scholarly journals Characterization of Pectinase from Bacillus subtilis Strain Btk 27 and Its Potential Application in Removal of Mucilage from Coffee Beans

2017 ◽  
Vol 2017 ◽  
pp. 1-7 ◽  
Author(s):  
Oliyad Jeilu Oumer ◽  
Dawit Abate
Keyword(s):  
Bacillus Subtilis ◽  
Potential Application ◽  
Tween 80 ◽  
Complete Removal ◽  
Industrial Applications ◽  
Global Market ◽  
Tween 20 ◽  
Subtilis Strain ◽  
Coffee Beans ◽  
Fast Pace

The demand for enzymes in the global market is projected to rise at a fast pace in recent years. There has been a great increase in industrial applications of pectinase owing to their significant biotechnological uses. For applying enzymes at industrial scale primary it is important to know the features of the enzyme. Thus, this study was undertaken with aims of characterizing the pectinase enzyme from Bacillus subtilis strain Btk27 and proving its potential application in demucilisation of coffee. In this study, the maximum pectinase activity was achieved at pH 7.5 and 50°C. Also, the enzyme activity was found stimulated with Mg2+ and Ca2+ metal ions. Moreover, it was stable on EDTA, Trixton-100, Tween 80, and Tween 20. Since Bacillus subtilis strain Btk27 was stable in most surfactants and inhibitors it could be applicable in various industries whenever pectin degradation is needed. The enzyme Km and Vmax values were identified as 1.879 mg/ml and 149.6 U, respectively. The potential application of the enzyme for coffee processing was studied, and it is found that complete removal of mucilage from coffee beans within 24 hours of treatment indicates the potential application in coffee processing.

scholarly journals Comparative Studies of Pectinase Production byBacillus subtilis strain Btk 27in Submerged and Solid-State Fermentations

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Oliyad Jeilu Oumer ◽  
Dawit Abate
Keyword(s):  
Solid State ◽  
Wheat Bran ◽  
Solid State Fermentation ◽  
Submerged Fermentation ◽  
Industrial Applications ◽  
Global Market ◽  
Subtilis Strain ◽  
Fast Pace ◽  
Initial Ph ◽  
Pectinase Production

The request for enzymes in the global market is expected to rise at a fast pace in recent years. With this regard, there has been a great increase in industrial applications of pectinase owing to their significant biotechnological uses. This study was undertaken with main objectives of meeting the growing industrial demands of pectinase, by improving the yield without increasing the cost of production. In addition, this research highlights the underestimated potential of agroresidues for the production of biotechnologically important products. In this study, the maximum pectinase production attained was using wheat bran, among the tested agroresidues. The production of pectinase was improved from 10.1 ± 1.4 U/ml to 66.3 ± 1.2 U/ml in submerged fermentation whereas it was in solid state fermentation from 800.0 ± 16.2 U/g to 1272.4 ± 25.5 U/g. The maximum pectinase production was observed using YEP (submerged fermentation) and wheat bran (solid state fermentation) at initial pH of 6.5, at 37°C and by supplementing the medium with 3 mM MgSO4.7H2O.

scholarly journals Biochemical Characterization of Cellulase From Bacillus subtilis Strain and its Effect on Digestibility and Structural Modifications of Lignocellulose Rich Biomass

2021 ◽  
Vol 9 ◽  
Author(s):  
Waseem Ayoub Malik ◽  
Saleem Javed
Keyword(s):  
Bacillus Subtilis ◽  
Biochemical Characterization ◽  
Biomass Conversion ◽  
Industrial Applications ◽  
Partial Purification ◽  
Subtilis Strain ◽  
Complex Nature ◽  
Structural Modifications ◽  
Optimum Activity

Microbial cellulases have become the mainstream biocatalysts due to their complex nature and widespread industrial applications. The present study reports the partial purification and characterization of cellulase from Bacillus subtilis CD001 and its application in biomass saccharification. Out of four different substrates, carboxymethyl cellulose, when amended as fermentation substrate, induced the highest cellulase production from B. subtilis CD001. The optimum activity of CMCase, FPase, and amylase was 2.4 U/ml, 1.5 U/ml, and 1.45 U/ml, respectively. The enzyme was partially purified by (NH4)2SO4 precipitation and sequenced through LC-MS/MS. The cellulase was found to be approximately 55 kDa by SDS-PAGE and capable of hydrolyzing cellulose, as confirmed by zymogram analysis. The enzyme was assigned an accession number AOR98335.1 and displayed 46% sequence homology with 14 peptide-spectrum matches having 12 unique peptide sequences. Characterization of the enzyme revealed it to be an acidothermophilic cellulase, having an optimum activity at pH 5 and a temperature of 60°C. Kinetic analysis of partially purified enzyme showed the Km and Vmax values of 0.996 mM and 1.647 U/ml, respectively. The enzyme activity was accelerated by ZnSO4, MnSO4, and MgSO4, whereas inhibited significantly by EDTA and moderately by β-mercaptoethanol and urea. Further, characterization of the enzyme saccharified sugarcane bagasse, wheat straw, and filter paper by SEM, ATR-FTIR, and XRD revealed efficient hydrolysis and structural modifications of cellulosic materials, indicating the potential industrial application of the B. subtilis CD001 cellulase. The findings demonstrated the potential suitability of cellulase from B. subtilis CD001 for use in current mainstream biomass conversion into fuels and other industrial processes.

Bacillus velezensis Identification and Recombinant Expression, Purification and Characterization of Its Alpha-Amylase

Fermentation ◽  
2021 ◽  
Vol 7 (4) ◽  
pp. 227
Author(s):  
Xiaodong Zhang ◽  
Caixia Li ◽  
Xuantong Chen ◽  
Chonlong Chio ◽  
Sarita Shrestha ◽  
...  
Keyword(s):  
Recombinant Expression ◽  
Industrial Applications ◽  
Global Market ◽  
Tween 20 ◽  
Bacillus Velezensis ◽  
Modeled Structure ◽  
Wide Range ◽  
Relative Molecular Weight ◽  
Industrial Needs ◽  
Triton X

Amylases account for about 30% of the global market of industrial enzymes, and the current amylases cannot fully meet industrial needs. This study aimed to identify a high α-amylase producing bacterium WangLB, to clone its α-amylase coding gene, and to characterize the α-amylase. Results showed that WangLB belonged to Bacillus velezensis whose α-amylase gene was 1980 bp coding 659 amino acids designated as BvAmylase. BvAmylase was a hydrophilic stable protein with a signal peptide and a theoretical pI of 5.49. The relative molecular weight of BvAmylase was 72.35 kDa, and was verified by SDS-PAGE. Its modeled structure displayed that it was a monomer composed of three domains. Its optimum temperature and pH were 70 °C and pH 6.0, respectively. It also showed high activity in a wide range of temperatures (40–75 °C) and a relatively narrow pH (5.0–7.0). It was a Ca2+-independent enzyme, whose α-amylase activity was increased by Co2+, Tween 20, and Triton X-100, and severely decreased by SDS. The Km and the Vmax of BvAmylase were 3.43 ± 0.53 and 434.19 ± 28.57 U/mg. In conclusion, the α-amylase producing bacterium WangLB was identified, and one of its α-amylases was characterized, which will be a candidate enzyme for industrial applications.

scholarly journals Developing auto-inducible Pgrac57 promoter in Bacillus subtilis

2019 ◽  
Vol 15 (3) ◽  
pp. 100
Author(s):  
Phan Thi Phương Trang ◽  
Tran Thi Anh Dao ◽  
Truong Thi Lan Lan ◽  
Nguyen Thuy Mỹ Linh ◽  
Au Thi Hanh ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Recombinant Proteins ◽  
Potential Application ◽  
Expression Vector ◽  
Cellular Proteins ◽  
Vector System ◽  
Free Expression ◽  
Subtilis Strain ◽  
Industrial Enzymes ◽  
Gfp Expression

Bacillus subtilis has many advantages such as: safe, non-pathogenic, endotoxin-free features. Therefore, B. subtilis has been widely ultilized in therapeutic proteins and important industrial enzymes production. Over the last few years, the potential application of B. subtilis for recombinant proteins synthesis has been significantly enhanced by using pHT - vector system with Pgrac promoter. In this study, we developed inducer-free expression vector for B. subitlis based on Pgrac57 promoter and used GFP protein as a reporter. The results showed that we successfully constructed inducer-free vector pHT1686 with Pgrac57 promoters. These vectors are totally able to express GFP protein without any inducer in B. subtilis strain 1012. Moreover, GFP expression level reached 11% of the total cellular proteins. Additionally, GFP activities are in the same range with the inducer-free vector.

scholarly journals Potential application of gold nanoparticles in food packaging: a mini review

Gold Bulletin ◽  
2021 ◽  
Author(s):  
Saeed Paidari ◽  
Salam Adnan Ibrahim
Keyword(s):  
Gold Nanoparticles ◽  
Potential Application ◽  
Food Industry ◽  
Food Packaging ◽  
Industrial Applications ◽  
Mechanisms Of Action ◽  
Microbial Load ◽  
Food Sector ◽  
The Past ◽  
Industry Applications

AbstractIn the past few decades, there have been remarkable advances in our knowledge of gold nanoparticles (AuNPs) and synthesizing methods. AuNPs have become increasingly important in biomedical and industrial applications. As a newly implemented method, AuNPs are being used in nanopackaging industries for their therapeutic and antibacterial characteristics as well as their inert and nontoxic nature. As with other NPs, AuNPs have privileges and disadvantages when utilized in the food sector, yet a significant body of research has shown that, due to the specific nontoxic characteristics, AuNPs could be used to address other NP flaws. In this mini review, we present synthesizing methods, food industry applications, and mechanisms of action of gold nanoparticles. Regarding the investigations, gold nanoparticles can play a major role to reduce microbial load in foodstuff and therefore can be implemented in food packaging as an effective approach.

scholarly journals Complete Genome Sequence of Bacillus subtilis subsp. subtilis Strain ∆6

2016 ◽  
Vol 4 (4) ◽  
Author(s):  
Daniel R. Reuß ◽  
Andrea Thürmer ◽  
Rolf Daniel ◽  
Wim J. Quax ◽  
Jörg Stülke
Keyword(s):  
Bacillus Subtilis ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Full Genome Sequence ◽  
Subtilis Strain ◽  
Full Genome ◽  
Biotechnological Applications ◽  
A Genome ◽  
Subtilis Subsp

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.

scholarly journals Intracellular serine proteinase of Bacillus subtilis strain Marburg 168. Comparison with the homologous enzyme from Bacillus subtilis strain A-50

1979 ◽  
Vol 179 (2) ◽  
pp. 333-339 ◽  
Author(s):  
A Y Strongin ◽  
D I Gorodetsky ◽  
I A Kuznetsova ◽  
V V Yanonis ◽  
Z T Abramov ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Serine Proteinase ◽  
Subtilis Strain ◽  
Bacterial Strains ◽  
Terminal Sequence ◽  
Gramicidin S ◽  
Intracellular Enzymes ◽  
Sepharose 4B ◽  
Homologous Enzyme ◽  
Strict Selection

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.

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