Cloning, expression and characterization of highly thermo- and pH-stable maltogenic amylase from a thermophilic bacterium Geobacillus caldoxylosilyticus TK4

Kolcuoğlu, Yakup; Çolak, Ahmėt; Faiz, Özlem; Beldüz, Ali Osman

doi:10.1016/j.procbio.2010.02.001

Cited by 35 publications

(15 citation statements)

References 29 publications

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“…The reduction percentage in enzyme activity was 7% at 90 °C, 8.4% at 80 °C and 8.7 at 65 °C after 8 h. Then, enzyme activity decreased to 5.02, 5.02 and 5.11 gm glucose/ml at 90, 80 and 60 °C respectively after 24 h. (Figure 4). Kolcuoğlu et al (2010) reported that incubation at 80°C resulted about 80% enzyme activity after 72 h. For α-amylase of Bacillus sp., the activity was completely stable at 80°C for at least 90 minutes (Ben Ali et al, 1999). This obtained result proof that gene transferred into BL had effective action on increase amylase activity.…”

Section: Thermal Stability For Enzymementioning

confidence: 99%

Evaluation of Amylase Activity Produced by Genetically Modified Bacillus Grown on Different Media Containing Sugar Crops Wastes

Khaled

Kash

El-Aziz

et al. 2017

Journal of Agricultural Chemistry and Biotechnology

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In this investigation, α-amylase gene region from a thermophilic Bacillus stearothermophilus isolated from sugar beet juice obtained from Dakahlia Sugar factory (Egypt) was cloned to competent Bacillus licheniformis ATCC 27811 cells. The original and modified Bacillus strains were spread on different media composition and enzyme activity was determined. According to the results, the α-amylase enzyme was seen to have highest activity at media containing sugarcane bagasse and/or sugar beet pulp. The results revealed that modified Bacillus surpassed the original one at all studied media. This obtained result proofed that gene transferred into BL had effective action on increase α-amylase activity. The thermo-stability studies revealed that enzyme activity of modified bacillus was high for the first 8 hours at 90°C, it was ranged from 95-90 % after 6 hours (enzyme activity decreased from 7.80 to 7.02 gm glucose/ml) then, decreased to 65-63 % at the end of 24 hours.

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Section: Thermal Stability For Enzymementioning

confidence: 99%

Evaluation of Amylase Activity Produced by Genetically Modified Bacillus Grown on Different Media Containing Sugar Crops Wastes

Khaled

Kash

El-Aziz

et al. 2017

Journal of Agricultural Chemistry and Biotechnology

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“…The recombinant expression resulted in high levels of extracellular amylase production, as high as 22 mg/L in the shake flask culture supernatant (Karakas et al, 2010 ). A gene corresponding to thermo- and pH-stable maltogenic α-amylase of G. caldoxylosilyticus TK4 has been cloned into pET28a (+) vector and expressed in E. coli with 6xHis-tag at the N-terminus (Kolcuoglu et al, 2010 ). A gene encoding a hyperthermostable maltogenic α-amylase of Staphylothermus marinus (SMMA) was cloned and over expressed in E .…”

Section: Gene Cloning and Over Expression Of Recombinant α-Amylasesmentioning

confidence: 99%

Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications

2016

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Industrial enzyme market has been projected to reach US$ 6.2 billion by 2020. Major reasons for continuous rise in the global sales of microbial enzymes are because of increase in the demand for consumer goods and biofuels. Among major industrial enzymes that find applications in baking, alcohol, detergent, and textile industries are α-amylases. These are produced by a variety of microbes, which randomly cleave α-1,4-glycosidic linkages in starch leading to the formation of limit dextrins. α-Amylases from different microbial sources vary in their properties, thus, suit specific applications. This review focuses on the native and recombinant α-amylases from bacteria and archaea, their production and the advancements in the molecular biology, protein engineering and structural studies, which aid in ameliorating their properties to suit the targeted industrial applications.

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“…. The percentages of remaining activities were expressed by comparison with the standard assay mixture with no metal ion added [16,17].…”

Section: Effect Of Various Inhibitors On Ppo Activitymentioning

confidence: 99%

Characterization of polyphenol oxidase during three ripening stages of an eggplant (Solanum melongena L.) fruit: a local type in northeast Anatolia

et al. 2015

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Characterization of polyphenol oxidase during three ripening stages of an eggplant (Solanum melongena L.) fruit: a local type in northeast Anatolia[Patlıcan (Solanum melongena L.) meyvesinin polifenol oksidazının üç olgunlaşma safhası boyunca karakterizasyonu: Doğu Anadolu' da yerel bir tip] ABSTRACT Objective: A relatively new local type of eggplant, Solanum melongena L. 'Kadife' is widely consumed in Turkey because of its economic availability and good nutritional qualities. However, the high polyphenol content of eggplant renders it susceptible to unattractive oxidative browning catalyzed by polyphenol oxides (PPOs). Therefore, the main aim of this study was to characterize PPO in this eggplant cultivar at three stages of its development. Methods: In this study, we determined substrate specificity, optimum pH and temperature, and optimum substrate concentration of the partial purified eggplant fruits PPO during ripening. Results: L-DOPA was proved to be the preferred PPO substrate in all three stages of ripening. Optimum activity was observed at pH 7.0 for PPO in extracts of ripening and overly-ripe eggplant, while activity in extracts of immature eggplant exhibited a broad pH optimum between, pH 5.0 and 7.0. In general, at all ripening stages, PPO was most active at 30°C and was most sensitive to inhibition by sodium metabisulphite and ascorbic acid. The metal ions (Hg ÖZETAmaç: Kısmen yeni bir yerel tip patlıcan çeşidi Solanum melongena L. 'Kadife', ekonomik uygunluğu ve iyi besin kalitesinden dolayı Türkiye'de yaygın olarak tüketilir. Bununla birlikte, patlıcanın yüksek polifenol içeriği, bu meyveyi polifenol oksidaz (PFO) tarafından katalizlenen istenmeyen oksidatif esmerleşmeye karşı duyarlı kılar. Dolayısıyla, bu çalışmanın temel amacı, gelişiminin üç safhasında bu patlıcan kültivarındaki PFO'yu karakterize etmektir. Metod: Bu çalışmada, olgunlaşma boyunca patlıcan meyvelerinden elde edilen kısmi saflaştı-rılmış PFO'nun substrat özgünlüğünü, optimum pH ve sıcaklığını, ve optimum substrat konsantrasyonunu belirledik. Bulgular: Olgunlaşmanın her üç safhasında, L-DOPA'nın tercih edilen PFO substratı olduğu ortaya konuldu. Olgunlaşmamış patlıcan özütlerinde optimum pH 5.0 ile 7.0 arasında geniş bir aktivite gösterirken olgun ve aşırı olgun patlıcan özütlerindeki PFO aktivitesi için optimum pH'nın 7.0 olduğu gözlendi. Genel olarak, tüm olgunlaşma safhalarında, PFO, 30°C'de en aktiftir ve inhibitör olarak sodyum metabisülfit ve askorbik aside oldukça duyarlıdır. 24, 2015] been named as "Kadife" for years by the local growers in northeast Anatolia (Turkey), at three different stages of maturation. The plant, with its light purple and white striped fruit is widely cultivated and consumed in Trabzon and elsewhere in the region compared to other species. Specifically, our aim was to determine PPO-specific activity from eggplants at time of flowering and at intervals of 2 weeks thereafter. In addition, we studied the effects of pH and temperature, as well as the effects of a variety of inhibitors and metal io...

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Cloning, expression and characterization of highly thermo- and pH-stable maltogenic amylase from a thermophilic bacterium Geobacillus caldoxylosilyticus TK4

Cited by 35 publications

References 29 publications

Evaluation of Amylase Activity Produced by Genetically Modified Bacillus Grown on Different Media Containing Sugar Crops Wastes

Evaluation of Amylase Activity Produced by Genetically Modified Bacillus Grown on Different Media Containing Sugar Crops Wastes

Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications

Characterization of polyphenol oxidase during three ripening stages of an eggplant (Solanum melongena L.) fruit: a local type in northeast Anatolia

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