scholarly journals Novel Recombinant keratin Degrading Subtilisin Like Serine Alkaline Protease from Bacillus Cereus Isolated from Marine Hydrothermal Vent Crabs 

2020 ◽  
Author(s):  
Revathi Gurunathan ◽  
Bin Huang ◽  
Vinoth Kumar Ponnusamy ◽  
Jiang-Shiou Hwang ◽  
Hans-Uwe Dahms
Keyword(s):  
Bacillus Cereus ◽  
Hydrothermal Vents ◽  
Extreme Environments ◽  
Serine Proteinase ◽  
Value Added ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Protease Gene ◽  
Hydrolytic Activities ◽  
Promising Source

Abstract Microbial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 ℃) ranges, with maximal hydrolytic activities at pH 10 and at 50 ℃ temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non- anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicate that the protein is suitable for waste management and value-added product synthesis as well as several research applications.

scholarly journals Novel recombinant keratin degrading subtilisin like serine alkaline protease from Bacillus cereus isolated from marine hydrothermal vent crabs

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Revathi Gurunathan ◽  
Bin Huang ◽  
Vinoth Kumar Ponnusamy ◽  
Jiang-Shiou Hwang ◽  
Hans-Uwe Dahms
Keyword(s):  
Bacillus Cereus ◽  
Hydrothermal Vents ◽  
Extreme Environments ◽  
Serine Proteinase ◽  
Value Added ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Protease Gene ◽  
Hydrolytic Activities ◽  
Promising Source

AbstractMicrobial secondary metabolites from extreme environments like hydrothermal vents are a promising source for industrial applications. In our study the protease gene from Bacillus cereus obtained from shallow marine hydrothermal vents in the East China Sea was cloned, expressed and purified. The protein sequence of 38 kDa protease SLSP-k was retrieved from mass spectrometry and identified as a subtilisin serine proteinase. The novel SLSP-k is a monomeric protein with 38 amino acid signal peptides being active over wide pH (7–11) and temperature (40–80 °C) ranges, with maximal hydrolytic activities at pH 10 and at 50 °C temperature. The hydrolytic activity is stimulated by Ca2+, Co2+, Mn2+, and DTT. It is inhibited by Fe2+, Cd2+, Cu2+, EDTA, and PMSF. The SLSP-k is stable in anionic, non-anionic detergents, and solvents. The ability to degrade keratin in chicken feather and hair indicates that this enzyme is suitable for the degradation of poultry waste without the loss of nutritionally essential amino acids which otherwise are lost in hydrothermal processing. Therefore, the proteinase is efficient in environmental friendly bioconversion of animal waste into fertilizers or value added products such as secondary animal feedstuffs.

scholarly journals The identification of distinctive forms of human α2-macroglobulin by using the numerical relationship between trypsin binding in α- and β-modes

1979 ◽  
Vol 177 (2) ◽  
pp. 501-508 ◽  
Author(s):  
R M Topping ◽  
A H Craven
Keyword(s):  
Bound States ◽  
Proteinase Inhibitors ◽  
Serine Proteinase ◽  
Preceding Paper ◽  
Hydrolytic Activity ◽  
Clinical Value ◽  
Straight Line ◽  
Hydrolytic Activities ◽  
Linear Differential ◽  
Alpha 1 Antitrypsin

Interactions between the serine proteinase trypsin and the protein proteinase inhibitors in human blood were expressed in terms of a coupled set of non-linear differential equations, which has been solved for each of 110 samples of serum obtained from colleagues and from a variety of hospital sources. Optimization of nine unknown theoretical parameters and 21 experimental rate measurements of the hydrolytic activity of trypsin in free and bound states after admixture with various amounts of a given serum was achieved by an iterative procedure using initial estimates of the parameters derived from the “four-straight-line” model described in the preceding paper [Topping & Seilman (1979) Biochem. J. 177, 493–499.] Such a procedure yielded the following information for each sample of serum examined: (a) the concentrations of alpha 1-antitrypsin and alpha 2-macroglobulin; (b) the unequivocal assignment of alpha 2-macroglobulin into one of seven categories on the basis of trypsin binding in two kinetically differentiated modes (alpha and beta); (c) the hydrolytic activities of trypsin (versus Bz-Arg-OEt) when bound to alpha 1-antitrypsin, and to alpha 2-macroglobulin in the alpha- and beta-modes. Molecular interpretations of the binding of trypsin to alpha 2-macroglobulin are discussed and the potential clinical value of recognizing the nature of such binding is reported.

Thermophilic Bacterial Exopolysaccharides

2022 ◽  
pp. 334-361
Author(s):  
Rakesh Goswami ◽  
Bidyut Bandyopadhyay ◽  
Sanjoy Sadhukhan
Keyword(s):  
Hydrothermal Vents ◽  
Extracellular Polymeric Substances ◽  
Hot Spring ◽  
Carbon Sources ◽  
Extreme Environments ◽  
Value Added ◽  
Low Ph ◽  
Extreme Conditions ◽  
Biotechnological Applications ◽  
Bacterial Exopolysaccharides

Bacterial exopolysaccharides have enormous diversity with valuable characteristics, synthesized by various pathways in extreme conditions like salinity, geothermal springs, or hydrothermal vents. Due to extreme environments, these microorganisms have various adaption principles (e.g., low pH, high temperature, high saltation, and high radiation). Exopolysaccharide is an organic compound produced by most bacteria during fermentation using various carbon sources, resulting in a jelly-like or mass network structure outside the cell wall. This biopolymer has an adherent cohesive layer throughout the cell layer. Hot spring bacterial polysaccharides contain diverse extracellular polymeric substances. With a gain in popularity in applications of thermophilic microbial polysaccharides and its demand in diverse value-added industrial products, this chapter aims to provide valuable information on the physicochemical function and biotechnological applications in the field of food, medical imaging, nano-drugs, bioremediation, cancer, anti-bacterial, tissue engineering, etc.

scholarly journals Complete Genome Sequence of the Extremophilic Bacillus cereus Strain Q1 with Industrial Applications

2008 ◽  
Vol 191 (3) ◽  
pp. 1120-1121 ◽  
Author(s):  
Zhaohui Xiong ◽  
Yan Jiang ◽  
Danhua Qi ◽  
Huaibao Lu ◽  
Fan Yang ◽  
...  
Keyword(s):  
Bacillus Cereus ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Extreme Environments ◽  
Industrial Applications ◽  
Northeastern China ◽  
Oil Field ◽  
Oil Reservoir ◽  
Deep Subsurface ◽  
Daqing Oil Field

ABSTRACT Bacillus cereus strain Q1 was isolated from a deep-subsurface oil reservoir in the Daqing oil field in northeastern China. This strain is able to produce biosurfactants and to survive in extreme environments. Here we report the finished and annotated genome sequence of this organism.

Purification and Characterization of Natural Solid-Substrate Degrading and Alcohol Producing Hyperthermostable Alkaline Amylase from Bacillus cereus (sm-sr14)

2020 ◽  
Vol 21 (9) ◽  
pp. 872-881
Author(s):  
Sumit Sahoo ◽  
Sudipta Roy ◽  
Dipannita Santra ◽  
Sayantani Maiti ◽  
Sonali Roul ◽  
...  
Keyword(s):  
Bacillus Cereus ◽  
Main Property ◽  
Solid Substrate ◽  
Industrial Applications ◽  
Starch Degradation ◽  
Significant Similarity ◽  
Alcohol Production ◽  
Cazy Database ◽  
Tim Barrel ◽  
Alkaline Amylase

Objective: Amylases enzymes hydrolyze starch molecules to produce diverse products including dextrins, and progressively smaller polymers. These include glucose units linked through α-1- 1, α-1-4, α-1-6, glycosidic bonds. Methods: This enzyme carrying an (α /β) 8 or TIM barrel structure is also produced containing the catalytic site residues. These groups of enzymes possess four conserved regions in their primary sequence. In the Carbohydrate-Degrading Enzyme (CAZy) database, α-amylases are classified into different Glycoside Hydrolase Families (GHF) based on their amino acid sequence. The present objective was to study one such enzyme based on its molecular characterization after purification in our laboratory. Its main property of solid-natural starch degradation was extensively investigated for its pharmaceutical/ industrial applications. Results: Amylase producing bacteria Bacillus cereus sm-sr14 (Accession no. KM251578.1) was purified to homogeneity on a Seralose 6B-150 gel-matrix and gave a single peak during HPLC. MALDITOF mass-spectrometry with bioinformatics studies revealed its significant similarity to α/β hydrolase family. The enzyme showed an efficient application; favourable Km, Vmax and Kcat during the catalysis of different natural solid starch materials. Analysis for hydrolytic product showed that this enzyme can be classified as the exo-amylase asit produced a significant amount of glucose. Conclusion: Besides the purified enzyme, the present organism Bacillus cereus sm-sr14 could degrade natural solid starch materials like potato and rice up to the application level in the pharmaceutical/ industrial field for alcohol production.

scholarly journals Effects of a Twin-Screw Extruder Equipped with a Molten Resin Reservoir on the Mechanical Properties and Microstructure of Recycled Waste Plastic Polyethylene Pellet Moldings

Polymers ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1058
Author(s):  
Hikaru Okubo ◽  
Haruka Kaneyasu ◽  
Tetsuya Kimura ◽  
Patchiya Phanthong ◽  
Shigeru Yao
Keyword(s):  
Mechanical Properties ◽  
Mechanical Performance ◽  
Value Added ◽  
Industrial Applications ◽  
Twin Screw Extruder ◽  
Screw Extruder ◽  
Polymer Properties ◽  
Wide Range ◽  
Twin Screw ◽  
Recycled Plastics

Each year, increasing amounts of plastic waste are generated, causing environmental pollution and resource loss. Recycling is a solution, but recycled plastics often have inferior mechanical properties to virgin plastics. However, studies have shown that holding polymers in the melt state before extrusion can restore the mechanical properties; thus, we propose a twin-screw extruder with a molten resin reservoir (MSR), a cavity between the screw zone and twin-screw extruder discharge, which retains molten polymer after mixing in the twin-screw zone, thus influencing the polymer properties. Re-extruded recycled polyethylene (RPE) pellets were produced, and the tensile properties and microstructure of virgin polyethylene (PE), unextruded RPE, and re-extruded RPE moldings prepared with and without the MSR were evaluated. Crucially, the elongation at break of the MSR-extruded RPE molding was seven times higher than that of the original RPE molding, and the Young’s modulus of the MSR-extruded RPE molding was comparable to that of the virgin PE molding. Both the MSR-extruded RPE and virgin PE moldings contained similar striped lamellae. Thus, MSR re-extrusion improved the mechanical performance of recycled polymers by optimizing the microstructure. The use of MSRs will facilitate the reuse of waste plastics as value-added materials having a wide range of industrial applications.

Mutations affecting the activity of the cyclodextrin glucanotransferase of Paenibacillus pabuli US132: insights into the low hydrolytic activity of cyclodextrin glucanotransferases

Biologia ◽  
2012 ◽  
Vol 67 (4) ◽  
Author(s):  
Sonia Jemli ◽  
Mamdouh Ben-Ali ◽  
Hajer Ben-Hlima ◽  
Bassem Khemakhem ◽  
Samir Bejar
Keyword(s):  
Hydrolytic Activity ◽  
Influential Factor ◽  
Rational Approach ◽  
Cyclodextrin Glucanotransferase ◽  
Hydrolytic Activities ◽  
Maltogenic Amylase ◽  
Structural Barrier ◽  
First Time

AbstractThe cyclodextrin glucanotransferase from Paenibacillus pabuli US132 (US132 CGTase) was engineered using a rational approach in an attempt to provide it with anti-staling properties comparable to those of the commercial maltogenic amylase (Novamyl). The study aimed to concurrently decrease the cyclization activity and increase the hydrolytic activity of US132 CGTase. A five-residue loop (PAGFS) was inserted, alone or with the substitution of essential residues for cyclization (G180, L194 and Y195), mimicking the case of Novamyl. The findings indicate that, unlike the case of the CGTase of Thermoanerobacterium thermosulfurigenes strain EM1 whose initial high hydrolytic activity was exceptional, these mutations completely abolished the cyclization and hydrolytic activities of the US132 CGTase. This suggests that those mutations are not able to convert conventional CGTases, whose hydrolytic activities are very weak, into hydrolases. Accordingly, and for the first time, a structural barrier at subsite −3 was advanced as an influential factor which might explain the low hydrolytic activity of conventional CGTases.

scholarly journals Properties of a new fungal b-galactosidase with potential application in the dairy industry

1999 ◽  
Vol 30 (3) ◽  
pp. 265-271 ◽  
Author(s):  
Rubens Cruz ◽  
Vinícius D'Arcádia Cruz ◽  
Juliana Gisele Belote ◽  
Marcelo de Oliveira Khenayfes ◽  
Claudia Dorta ◽  
...  
Keyword(s):  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Transferase Activity ◽  
Optimum Temperature ◽  
Milk Whey ◽  
Beneficial Effects ◽  
Optimum Ph ◽  
Semi Solid ◽  
Good Productivity ◽  
Hydrolysis Of

<FONT FACE="Symbol">b</font>-Galactosidase or <FONT FACE="Symbol">b</font>-D-galactoside-galactohydrolase (EC. 3.2.1.23) is an important enzyme industrially used for the hydrolysis of lactose from milk and milk whey for several applications. Lately, the importance of this enzyme was enhanced by its galactosyltransferase activity, which is responsible for the synthesis of transgalactosylated oligosaccharides (TOS) that act as functional foods, with several beneficial effects on consumers. Penicillium simplicissimum, a strain isolated from soil, when grown in semi-solid medium showed good productivity of <FONT FACE="Symbol">b</font>-galactosidase with galactosyltransferase activity. The optimum pH for hydrolysis was in the 4.04.6 range and the optimum pH for galactosyltransferase activity was in the 6.07.0 range. The optimum temperature for hydrolysis and transferase activity was 55-60°C and 50°C, respectively, and the enzyme showed high thermostability for the hydrolytic activity. The enzyme showed a potential for several industrial applications such as removal of 67% of the lactose from milk and 84% of the lactose from milk whey when incubated at their original pH (4.5 and 6.34, respectively) under optimum temperature conditions. When incubated with a 40% lactose solution in 150 mM McIlvaine buffer, pH 4.5, at 55°C the enzyme converted 86.5% of the lactose to its component monosaccharides. When incubated with a 60% lactose solution in the same buffer but at pH 6.5 and 50°C, the enzyme can synthetize up to 30.5% TOS, with 39.5% lactose and 30% monosaccharides remaining in the preparation.

scholarly journals Extremophilic Exopolysaccharides: Biotechnologies and Wastewater Remediation

2021 ◽  
Vol 12 ◽  
Author(s):  
Aparna Banerjee ◽  
Shrabana Sarkar ◽  
Tanvi Govil ◽  
Patricio González-Faune ◽  
Gustavo Cabrera-Barjas ◽  
...  
Keyword(s):  
Hydrothermal Vents ◽  
Hot Springs ◽  
Mine Drainage ◽  
Oil Spills ◽  
Extreme Environments ◽  
Substantial Part ◽  
Wastewater Remediation ◽  
Water Contaminants ◽  
Chemical Groups ◽  
Trace And Toxic Metals

Various microorganisms thrive under extreme environments, like hot springs, hydrothermal vents, deep marine ecosystems, hyperacid lakes, acid mine drainage, high UV exposure, and more. To survive against the deleterious effect of these extreme circumstances, they form a network of biofilm where exopolysaccharides (EPSs) comprise a substantial part. The EPSs are often polyanionic due to different functional groups in their structural backbone, including uronic acids, sulfated units, and phosphate groups. Altogether, these chemical groups provide EPSs with a negative charge allowing them to (a) act as ligands toward dissolved cations as well as trace, and toxic metals; (b) be tolerant to the presence of salts, surfactants, and alpha-hydroxyl acids; and (c) interface the solubilization of hydrocarbons. Owing to their unique structural and functional characteristics, EPSs are anticipated to be utilized industrially to remediation of metals, crude oil, and hydrocarbons from contaminated wastewaters, mines, and oil spills. The biotechnological advantages of extremophilic EPSs are more diverse than traditional biopolymers. The present review aims at discussing the mechanisms and strategies for using EPSs from extremophiles in industries and environment bioremediation. Additionally, the potential of EPSs as fascinating biomaterials to mediate biogenic nanoparticles synthesis and treat multicomponent water contaminants is discussed.

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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