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Journal ArticleDOI

Effect of Cultural Conditions on Protease Production by a Thermophilic Geobacillus thermoglucosidasius SKF4 Isolated from Sungai Klah Hot Spring Park, Malaysia.

04 Jun 2020-Molecules (Multidisciplinary Digital Publishing Institute)-Vol. 25, Iss: 11, pp 2609
TL;DR: A new potent strain of thermophilic bacterium isolated from Sungai Klah Hot Spring Park in Perak, Malaysia for the first time is revealed and the high production of thermostable protease enzyme by G. thermoglucosidasius SKF4 highlighted the promising properties of this bacterium for industrial and biotechnological applications.
Abstract: Major progress in the fields of agriculture, industry, and biotechnology over the years has influenced the quest for a potent microorganism with favorable properties to be used in scientific research and industry. This study intended to isolate a new thermophilic-protease-producing bacterium and evaluate its growth and protease production under cultural conditions. Protease producing bacteria were successfully isolated from Sungai Klah Hot Spring Park in Perak, Malaysia, and coded as SKF4; they were promising protease producers. Based on microscopic, morphological, and 16S rRNA gene analysis, isolate SKF4 was identified as Geobacillus thermoglucosidasius SKF4. The process of isolating SKF4 to grow and produce proteases under different cultural conditions, including temperature, pH, NaCl concentration, carbon and nitrogen sources, and incubation time, was explored. The optimum cultural conditions observed for growth and protease production were at 60 to 65 °C of temperature, pH 7 to 8, and under 1% NaCl concentration. Further, the use of casein and yeast extract as the nitrogen sources, and sucrose and fructose as the carbon sources enhanced the growth and protease production of isolate SKF4. Meanwhile, isolate SKF4 reached maximum growth and protease production at 24 h of incubation time. The results of this study revealed a new potent strain of thermophilic bacterium isolated from Sungai Klah Hot Spring Park in Perak, Malaysia for the first time. The high production of thermostable protease enzyme by G. thermoglucosidasius SKF4 highlighted the promising properties of this bacterium for industrial and biotechnological applications.
Citations
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Journal ArticleDOI
08 Sep 2021
TL;DR: Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics.
Abstract: Proteases are ubiquitous enzymes, having significant physiological roles in both synthesis and degradation. The use of microbial proteases in food fermentation is an age-old process, which is today being successfully employed in other industries with the advent of 'omics' era and innovations in genetic and protein engineering approaches. Proteases have found application in industries besides food, like leather, textiles, detergent, waste management, agriculture, animal husbandry, cosmetics, and pharmaceutics. With the rising demands and applications, researchers are exploring various approaches to discover, redesign, or artificially synthesize enzymes with better applicability in the industrial processes. These enzymes offer a sustainable and environmentally safer option, besides possessing economic and commercial value. Various bacterial and fungal proteases are already holding a commercially pivotal role in the industry. The current review summarizes the characteristics and types of proteases, microbial source, their current and prospective applications in various industries, and future challenges. Promoting these biocatalysts will prove significant in betterment of the modern world.

23 citations

Journal ArticleDOI
TL;DR: In this article, a pectinolytic enzyme producing Bacillus subtilis strain BK-3 was isolated from Bakreshwer hot spring, which contains citrus peel waste as a substrate.
Abstract: Clarification of fruit juice is a pivotal step in the juice and beverages industries which enhance appearance and marketability. In the present study, a pectinolytic enzyme producing Bacillus subtilis strain BK-3 was isolated from Bakreshwer hot spring. The pectinase production was increased in a liquid medium, which contains citrus peel waste as a substrate. Pectinase production was 2.47 fold enhanced than initial production after the response surface methodology (RSM) approach. SDS PAGE result shown that the molecular weight of pectinase was ~33 kDa. The pH and temperature optima were 5.0 and 50 °C, respectively, and pectinase presented stability at a broader pH (4-10) and temperature range (30–60 °C). The metal ions KCl and MnCl2 significantly affected enzyme activity in a positive direction, whereas the solvent inhibited the biocatalytic performance. The Km and Vmax of pectinase were 0.4770 mg mL-1 and 43.46 IU mL-1, respectively. After the pectinase treatment in various fruit juice (black mulberry, apple, orange, and pineapple), clarity and reducing sugar were increased, and turbidity was decreased. All this characteristic of pectinase exhibit a good prospect for bio-industrial exploration.

19 citations

Journal ArticleDOI
TL;DR: The first revelation of thermophilic nitroalkane-degrading mechanism under both aerobic and anaerobic conditions provides guidance and platform for biotechnological and industrial applications.

14 citations

Journal ArticleDOI
TL;DR: This review covers the prospective applications of extremozymes in the food industry in a broader sense, including degradation of toxins, deconstruction of polymers into monomers, and catalysis of multistep processes.
Abstract: Microorganisms from extreme environments tend to undergo various adaptations due to environmental conditions such as extreme pH, temperature, salinity, heavy metals, and solvents. Thus, they produce enzymes with unique properties and high specificity, making them useful industrially, particularly in the food industries. Despite these enzymes' remarkable properties, only a few instances can be reported for actual exploitation in the food industry. This review's objectives are to highlight the properties of these enzymes and their prospects in the food industry. First, an introduction to extremophilic organisms is presented, followed by the categories and application of food enzymes from extremophiles. Then, the unique structural features of extremozymes are shown. This review also covers the prospective applications of extremozymes in the food industry in a broader sense, including degradation of toxins, deconstruction of polymers into monomers, and catalysis of multistep processes. Finally, the challenges in bioprocessing of extremozymes and applications in food are presented. PRACTICAL APPLICATIONS: Enzymes are important players in food processing and preservation. Extremozymes, by their nature, are ideal for a broad range of food processing applications, particularly those that require process conditions of extreme pH, temperature, and salinity. As the global food industry grows, so too will grow the need to research and develop food products that are diverse, safe, healthy, and nutritious. There is also the need to produce food in a sustainable way that generates less waste or maximizes waste valorization. We anticipate that extremozymes can meet some of the research and development needs of the food industry.

10 citations

Journal ArticleDOI
TL;DR: In this paper, a serine protease of thermophilic Geobacillus sp. GS53 from Balcova geothermal region, Izmir, Turkey, was performed.
Abstract: Proteases account for approximately 60% of the enzyme market in the world, and they are used in various industrial applications including the detergent industry. In this study, production and characterization of a novel serine protease of thermophilic Geobacillus sp. GS53 from Balcova geothermal region, Izmir, Turkey, were performed. The thermostable protease was purified through ammonium sulfate precipitation and anion-exchange chromatography. The results showed that the protease had 137.8 U mg-1 of specific activity and optimally worked at 55 oC and pH 8. It was also active in a broad pH (4-10) and temperature (25-75 °C) ranges. The protease was highly stable at 85 °C and demonstrated relative stability at pH 4, 7, and 10. Also, the enzyme had high stability against organic solvents and surfactants; enzyme relative activity did not decrease below 81% upon preincubation for 10 min. Ca2+, Cu2+, and Zn2+ ions slightly induced protease activity. The protease was highly specific to casein, skim milk, Hammerstein casein, and BSA substrates. These results revealed that the protease might have a potential effect in a variety of industrial fields, especially the detergent industry, because of its high thermostability and stability to surfactants.

4 citations

References
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Journal ArticleDOI
TL;DR: Jalview 2 is a system for interactive WYSIWYG editing, analysis and annotation of multiple sequence alignments that employs web services for sequence alignment, secondary structure prediction and the retrieval of alignments, sequences, annotation and structures from public databases and any DAS 1.53 compliant sequence or annotation server.
Abstract: Summary: Jalview Version 2 is a system for interactive WYSIWYG editing, analysis and annotation of multiple sequence alignments. Core features include keyboard and mouse-based editing, multiple views and alignment overviews, and linked structure display with Jmol. Jalview 2 is available in two forms: a lightweight Java applet for use in web applications, and a powerful desktop application that employs web services for sequence alignment, secondary structure prediction and the retrieval of alignments, sequences, annotation and structures from public databases and any DAS 1.53 compliant sequence or annotation server. Availability: The Jalview 2 Desktop application and JalviewLite applet are made freely available under the GPL, and can be downloaded from www.jalview.org Contact: g.j.barton@dundee.ac.uk

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"Effect of Cultural Conditions on Pr..." refers methods in this paper

  • ...Evolutionary distances of nucleotide sequences were computed using the Jukes–Cantor model (bootstrap values: 1000 resampling) [27]....

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Journal ArticleDOI
TL;DR: Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes and deciphering these secrets would enable to exploit proteases for their applications in biotechnology.
Abstract: Proteases represent the class of enzymes which occupy a pivotal position with respect to their physiological roles as well as their commercial applications. They perform both degradative and synthetic functions. Since they are physiologically necessary for living organisms, proteases occur ubiquitously in a wide diversity of sources such as plants, animals, and microorganisms. Microbes are an attractive source of proteases owing to the limited space required for their cultivation and their ready susceptibility to genetic manipulation. Proteases are divided into exo- and endopeptidases based on their action at or away from the termini, respectively. They are also classified as serine proteases, aspartic proteases, cysteine proteases, and metalloproteases depending on the nature of the functional group at the active site. Proteases play a critical role in many physiological and pathophysiological processes. Based on their classification, four different types of catalytic mechanisms are operative. Proteases find extensive applications in the food and dairy industries. Alkaline proteases hold a great potential for application in the detergent and leather industries due to the increasing trend to develop environmentally friendly technologies. There is a renaissance of interest in using proteolytic enzymes as targets for developing therapeutic agents. Protease genes from several bacteria, fungi, and viruses have been cloned and sequenced with the prime aims of (i) overproduction of the enzyme by gene amplification, (ii) delineation of the role of the enzyme in pathogenecity, and (iii) alteration in enzyme properties to suit its commercial application. Protein engineering techniques have been exploited to obtain proteases which show unique specificity and/or enhanced stability at high temperature or pH or in the presence of detergents and to understand the structure-function relationships of the enzyme. Protein sequences of acidic, alkaline, and neutral proteases from diverse origins have been analyzed with the aim of studying their evolutionary relationships. Despite the extensive research on several aspects of proteases, there is a paucity of knowledge about the roles that govern the diverse specificity of these enzymes. Deciphering these secrets would enable us to exploit proteases for their applications in biotechnology.

2,159 citations


"Effect of Cultural Conditions on Pr..." refers background in this paper

  • ...[3] described the protease enzyme as a hydrolytic enzyme that increases the rate of the splitting of peptides links in other proteins....

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Journal ArticleDOI
TL;DR: Developments from the understanding of the complex protein translocation machinery of Gram-positive bacteria should allow the resolution of current secretion challenges and make Bacillus species preeminent hosts for heterologous protein production.
Abstract: Bacillus species continue to be dominant bacterial workhorses in microbial fermentations. Bacillus subtilis (natto) is the key microbial participant in the ongoing production of the soya-based trad...

1,100 citations

Book
31 Jul 1994
TL;DR: Bioreactor Modelling: Morph Structured Models for Population Balances Based on Cell Number and Mass Transfer and Cellular Growth Reactions.
Abstract: Introduction. Cellular Growth Reactions. Analysis of Reaction Rates. Modelling of Reaction Kinetics. Morphologically Structured Models. Population Balances Based on Cell Number. Mass Transfer. Ideal Bioreactors. Bioreactor Modelling. Index.

775 citations


"Effect of Cultural Conditions on Pr..." refers result in this paper

  • ...Moreover, reports by Nielsen and Villadsen, [39] and Bhunia et al. [38] stated that temperature affects the specific growth rate of bacteria; there was a gradual increase in specific growth rate until the optimum temperature and then a rapid decrease beyond the optimum temperature....

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  • ...Moreover, reports by Nielsen and Villadsen, [39] and Bhunia et al....

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  • ...Moreover, reports by Nielsen and Villadsen, [39] and Bhunia et al. [38] stated that temperature affects the specific growth rate of bacteria; there was a gradual increase in specific growth rate until the optimum temperature and then a rapid decrease beyond the optimum temperature....

    [...]

Journal ArticleDOI
TL;DR: Comparative analysis of the 16S rDNA sequences and fatty acid compositions of the novel isolates and established species of thermophilic bacilli indicated that the subsurface strains represent two new species within a new genus, for which the names Geobacillus subterraneus gen. nov., sp.nov.
Abstract: Five hydrocarbon-oxidizing strains were isolated from formation waters of oilfields in Russia, Kazakhstan and China. These strains were moderately thermophilic, neutrophilic, motile, spore-forming rods, aerobic or facultatively anaerobic. The G+C content of their DNA ranged from 49.7 to 52.3 mol%. The major isoprenoid quinone was menaquinone-7; cellular fatty acid profiles consisted of significant amounts of iso-15:0, iso-16:0 and iso-17:0 fatty acids (61.7-86.8% of the total). Based on data from 16S rDNA analysis and DNA-DNA hybridization, the subsurface isolates could be divided into two groups, one of which consisted of strains UT and X and the other of which consisted of strains K, Sam and 34T. The new strains exhibited a close phylogenetic relationship to thermophilic bacilli of 'Group 5' of Ash et al. [Ash, C., Farrow, J. A. E., Wallbanks, S. & Collins, M. D. (1991). Lett Appl Microbiol 13, 202-206] and a set of corresponding signature positions of 16S rRNA. Comparative analysis of the 16S rDNA sequences and fatty acid compositions of the novel isolates and established species of thermophilic bacilli indicated that the subsurface strains represent two new species within a new genus, for which the names Geobacillus subterraneus gen. nov., sp. nov., and Geobacillus uzenensis sp. nov. are proposed. It is also proposed that Bacillus stearothermophilus, Bacillus thermoleovorans, Bacillus thermocatenulatus, Bacillus kaustophilus, Bacillus thermoglucosidasius and Bacillus thermodenitrificans be transferred to this new genus, with Geobacillus stearothermophilus (formerly Bacillus stearothermophilus) as the type species.

713 citations


"Effect of Cultural Conditions on Pr..." refers background in this paper

  • ...[8], which stated that there is more than 96% sequence homology among the members of Geobacillus species....

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  • ...They have a broad distribution and are less difficult to be isolated from the diverse natural environment [8,9]....

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  • ...Geobacillus species have been isolated from several environments, such as high-temperature oil fields, a corroded pipeline in a very deep well [13], an African hot spring [8], a Russian hot spring, and a marine vent [14]....

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  • ...[8] arranged thermophilic bacteria bacilli that are Gram-positive with rod shape cells and formed endospores to be known as genus Geobacillus....

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