scholarly journals SCREENING OF L-ASPARAGINASE THE SALT-TOLERANT AND THERMOSTABLE MARINE BACILLUS SUBTILIS STRAIN SR61

2019 ◽  
pp. 93-100
Author(s):  
Bruno Oliveira de Veras ◽  
Yago Queiroz dos Santos ◽  
Anderson Felipe Jácome de França ◽  
Penha Patricia Cabral Ribeiro ◽  
Elaine Costa Almeida Barbosa ◽  
...  
F1000Research ◽  
2018 ◽  
Vol 7 ◽  
pp. 1704 ◽  
Author(s):  
Bruno Oliveira de Veras ◽  
Yago Queiroz dos Santos ◽  
Katharina Marquez Diniz ◽  
Gabriela Silva Campos Carelli ◽  
Elizeu Antunes dos Santos

Background:The marine environment harbours different microorganisms that inhabit niches with adverse conditions, such as temperature variation, pressure and salinity. To survive these particular conditions, marine bacteria use unique metabolic and biochemical features, producing enzymes that may have industrial value.Methods:The aim of this study was to observe the production of multiple thermoenzymes and haloenzymes, including protease, cellulase, amylase and xylanase, from bacterial strains isolated from coral reefs Cabo Branco, Paraiba State, Brazil. Strain SR60 was identified by the phylogenetic analysis to beBacillus subtilisthrough a 16S ribosomal RNA assay. To screening of multiples enzymesB. subtilisSR60 was inoculated in differential media to elicit the production of extracellular enzymes with the addition of a range of salt concentrations (0, 0.25, 0.50, 1.0, 1.25 and 1.5 M NaCl).Results:The screening showed a capacity of production of halotolerant protease, cellulase, amylase and xylanase and thermostable by the isolate (identified asB. subtilisSR60). Protease, cellulase, amylase and xylanase production were limited to 1.5, 1.5, 1.0 and 1.25 M NaCl, respectively.Conclusions:Bacillus subtilisSR60 was shown in this study be capable of producing protease, cellulase, amylase and xylanase when submitted to a high salinity environment. These data demonstrate the halophytic nature of SR60 and its ability to produce multiples enzymes.


2016 ◽  
Vol 4 (4) ◽  
Author(s):  
Daniel R. Reuß ◽  
Andrea Thürmer ◽  
Rolf Daniel ◽  
Wim J. Quax ◽  
Jörg Stülke

Bacillus subtilis ∆6 is a genome-reduced strain that was cured from six prophages and AT-rich islands. This strain is of great interest for biotechnological applications. Here, we announce the full-genome sequence of this strain. Interestingly, the conjugative element ICE Bs 1 has most likely undergone self-excision in B. subtilis ∆6.


1979 ◽  
Vol 179 (2) ◽  
pp. 333-339 ◽  
Author(s):  
A Y Strongin ◽  
D I Gorodetsky ◽  
I A Kuznetsova ◽  
V V Yanonis ◽  
Z T Abramov ◽  
...  

Intracellular serine proteinase was isolated from sporulating cells of Bacillus subtilis Marburg 168 by gramicidin S-Sepharose 4B affinity chromatography. The enzymological characteristics, the amino acid composition and the 19 residues of the N-terminal sequence of the enzyme are reported. The isolated proteinase was closely related to, but not completely identical with, the intracellular serine proteinase of B. subtilis A-50. The divergence between these two intracellular enzymes was less than that between the corresponding extracellular serine proteinases (subtilisins) of types Carlsberg and BPN′!, produced by these bacterial strains. This may be connected with the more strict selection constraints imposed in intracellular enzymes during evolution.


2017 ◽  
Vol 12 (1) ◽  
pp. 255-263 ◽  
Author(s):  
Kanjana Thumanu ◽  
Darawadee Wongchalee ◽  
Mathukorn Sompong ◽  
Piyaporn Phansak ◽  
Toan Le Thanh ◽  
...  

Microbiology ◽  
2008 ◽  
Vol 154 (1) ◽  
pp. 54-63 ◽  
Author(s):  
Kazuo Kobayashi ◽  
Ritsuko Kuwana ◽  
Hiromu Takamatsu

Author(s):  
Meichun Chen ◽  
Meixia Zheng ◽  
Yanping Chen ◽  
Rongfeng Xiao ◽  
Xuefang Zheng ◽  
...  

2018 ◽  
Vol 7 (18) ◽  
Author(s):  
Haeyoung Jeong ◽  
Da-Eun Jeong ◽  
Seung-Hwan Park ◽  
Seong Joo Kim ◽  
Soo-Keun Choi

Bacillus subtilis WB800N is a genetically engineered variant of B. subtilis 168, such that all extracellular proteases are disrupted, which enables WB800N to be widely used for the expression of secretory proteins. Here, we report the 4.2-Mb complete genome sequence of WB800N and present all of the disrupted gene structure.


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