scholarly journals Identification of a Novel Thermostable Alkaline Protease from Bacillus megaterium-TK1 for the Detergent and Leather Industry

Biology ◽  
2020 ◽  
Vol 9 (12) ◽  
pp. 472
Author(s):  
Tamilvendan Manavalan ◽  
Arulmani Manavalan ◽  
Shiyamsundar Ramachandran ◽  
Klaus Heese
Keyword(s):  
Serine Protease ◽  
Bacillus Megaterium ◽  
Industrial Applications ◽  
Phenylmethylsulfonyl Fluoride ◽  
Serine Hydrolase ◽  
Leather Industry ◽  
Bivalent Metal ◽  
Green Industry ◽  
Proteolytic Action ◽  
Relative Molecular Weight

An increased need by the green industry for enzymes that can be exploited for eco-friendly industrial applications led us to isolate and identify a unique protease obtained from a proteolytic Bacillus megaterium-TK1 strain from a seawater source. The extracellular thermostable serine protease was processed by multiple chromatography steps. The isolated protease displayed a relative molecular weight (MW) of 33 kDa (confirmed by zymography), optimal enzyme performance at pH 8.0, and maximum enzyme performance at 70 °C with 100% substrate specificity towards casein. The proteolytic action was blocked by phenylmethylsulfonyl fluoride (PMSF), a serine hydrolase inactivator. Protease performance was augmented by several bivalent metal cations. The protease tolerance was studied under stringent conditions with different industrial dispersants and found to be stable with Surf Excel, Tide, or Rin detergents. Moreover, this protease could clean blood-stained fabrics and showed dehairing activity for cow skin with significantly reduced pollution loads. Our results suggest that this serine protease is a promising additive for various eco-friendly usages in both the detergent and leather industries.

scholarly journals Production and Characterization of Keratinolytic Protease of Bacillus licheniformis MZK-03 Grown on Feather Mill

1970 ◽  
Vol 24 (1) ◽  
pp. 57-61 ◽  
Author(s):  
Debasish Paul ◽  
Alamgir Rahman ◽  
Mohammad Ilias ◽  
M Mozammel Hoq
Keyword(s):  
Serine Protease ◽  
Bacillus Licheniformis ◽  
Half Life ◽  
Maximum Level ◽  
Leather Industry ◽  
Remarkable Effect ◽  
Wide Range ◽  
Commercial Enzymes ◽  
Initial Ph ◽  
Keratinolytic Protease

Keratinolytic protease is an inducible specific proteolytic enzyme, which is produced by Bacillus licheniformis MZK-03 in presence of keratin (feather mill) as sole carbon and nitrogen source in growth medium. Maximum level of keratinolytic protease was produced after 42 h at 37°C over a wide range of initial pH (5.0 to 12.0) under continuous agitation (200 rpm). Keratinolytic protease worked best at 37°C and at pH 8.5. The enzyme was quite stable over a wide range of pH (7.0 to 11.0) but activity dropped drastically beyond this level (enzyme activity dropped to 8.8% and 19.3% at pH 6.5 and 12.0, respectively). Half-life of keratinolytic protease at 70° and 60°C were found to be 3 and 7 min respectively. The enzyme showed highest stability at 40°C (>90% after 3 h). The half-life at 4°C was 34 days. The presence of metal ions (5 mM) like Mg2+, Mn2+, Ca2+ and K+ had no remarkable effect on the keratinolytic protease activity but the activity decreased in presence of Hg2+ and Cu2+. The enzyme may belong to serine protease group as it is inhibited by serine protease inhibitor phenyl methyl sulphonyl fluoride (PMSF). The enzyme is as compatible as other commercially available enzymes used in leather industry with tannery chemicals. It was completely incompatible with Na2S and CaO for their high alkalinity (pH >13.0), which was also observed for other commercial enzymes except the commercial enzyme supplemented with ammonium sulphate. Keywords: Bacillus licheniformis MZK-03, Keratinolytic protease, Keratin, Production, CharacterizationDOI: http://dx.doi.org/10.3329/bjm.v24i1.1239 Bangladesh J Microbiol, Volume 24, Number 1, June 2007, pp 57-61

scholarly journals Functional characterization of a subtilisin-like serine protease from Vibrio cholerae

2019 ◽  
Vol 294 (25) ◽  
pp. 9888-9900
Author(s):  
Matthew Howell ◽  
Daniel G. Dumitrescu ◽  
Lauren R. Blankenship ◽  
Darby Herkert ◽  
Stavroula K. Hatzios
Keyword(s):  
Vibrio Cholerae ◽  
Serine Protease ◽  
Diarrheal Disease ◽  
Functional Characterization ◽  
Large Family ◽  
Protein Domain ◽  
Carbohydrate Binding ◽  
Serine Hydrolase ◽  
Reporter Protein

Vibrio cholerae, the causative agent of the human diarrheal disease cholera, exports numerous enzymes that facilitate its adaptation to both intestinal and aquatic niches. These secreted enzymes can mediate nutrient acquisition, biofilm assembly, and V. cholerae interactions with its host. We recently identified a V. cholerae-secreted serine protease, IvaP, that is active in V. cholerae-infected rabbits and human choleric stool. IvaP alters the activity of several host and pathogen enzymes in the gut and, along with other secreted V. cholerae proteases, decreases binding of intelectin, an intestinal carbohydrate-binding protein, to V. cholerae in vivo. IvaP bears homology to subtilisin-like enzymes, a large family of serine proteases primarily comprised of secreted endopeptidases. Following secretion, IvaP is cleaved at least three times to yield a truncated enzyme with serine hydrolase activity, yet little is known about the mechanism of extracellular maturation. Here, we show that IvaP maturation requires a series of sequential N- and C-terminal cleavage events congruent with the enzyme's mosaic protein domain structure. Using a catalytically inactive reporter protein, we determined that IvaP can be partially processed in trans, but intramolecular proteolysis is most likely required to generate the mature enzyme. Unlike many other subtilisin-like enzymes, the IvaP cleavage pattern is consistent with stepwise processing of the N-terminal propeptide, which could temporarily inhibit, and be cleaved by, the purified enzyme. Furthermore, IvaP was able to cleave purified intelectin, which inhibited intelectin binding to V. cholerae. These results suggest that IvaP plays a role in modulating intelectin–V. cholerae interactions.

scholarly journals Draft Genome Sequence of Bacillus megaterium BHG1.1, a Strain Isolated from Bar-Headed Goose ( Anser indicus ) Feces on the Qinghai-Tibet Plateau

2016 ◽  
Vol 4 (3) ◽  
Author(s):  
Wen Wang ◽  
Si-Si Zheng ◽  
Hao Sun ◽  
Jian Cao ◽  
Fang Yang ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Bacillus Megaterium ◽  
Protein Production ◽  
Draft Genome ◽  
Industrial Applications ◽  
Draft Genome Sequence ◽  
Tibet Plateau ◽  
Positive Bacterium ◽  
Anser Indicus ◽  
Qinghai Tibet Plateau

Bacillus megaterium is a soil-inhabiting Gram-positive bacterium that is routinely used in industrial applications for recombinant protein production and bioremediation. Studies involving Bacillus megaterium isolated from waterfowl are scarce. Here, we report a 6.26-Mbp draft genome sequence of Bacillus megaterium BHG1.1, which was isolated from feces of a bar-headed goose.

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.

Oxidative polymerization of waste cooking oil with air under hydrodynamic cavitation

2017 ◽  
Vol 6 (4) ◽  
Author(s):  
Laura Rinaldi ◽  
Zhilin Wu ◽  
Samuele Giovando ◽  
Marco Bracco ◽  
Daniele Crudo ◽  
...  
Keyword(s):  
Animal Feed ◽  
Oxidative Polymerization ◽  
Cost Effective ◽  
Waste Cooking Oil ◽  
Industrial Applications ◽  
Hydrodynamic Cavitation ◽  
Leather Industry ◽  
Cooking Oil ◽  
Used Cooking Oil ◽  
Fold Reduction

AbstractApart from being a component of some animal feed products, the main industrial use of recycled waste frying oils is biodiesel preparation. With the aim of finding a suitable technology for a cost-effective valorization of used cooking oil, we investigated some oxidative treatments under hydrodynamic cavitation with air flow. This process enabled the preparation of a useful precursor of fatliquor used in the leather industry through the efficient oxidation/polymerization of waste oils at 90°C. The same technique enabled a stable dispersion/emulsification in water without surfactants. Thanks to the use of these innovative techniques, a four-fold reduction of the oxidation time of waste oil was achieved. All the results indicate that the use of a highly efficient rotor-stator generator of hydrodynamic cavitation is compatible with a process scaling up for potential industrial applications.

BACTERIOLOGICAL STUDIES ON THE RED DISCOLORATION OF SALTED HIDES

1934 ◽  
Vol 10 (3) ◽  
pp. 275-286 ◽  
Author(s):  
A. G. Lochhead
Keyword(s):  
New Species ◽  
Salt Concentration ◽  
Halophilic Bacteria ◽  
The Other ◽  
Leather Industry ◽  
Eastern Canada ◽  
Proteolytic Action ◽  
A New Species

A study was made of organisms concerned with the red discoloration of salted hides, also termed "red heat", which defect may occasion loss in the leather industry through spotting and weakening of the fibre. Red halophilic sarcinae were isolated from Argentine hide. From Canadian hides showing red discoloration, two species of pleomorphic rods were isolated as active agents. One of these, occurring on salted cowhides, was found to be similar to Serratia salinaria (Harrison and Kennedy) Bergey et al., a source of reddening of cured codfish in eastern Canada. The other organism causing discoloration, isolated from buffalo hide, was regarded as a new species and designated Serratia cutirubra n.sp. Both of these halophilic organisms, owing to their proteolytic action, are considered capable of greater damage to hides than the red sarcinal types which are non-liquefying, and which may also be present on Canadian hides. Non-chromogenic halophilic bacteria were also isolated from discolored hides. These develop at a lower salt concentration range than the red organisms and are probably less active in causing injury to fibre in well salted hides.

scholarly journals Use of SPR Biosensor for the Study of Proteolytic Action of a Serine Protease Enzyme

2011 ◽  
pp. 253-257 ◽  
Author(s):  
Muhammad Ali Syed ◽  
Arshad Saleem Bhatti ◽  
Chenzhong Li ◽  
Habib Bokhari
Keyword(s):  
Serine Protease ◽  
Spr Biosensor ◽  
Protease Enzyme ◽  
Proteolytic Action

scholarly journals Biocomposites based on collagen and keratin with properties for agriculture and industrie applications

2019 ◽  
Vol 3 (3) ◽  
pp. 160-166 ◽  
Author(s):  
Mihaela-Doina Niculescu ◽  
Doru-Gabriel Epure ◽  
Magdalena Lasoń-Rydel ◽  
Carmen Gaidau ◽  
Mihai Gidea ◽  
...  
Keyword(s):  
Controlled Release ◽  
Plant Biomass ◽  
Water Vapor Permeability ◽  
Industrial Applications ◽  
Vapor Permeability ◽  
Mechanical Resistance ◽  
Leather Industry ◽  
Agricultural Applications ◽  
Vegetable Tanning ◽  
By Products

Abstract In the present research biocomposites based on extracts of collagen and keratin recovered from the leather industry by-products were made and the specific properties for applications in agriculture and industry were studied. To this aim, collagen and keratin have been extracted from bovine leather and sheep wool by-products and have been added and crosslinked with recognized compounds for reduced environmental impact (glycerol, vegetable tanning extract, essential oils with fungicidal properties and insecticides). The biocomposite properties were evaluated on the basis of complex analytical investigations on chemical structure, texture, contact angle, mechanical resistance, water vapor permeability and water absorption, biodegradation, germination and plant biomass growth. The biocomposites have demonstrated pelliculogenic properties and nitrogen controlled release to stimulate germination and nutrition of rape seedlings, which promotes them for agricultural applications, but also other surface properties have been identified, for industrial applications, for example in leather finishing for special destinations. Addition of odorous principles with controlled release recommends this type of biocomposites for environmentally friendly products, maintenance of cleaning, etc.

scholarly journals In silico analysis to elect superior bacterial alkaline protease for detergent and leather industries

2015 ◽  
Vol 5 (3) ◽  
pp. 685-698 ◽  
Author(s):  
Kamonashis Das ◽  
Sourav Chakraborty ◽  
Mahmudul Hasan ◽  
Abdullah Maruf Rahman Shovo
Keyword(s):  
High Temperature ◽  
Bacillus Megaterium ◽  
In Silico ◽  
Alkaline Protease ◽  
Protein Sequences ◽  
In Silico Analysis ◽  
Alkaline Proteases ◽  
Leather Industry ◽  
Catalytic Function ◽  
Common Motif

Alkaline protease contributes 40% of the total worldwide enzyme sales. Alkaline protease that is stable at very high temperature and pH is massively desirable for detergent industry and leather industry specially in tanning process. So the present study aims to elect superior bacterial alkaline protease (high temperature and pH stable) as compared to the alkaline proteases of currently industrially used bacteria (Bacillus subtilis and Bacillus cereus). A total of 50 protein sequences of alkaline proteases of different bacteria were analyzed through in silico characterization. ProtParam result revealed that isoelectric point and aliphatic index of alkaline protease of Bacillus megaterium were 8.83 and 93.35 respectively. In case of alkaline protease of B. megaterium, these two properties were significant in comparison to alkaline proteases of industrially used bacteria and other considered bacteria. A common motif of 28 amino acid residues i.e., IQSTYPGEDYEYMSGTSMATPHVAGVAA was found using MEME software in 46 protein sequences. It can be concluded that alkaline protease of Bacillus megaterium may be superior to alkaline proteases of industrially used bacteria and other considered bacteria. In addition, obtained common motif indicates its probable role in catalytic function and structure of alkaline proteases. 

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