identified the isolate as Burkholderia sps. We have reported the presence of genus Burkholderia in the rhizospheric zone of Cymbopogon citratus. Further studies are warranted for species level identification of the isolate.

scholarly journals Acquisition of an Agrobacterium Ri Plasmid and Pathogenicity by Other α-Proteobacteria in Cucumber and Tomato Crops Affected by Root Mat

2004 ◽  
Vol 70 (5) ◽  
pp. 2779-2785 ◽  
Author(s):  
S. A. Weller ◽  
D. E. Stead ◽  
J. P. W. Young
Keyword(s):  
Pathogenicity Test ◽  
Agrobacterium Radiobacter ◽  
Rrna Sequence ◽  
16S Rrna Sequence ◽  
Ri Plasmid ◽  
Fatty Acid Profiling ◽  
Transformation Rates ◽  
16S Rrna Sequence Analysis ◽  
Average Transformation

ABSTRACT Root mat of cucumbers and tomatoes has previously been shown to be caused by Agrobacterium radiobacter strains harboring a root-inducing Ri plasmid (pRi). Nine other pRi-harboring α-Proteobacteria have subsequently been isolated from root mat-infected crops. Fatty acid profiling and partial 16S rRNA sequence analysis identified three of these strains as being in the genus Ochrobactrum, five as being in the genus Rhizobium, and one as being in the genus Sinorhizobium. An in vitro pathogenicity test involving inoculation of cucumber cotyledons was developed. All pRi-harboring α-Proteobacteria induced typical root mat symptoms from the cotyledons. Average transformation rates for rhizogenic Ochrobactrum (46%) and Rhizobium (44%) strains were lower than those observed for rhizogenic A. radiobacter strains (64%). However, individual strains from these three genera all had transformation rates comparable to those observed from cotyledons inoculated with a rhizogenic Sinorhizobium strain (75%).

Purification, Properties and Mass Spectrometry Analysis of Two Novel Thermotolerant Endoglucanases from Bacillus akibai I-2

2011 ◽  
Vol 393-395 ◽  
pp. 911-915
Author(s):  
Sen Lin Liu ◽  
Miao Xing
Keyword(s):  
Mass Spectrometry ◽  
Soda Lakes ◽  
Maximum Activity ◽  
Mass Spectrometry Analysis ◽  
16S Rrna Sequence ◽  
Spectrometry Analysis ◽  
16S Rrna Sequence Analysis ◽  
Bacterium Strain ◽  
Terminal Amino ◽  
Alkaliphilic Bacterium

The alkaliphilic bacterium strain Ⅰ-2, which was isolated from soda lakes, was identified as Bacillus akibai by 16S rRNA sequence analysis and suggested to be a new subspecies of genus Bacillus. Two novel thermotolerant alkaline endoglucanases Ⅰ-2-A and Ⅰ-2-B were produced by this alkaliphilic strain. The purified Ⅰ-2-A and Ⅰ-2-B had molecular mass of approximately 60 and 90 kDa, respectively. The optimum pH of Ⅰ-2-A was about 9.0, while that of Ⅰ-2-B was about 8.0. Both enzymes exhibited maximum activity at around 50 °C and were stable up to 50 °C.The two enzymes were resistant to most metal ions and reagents examined. Mass spectrometry analysis indicated that Ⅰ-2-A was probably different from the endoglucanases reported. Ⅰ-2-B showed homology with those of family A5 endoglucanases but low similarity was found in C-terminal amino acid sequence.

scholarly journals Purification, characterization and application of novel alkaline protease from new Bacillus cereus UV-15 mutant

2017 ◽  
Vol 7 (4) ◽  
pp. 1 ◽  
Author(s):  
Sreedevi Basavaraju ◽  
Chandrasekhar Kathera ◽  
Pramoda Kumari Jasti
Keyword(s):  
Bacillus Cereus ◽  
Ammonium Sulphate ◽  
Alkaline Protease ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Tween 20 ◽  
Original Activity ◽  
Protease Enzyme

The alkaline protease produced by Bacillus cereus UV-15 mutant was purified by precipitation with ammonium sulphate and gel filtration through sephadex G-100. The enzyme has shown to have a molecular weight of 29kDa by SDS polyacrylamide gel electrophoresis. The extracted protease enzyme was purified by 16.64 fold through ammonium sulphate precipitation and chromatography separation in Sephadex G-100. The purified protease had a specific activity of 2915 (U/mg). The zymogram also revealed a clear hydrolytic zone due to proteolytic activity, which coincided with the band obtained with SDS–PAGE. The enzyme was remained active and stable at pH 8-11, with an optimum at pH 10.0. The protease was stable in the temperature ranging from 40°C to 60°C, but gradually decreased at temperature 70°C. The optimum temperature for protease activity was determined at 60°C. The enzyme showed stability towards non-ionic and anionic surfactants, and oxidizing agents. At 1% concentration of Tween-20 and Tween-80, the enzyme retained 78% and 94% relative activity respectively. Alkaline protease retained 95% activity toward 0.5% concentration of the anionic detergent SDS. The enzyme showed compatibility at 50°C with commercial detergents such as Ariel, Surf excel, Rin, wheel, Tide and Nirma. In the presence of Ariel and Rin the enzyme retained about 72 and 75% of the original activity respectively. The supplementation of the enzyme in detergents could improve the cleansing performance towards the blood stains and suggested to be used as a detergent additive. The enzyme also removed goat hide hairs completely after 15 hr of incubation. These characteristics may make the enzyme suitable for several industrial applications, especially in leather industries.

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