Isolation and characterization of a cold-active amylase from marine Wangia sp. C52

Liu, Jianguo; Zhang, Zhi‐Qiang; Dang, Hongyue; Lu, Jiakai; Cui, Zhanfeng

doi:10.5897/ajmr10.743

Cited by 12 publications

(5 citation statements)

References 16 publications

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“…Based on this, the enzyme was also found to be mesophilic and thermophilic, along with being a psychrophilic enzyme. Related results were reported by Liu et al [37] in their study on cold-active amylase of Wangia sp. C52, which showed the enzyme activity and stability at cold temperature, i.e., 10 °C.…”

Section: Effect Of Temperature On the α-Amylase Activitysupporting

confidence: 80%

“…The enzyme purification results were summarized in Table 2. The established molecular weight of α-amylase calculated by Kav (a gel-phase distribution coefficient) versus the log of BSA, ovalbumin, carbonic anhydrase and cytochrome C was found to be 45 kDa [37,38]. After subjected to four purification steps, 6.87 purification fold was achieved with a 7.47% yield and specific activity of 36,690.47 U/ mg protein of purified α-amylase.…”

Section: Purification Of α-Amylasementioning

confidence: 99%

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Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2

Rathour

Gupta

Tyagi

et al. 2020

Amylase

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A psychrophilic and halophilic bacterial isolate, Shewanella sp. ISTPL2, procured from the pristine Pangong Lake, Ladakh, Jammu and Kashmir, India, was used for the production and characterization of the psychrophilic and alkalophilic α-amylase enzyme. The α-amylase is a critical enzyme that catalyses the hydrolysis of α-1,4-glycosidic bonds of starch molecules and is predominately utilized in biotechnological applications. The highest enzyme activity of partially purified extracellular α-amylase was 10,064.20 U/mL after 12 h of incubation in a shake flask at pH 6.9 and 10 °C. Moreover, the maximum intracellular α-amylase enzyme activity (259.62 U/mL) was also observed at 6 h of incubation. The extracellular α-amylase was refined to the homogeneity with the specific enzyme activity of 36,690.47 U/mg protein corresponding to 6.87-fold purification. The optimized pH and temperature for the α-amylase were found to be pH 8 and 4 °C, respectively, suggesting its stability at alkaline conditions and low or higher temperatures. The amylase activity was highly activated by Cu2+, Fe2+ and Ca2+, while inhibited by Cd2+, Co2+ and Na2+. As per our knowledge, the current study reports the highest activity of a psychrophilic α-amylase enzyme providing prominent biotechnological potential.

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Section: Effect Of Temperature On the α-Amylase Activitysupporting

confidence: 80%

Section: Purification Of α-Amylasementioning

confidence: 99%

Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2

Rathour

Gupta

Tyagi

et al. 2020

Amylase

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“…[80], Wangia sp. C52 [81], Pontibacillus chungwhensis [82], Bacillus barbaricus [82], Nocardiopsis sp. B2 [83], and Anoxybacillus beppuensis TSSC-1 [84].…”

Section: Discussionmentioning

confidence: 99%

Bioprospecting of Culturable Halophilic Bacteria Isolated from Mediterranean Solar Saltern for Extracellular Halotolerant Enzymes

Ali,

Abdel-Rahman,

Farahat

2024

Microbiol. Biotechnol. Lett.

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Halophilic bacteria are promising reservoirs for halotolerant enzymes that have gained much attention in biotechnological applications due to their remarkable activity and stability. In this study, 62 halophilic bacterial strains isolated from a solar saltern were screened for the production of various extracellular enzymes. The results revealed that 31 strains (50%) were positive for amylase production while 26 strains (41.9%) were positive for protease. Further, 22 strains (35.48%) exhibited β-glucosidase activity and only 17 (27.41%) demonstrated lipase activity. Of the investigated halophiles, ten strains growing in the presence of ≥15% NaCl (w/v) were selected and identified based on their 16S rRNA gene sequences as Halomonas meridiana, Salinivibrio costicola, Virgibacillus oceani, Virgibacillus marismortui, Marinobacter lipolyticus, Halobacillus karajensis, Salicola salis, Pseudoalteromonas shioyasakiensis, Salinicoccus amylolyticus, and Paracoccus salipaludis. Therefore, the present study highlights the diversity of the culturable halophilic bacteria in a Mediterranean solar saltern, harboring various valuable halotolerant enzymes.

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“…Liu et al found the best stimulator as Co 2+ and Ca 2+ and inhibitor as Mn 2+ , Hg 2+ , Cu 2+ , Zn 2+ , Al 3+ and Fe 3+ for cold active amylase activity. 31…”

Section: Effect Of Metal Ions On the Activity Of Alpha Amylasementioning

confidence: 99%

“…reported the optimum enzyme-substrate reaction time at 60 min. According to Alva et al, highest yield was found during the enzyme -substrate reaction time at 5 min 31. …”

mentioning

confidence: 94%

Cold Active Amylase Production from Bacillus cereus RGUJS2023

2023

TJNPR

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IntroductionAmylases are extracellular enzymes (endo-1,4-Dglucanohydrolases, E.C. 3.2.1.1) that hydrolyze starch polymer to glucose. 1 World-wide, amylases account for 30% of the market for industrial enzymes. 2 Amylases has been shown to have a wide range of importance in industry. 3 Cold-active amylases are suitable for a range of industrial processes, including detergents for cold washing, leather softening, bioremediation, biofuel production, textiles, alcohol production, paper industry, the food industry, pharmaceuticals, and molecular biology applications. 4,5 From ancient times to present, amylase has been discovered in animal, plant, and microbial sources; however, microbial sources are more preferred for commercial usage. 6 The primary benefits of using microorganisms in the synthesis of amylase include their ability to perform a variety of modifications to produce enzymes with desired properties quickly. 7 In particular, bacterial amylases from Bacillus spp. are sought-after industrial organisms because of their ability to produce the extracellular enzymes and have rapid growth rates that result in fast fermentation times, which are crucial for the starch processing industries. 8 Bacillus species make up the vast majority of the bacteria that create cold-active amylases. 9 In order to produce cold active amylase for commercial use, Bacillus spp. (Bacillus cereus, Bacillus amyloliquefaciens, Bacillus marisflavi and Bacillus subtilis) 10,11,12 have been widely employed. Several of the species were isolated, characterized, and optimized for amylase synthesis.

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Isolation and characterization of a cold-active amylase from marine Wangia sp. C52

Cited by 12 publications

References 16 publications

Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2

Production and characterization of psychrophilic α-amylase from a psychrophilic bacterium, Shewanella sp. ISTPL2

Bioprospecting of Culturable Halophilic Bacteria Isolated from Mediterranean Solar Saltern for Extracellular Halotolerant Enzymes

Cold Active Amylase Production from Bacillus cereus RGUJS2023

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