scholarly journals Characterization of intracellular β-galactosidase from Bacillus subtilis 4NK and Bacillus paralicheniformis 5NK isolated from a hot water spring and effects of various inhibitors on enzyme activity

2021 ◽  
Vol 30 (2) ◽  
pp. 71-87
Author(s):  
Şaban TUNÇ ◽  
Fatma MATPAN BEKLER ◽  
Kemal GÜVEN
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Hot Water ◽  
Bacillus Paralicheniformis ◽  
Water Spring

IMMOBILIZATION OF AMYLASE PRODUCING BACTERIA (BACILLUS SUBTILIS) FROM SOIL OF WESTERN HIMALAYAN REGION SOLAN, HIMACHAL PRADESH, INDIA

2021 ◽  
pp. 109-115
Author(s):  
ARUN KUMAR ◽  
POONAM KUMARI ◽  
KASAHUN GUDETA ◽  
JM JULKA
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Physicochemical Properties ◽  
Bacterial Strain ◽  
Enzyme Activities ◽  
Enzyme Assay ◽  
Himachal Pradesh ◽  
Genus Bacillus ◽  
Western Himalayan Region

Objective: The paper aimed to immobilize amylase producing bacterial strain on a suitable matrix and characterization of its physicochemical properties so that much amount of amylase could be produced to be applied in different industries. Methods: Bacterial colonies were sub-cultured from samples collected from soil in freshly prepared dishes containing starch agar by dot method using sterile inoculating needles from which five different bacteria belonged to genus Bacillus were isolated and assigned as A1, A2, A3, A4, and A5. Results: It was found that A1 displayed the highest enzyme activity of 17.89 IU/ml with enzyme assay of 0.83 mg/ml and the bacterium was identified to be Bacillus subtilis. A5 displayed 10.13 IU/ml with protein contents of 0.11 mg/ml indicated that A1 possess the highest enzyme activities which were categorized under Bacillus and protein contents and A5 showed less amount of enzyme activities and protein contents as compared to other. Conclusion: The bacteria which were produced much amount of enzyme activities identified as Bacillus subtilis and recommended and have been recommended to be cultured for the production of amylase enzyme.

Gene cloning and characterization of glycine oxidase from newly isolated Bacillus subtilis strain R5

Biologia ◽  
2011 ◽  
Vol 66 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Farrukh Jamil ◽  
Naeem Rashid ◽  
Qurra-tul-Ann Gardner ◽  
Muhammad Akhtar
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Specific Activity ◽  
Subtilis Strain ◽  
Amino Acid Residues ◽  
Expression And Purification ◽  
Gene Encoding ◽  
Glycine Oxidase ◽  
Bacillus Subtilis Strain R5

AbstractThe gene encoding the glycine oxidase from Bacillus subtilis strain R5 (goxR) was cloned and expressed in Escherichia coli. The gene consisted of 1,110 nucleotides that encoded a protein (GoxR) of 369 amino acid residues with a molecular mass of 40,761 Da. The GoxR exhibited 98.6% identity with glycine oxidase from B. subtilis strain 168. Gene expression and purification of the recombinant GoxR were performed. The recombinant GoxR existed in a homotetramer form. The recombinant protein effectively catalyzed the oxidation of glycine and d-alanine. The specific activity of the purified recombinant GoxR was 0.96 U/mg when glycine was used as a substrate and 1.0 U/mg when d-alanine was substrate. The enzyme displayed its highest activity at pH 8.0 and at a temperature of 50°C. The activation energy of the reaction catalyzed by the enzyme was calculated to be 26 kJ/mol. The enzyme activity was significantly inhibited in the presence of organic solvents. No enhancement of enzyme activity was observed in the presence of metal cations. The experimental results presented in this study demonstrate that the enzyme was a bonafide glycine oxidase.

Enzymic characterization of Bacillus subtilis GTP cyclohydrolase I. Evidence for a chemical dephosphorylation of dihydroneopterin triphosphate

1995 ◽  
Vol 306 (2) ◽  
pp. 371-377 ◽  
Author(s):  
A De Saizieu ◽  
P Vankan ◽  
A P GM van Loon
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Folic Acid ◽  
Physiological Role ◽  
Gtp Cyclohydrolase I ◽  
Gtp Cyclohydrolase ◽  
Folate Biosynthesis

GTP cyclohydrolase I catalyses the first committing step in the biosynthesis of the pterin moiety of folic acid: conversion of GTP to dihydroneopterin triphosphate. GTP cyclohydrolase I of Bacillus subtilis was purified to homogeneity and shown to have a homo-octameric structure. The enzyme had an apparent Km for GTP of 4 microM and, in the absence of cations, a Vmax. of 80 nmol/min per mg of protein. K+ ions moderately increased its Vmax., whereas UTP and Ca2+ and Mg2+ ions drastically increased its Km for GTP. Dihydrofolate and other products of the folate and tetrahydrobiopterin pathways did not inhibit GTP cyclohydrolase I. In addition to their effect on the enzyme activity, Ca2+ and Mg2+ ions catalysed the chemical dephosphorylation of dihydroneopterin triphosphate to non-cyclic dihydroneopterin monophosphate, the substrate for the phosphomonoesterase reaction in folate biosynthesis. This dephosphorylation was specific and did not require the action of a phosphatase. We suggest a physiological role for Ca2+ ions and UTP in regulation of folate biosynthesis at the levels of GTP cyclohydrolase I and dephosphorylation of dihydroneopterin triphosphate.

scholarly journals THE IDENTIFICATION, PRODUCTION AND CHARACTERIZATION OF NATTOKINASE, BACTERIOCIN FROM BACTERIAL SPECIES

2019 ◽  
Vol 2 (4) ◽  
pp. 91
Author(s):  
Lal Krishna
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Pathogenic Bacteria ◽  
Blood Clot ◽  
Bacterial Species ◽  
Antagonistic Activity ◽  
Bacterial Strains ◽  
Wide Range

The study was aimed at identification, production and characterization of nattokinase, bacteriocin from bacterial species. Nattokinase and bacteriocins finds a wide range of applications in Pharmaceutical industry, health care and medicine. Nattokinase is a highly active fibrinolytic enzyme secreted by Bacillus subtilis and bacteriocins are proteinaceous toxins produced by Lactobacillus to inhibit the growth of closely related bacterial strains. Bacillus subtilis and Lactobacillus isolates shown positive results to microscopic, biochemical analysis.  The nattokinase and bacteriocins were produced by optimizing the media. The enzymes were purified by ammonium sulfate precipitation and HPLC. The enzyme activity for nattokinase was found at 7 mg/ml, pH 8.0 and temperature 48 ºC and the enzyme activity for bacteriocin was found at 3.9 mg/ml, pH 6.5 and temperature 30 °C. Bacteriocins from Lactobacillus showed good antagonistic activity against pathogenic bacteria. Nattokinase from Bacillus subtilis played a significant role in thrombolytic and anti-coagulation at in vitro. The results indicated that the pure enzyme has a potential in dissolving blood clot.

Production and partial characterization of elastase of Bacillus subtilis isolated from the cervices of human females

1988 ◽  
Vol 34 (7) ◽  
pp. 855-859 ◽  
Author(s):  
Mohinder Kaur ◽  
K. K. Tripathi ◽  
Meenakshi Gupta ◽  
P. K. Jain ◽  
M. R. Bansal ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Ammonium Sulphate ◽  
Phosphate Buffer ◽  
Gel Filtration ◽  
Ammonium Sulphate Precipitation ◽  
Tris Maleate ◽  
Culture Supernatants

Conditions are described for the production of extracellular elastase by Bacillus subtilis. The yield of enzyme was maximum in shake–cultures grown in Syncase medium at 37 °C and was stable in culture supernatants. The enzyme, purified by ammonium sulphate precipitation and Sephadex G-75 gel filtration, showed a molecular weight of 25 000 and activity between pH 6.0 and 9.5, with an optimum of 9.0 in Tris–maleate buffer. Elastinolytic activity was maximum in glycine–NaOH buffer and minimum in phosphate buffer. Enzyme activity was adversely affected by temperature ≥ 40 °C.

scholarly journals Biochemical, molecular and in silico characterization of arsenate reductase from pH, salt and arsenic tolerant Bacillus thuringiensis KPWP1

2021 ◽  
Author(s):  
Paromita Banerjee ◽  
Ananya Chatterjee ◽  
Sushmita Jha ◽  
Nirbhay Bhadani ◽  
Partha Datta ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Bacillus Subtilis ◽  
Surface Water ◽  
Bacillus Thuringiensis ◽  
Bacillus Cereus ◽  
Binding Site ◽  
In Silico ◽  
Arsenate Tolerance ◽  
In Silico Characterization

Abstract The objective of the present study was to characterize aresenate reductase of pH, salt and arsenate tolerant Bacillus thuringiensis KPWP1, isolated from contaminated surface water. Interestingly, it was found that the arsC, arsB and arsR genes involved in arsenate tolerance are distributed in the genome of KPWP1. The inducible arsC gene was cloned, expressed and the purified ArsC protein showed profound enzyme activity with the KM and Kcat values as 25 µM and 0.00119 s− 1, respectively. In silico studies of KPWP1 ArsC revealed that in spite of 19–26% differences in gene sequences, the ArsC proteins of Bacillus thuringiensis, Bacillus subtilis and Bacillus cereus are structurally conserved and KPWP1 ArsC structure is close to nature. Docking and analysis of binding site showed that arsenate ion interacts with three cysteine residues of ArsC of KPWP1and predicts that the ArsC from B. thuringiensis reduces arsenate by using the triple Cys redox relay mechanism.

scholarly journals Characterization of hot water spring source isolated clones of bacteria and their industrial applicability

2010 ◽  
Vol 2 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Gopala Rao TV ◽  
◽  
Sudip Kumar Sen ◽  
Sudhir Kumar Mohapatra ◽  
Soumya Satpathy
Keyword(s):  
Hot Water ◽  
Water Spring

Characterization of dissolved organic matter (DOM) extracted from soils by hot water percolation (HWP)

2010 ◽  
Vol 59 (1) ◽  
pp. 99-108 ◽  
Author(s):  
M. Takács ◽  
Gy. Füleky
Keyword(s):  
Organic Matter ◽  
Humic Acid ◽  
Natural Organic Matter ◽  
Extraction Methods ◽  
Soil Samples ◽  
Hot Water ◽  
Soil Extracts ◽  
Water Percolation ◽  
Soil Humic Acid

The Hot Water Percolation (HWP) technique for preparing soil extracts has several advantages: it is easily carried out, fast, and several parameters can be measured from the same solution. The object of this study was to examine the possible use of HWP extracts for the characterization of soil organic matter. The HPLC-SEC chromatograms, UV-VIS and fluorescence properties of the HWP extracts were studied and the results were compared with those of the International Humic Substances Society (IHSS) Soil Humic Acid (HA), IHSS Soil Fulvic Acid (FA) and IHSS Suwannee Natural Organic Matter (NOM) standards as well as their HA counterparts isolated by traditional extraction methods from the original soil samples. The DOM of the HWP solution is probably a mixture of organic materials, which have some characteristics similar to the Soil FA fractions and NOM. The HWP extracted organic material can be studied and characterized using simple techniques, like UV-VIS and fluorescence spectroscopy.

Sign in / Sign up

Export Citation Format

Share Document