Allison D Suleiman
Other affiliations: Adama University
Bio: Allison D Suleiman is an academic researcher from Universiti Putra Malaysia. The author has contributed to research in topics: Protease & Geobacillus thermoglucosidasius. The author has an hindex of 1, co-authored 1 publications receiving 9 citations. Previous affiliations of Allison D Suleiman include Adama University.
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.
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.
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.
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.
Abstract: In this study, a thermophilic facultative anaerobic strain Geobacillus thermoglucosidasius W-2 was found to degrade nitroalkane under both aerobic and anaerobic conditions. Bioinformatical analysis revealed three putative nitroalkane-oxidizing enzymes (Gt-NOEs) genes from the W-2 genome. The three identified proteins Gt2929, Gt1378, and Gt1208 displayed optimal activities at high temperatures (70, 70, and 80 °C, respectively). Among these, Gt2929 exhibited excellent degradation capability, pH stability, and metal ion tolerance for nitronates under aerobic condition. Interestingly, under anaerobic condition, only Gt1378 still maintained high activity for 2-nitropropane and nitroethane, indicating that the W-2 strain utilized various pathways to degrade nitronates under aerobic and anaerobic conditions, respectively. Taken together, the first revelation of thermophilic nitroalkane-degrading mechanism under both aerobic and anaerobic conditions provides guidance and platform for biotechnological and industrial applications.
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.
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.