Production optimization of ?-amylase from Bacillus licheniformis

Hiteshi, Kalpana; Didwal, Gunjan; Gupta, Reena

doi:10.53555/nnbma.v2i5.497

Cited by 3 publications

(3 citation statements)

References 37 publications

(43 reference statements)

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“…Underexposure to temperatures higher than 65°C, the activity was found to drop up to 20% or less. The optimum temperature of the A7 strain (60°C) is under the range of thermostable enzymes and comparable to the optimum temperature of some thermophilic APB, including B. licheniformis from hot springs of Himachal Pradesh (50°C), and B. megaterium HAT1 (Hiteshi et al 2016;Malle et al 2012). Nevertheless, some thermostable APB were shown to have amylase activity at higher optimum temperatures than the A7 strain, including Bacillus licheniformis from Iran soil (70°C) and B. amyloliquefaciens KCP2 (65°C) (Prajapati et al 2015;Rasooli et al 2008).…”

Section: Resultsmentioning

confidence: 78%

Screening, isolation, and characterization of amylase-producing bacteria from Poring Hot Spring Sabah, Malaysia

et al. 2022

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Abstract. Fazal BZ, Budiman C, Amin Z, Ling CMW. 2022. Screening, isolation, and characterization of amylase-producing bacteria from Poring Hot Spring Sabah, Malaysia. Biodiversitas 23: 2807-2815. Thermostable ?-amylases are being used in a wide range of industries, including food, textiles, detergents, pharmaceuticals, and fine chemicals. A good source of thermostable ?-amylases in thermophilic bacteria is found in high-temperature habitats like hot springs. Hence, this study aimed to screen, isolate, and characterize amylase-producing bacteria (APB) from the Poring hot spring in Sabah. Sediment and water samples were collected from the hot springs, serially diluted, plated onto the Luria Bertani agar medium containing starch, and incubated at 60°C for 48 hours. The amylase-producing bacterium was identified by the halo formation around the colony after the agar medium was stained with Lugol's solution. Nine colonies were found to be able to form halo zones, with a creamy colony (A7 strain) producing the highest amylolytic index (4.24). Further characterization of the A7 strain showed that the isolate was a Gram-positive, rod-shaped bacterium, with a positive reaction upon oxidase and catalase tests. The 16S rRNA sequence showed that the A7 strain had 99.81% similarity with the Anoxybacillus flavithermus, and therefore identified as A. flavithermus A7 strain. Further, the growth curve analysis indicated that the A7 strain grew well at 60°C. The 3, 5-dinitrosalicyclic acid (DNS) assay showed the crude enzyme secreted by the A7 strain exhibited optimum amylase activity at 60°C with 8.6 x 10-2 U/ml. This is the first APB obtained from hot springs in Sabah and promising for further studies and applications.

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Section: Resultsmentioning

confidence: 78%

Screening, isolation, and characterization of amylase-producing bacteria from Poring Hot Spring Sabah, Malaysia

et al. 2022

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“…Various studies have explored the optimum culture conditions for amylase synthesis. For instance, Hiteshi et al (2018) noted that Bacillus licheniformis achieved maximal amylase production at a temperature of 50°C, a pH of 8.0, and an incubation period of 48h.…”

Section: Discussionmentioning

confidence: 99%

Thermostable Amylase from Cytobacillus firmus: Characterization, Optimization, and Implications in Starch Hydrolysis

Al-Harthy,

Hozzein,

Abdelkader

et al. 2024

Egypt. J. Microbiol.

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H OT springs are known to be rich in diverse microorganisms, including thermophilic bacteria capable of producing industrially important enzymes. This study aimed to isolate, purify, and identify thermophilic bacteria from three hot springs located in the southern region of Saudi Arabia, namely Al-Ma'a Al-Har, Al-Aredhah, and Al-Ahsarai hot spring. The isolated bacterial isolates were screened for amylase enzyme production, and the most potent isolate, Cytobacillus firmus OQ834432 isolate OHA8, was selected for large-scale production of the amylase enzyme. The enzyme was then purified using salt precipitation, Sephacryl S-200 chromatography, and DEAE-Sepharose column chromatography. A total of twenty-one bacterial species were identified, with Cytobacillus firmus exhibiting the highest amylase activity. The optimal conditions for the amylase enzyme activity were found to be at 50°C and pH 5.0, with a 153% enhancement in activity in the presence of magnesium ions. The enzyme's activity was inhibited by EDTA and was found to be active with starch and amylopectin at 100% and 110.3%, respectively. In conclusion, this study demonstrates the potential of thermophilic bacteria from hot springs to produce industrially important enzymes and provides insights into the optimal conditions for enzyme production and activity. These findings have significant implications for the development of biotechnological applications utilizing thermophilic bacteria in various industrial sectors.

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“…Bacterial sources for the production of amylases are more preferred than any other sources because of their plasticity and vast availability and ability to produce in bulk and ease with which they can be manipulated for desired products (Arora et al, 2020). These contribute a major class of industrial enzymes constituting 25% of the enzyme market (Hiteshi et al, 2016). The global market for industrial enzymes estimated at $2 billion in 2004 and expected to rise at an average annual growth rate of 3.3% (Periasamy Anbu and Lakshmipriya, 2017, He et al, 2023).…”

Section: Introductionmentioning

confidence: 99%

Improvement of Alpha-amylase Activity from Bacillus Licheniformis using UV Radiation and Modified Media Composition

Khatun,

Zarin,

Tasnim

et al. 2023

Bioresearch Communications

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Alpha-amylases are glycosidic bond hydrolyzing enzymes produced in many microorganisms. In the modern era, the spectrum of amylase applications has expanded into various industries, including medical fields. Among other approaches, strain improvement by mutation and culture optimization are attractive methods for increasing the productivity of alpha-amylase in bacterial strains. The present study aimed at enhancing the yield of the enzyme alpha-amylase from the host strain Bacillus licheniformis. The UV irradiation has been used to induce mutations in the bacterial strain with different time durations. Afterwards, the mutant strains were cultured in different modified growth media for enzyme production. Among the four time periods,the highest enzyme activity (705.23 U/ml) was observed after 24 hours which is more than two-fold higher compared to the enzyme activity of the host stain (345.31 U/ml). In addition, enzyme yield varied significantly in modified culture media (i.e, MP1 and MP2, MP3 and MP4) with different carbon and nitrogen compositions. The mutant strain cultured in MP3 medium had the highest amylase activity which was 1461.2 U/ml at 24 hours. More interestingly, this medium also had the highest enzyme activity (1080.5 U/ml) at 48 hours. The trend of enzyme activity showed a decreasing tendency when the strains cultured in MP1, MP2, and MP3 media, but exceptionally, a sharp decreasing trend was seen in MP4 media from 622.1 U/ml at 24 hours to 428.4 U/ml at 48 hours. From the findings, it can be concluded that B. licheniformis is a good candidate to employ for alpha-amylase production in a modified MP3 culture condition for a short time. However, other limiting factors need to be considered for increasing the yield. Bioresearch Commu. 9(2): 1351-1356, 2023 (July)

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Production optimization of ?-amylase from Bacillus licheniformis

Cited by 3 publications

References 37 publications

Screening, isolation, and characterization of amylase-producing bacteria from Poring Hot Spring Sabah, Malaysia

Screening, isolation, and characterization of amylase-producing bacteria from Poring Hot Spring Sabah, Malaysia

Thermostable Amylase from Cytobacillus firmus: Characterization, Optimization, and Implications in Starch Hydrolysis

Improvement of Alpha-amylase Activity from Bacillus Licheniformis using UV Radiation and Modified Media Composition

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