Purification and characterization of α-amylase from Trichoderma pseudokoningii

Abdulaal, Wesam H.

doi:10.1186/s12858-018-0094-8

Cited by 47 publications

(26 citation statements)

References 26 publications

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“…The optimal conditions of action of enzymes may vary according to the microorganism that produces. Amylases of fungal origin are required because they act mainly at lower temperatures and more acidic pH, when compared to the conditions of bacterial amylases that act at high temperatures, around 95 to 105ºC and pH close to neutral, between 5.8 and 6.8 (Abdulaal, 2018;Yan, Xiangsong, & Xiang, 2019). From the inspection of the response surface (Figure 1) it is possible to consider that the amylase produced by R. microsporus var.…”

Section: Nº Phmentioning

confidence: 99%

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Produção e caracterização da amilase obtida de Rhizopus microsporus var. oligosporus

Santos

Mendes

Miranda

et al. 2020

RSD

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Amylases have the ability to catalyze the α-1,4 binding of starch by releasing glucose and dextrin, with prominence in several industrial fields. The research sought to characterize the enzyme amylase obtained from the fungus Rhizopus microsporus var. oligosporus, through the Doehlert methodology, evaluating the behavior of the enzyme in the face of variations in pH and temperature. The production of amylase occurred with the use of starch as an inducer, and the characterization was carried out using the response surface methodology, with pH analysis at 5 levels (3.0, 4.0, 5.0, 6.0 and 7.0) and temperature in 3 levels (30, 50 and 70°C). The evaluation of the amylase thermostability occurred at 60, 70 and 80ºC. The application of the experimental model indicated that the amylase obtained from R. microsporus var. oligosporus shows better catalytic development at temperatures between 40ºC and 55ºC and pH between 2.5 and 3.2. The evaluation of thermostability indicated that the increase in temperature negatively influences the catalytic activity of amylase. The experimental model led to the understanding of the conditions favorable to the production of amylases from R. microsporus var. oligosporus.

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Section: Nº Phmentioning

confidence: 99%

“…Amylases consist of a group of hydrolases that catalyze the breakdown of starch molecules into dextrin, maltose and glucose units (Simair et al, 2017). They are important in industrial processes and have the largest share in the world enzyme market (Abdulaal, 2018).…”

Section: Introductionmentioning

confidence: 99%

Produção e caracterização da amilase obtida de Rhizopus microsporus var. oligosporus

Santos

Mendes

Miranda

et al. 2020

RSD

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“…The enzyme activity was also dropped to 74.32 and 78.67% when α-amylase was incubated with Cu 2+ and Cd 2+ ions. This result was higher than the activity of thermostable and alkaline α-amylase from Tepidimonas fonticaldi and thermostable α-amylase from Trichoderma pseudokoningii in the presence of 5 mM Cu 2+ and Cd 2+ ( Abdulaal, 2018 ; Allala et al, 2019 ).…”

Section: Discussionmentioning

confidence: 72%

Highly Efficient Computationally Derived Novel Metagenome α-Amylase With Robust Stability Under Extreme Denaturing Conditions

et al. 2021

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α-Amylases are among the very critical enzymes used for different industrial purposes. Most α-amylases cannot accomplish the requirement of industrial conditions and easily lose their activity in harsh environments. In this study, a novel α-amylase named PersiAmy1 has been identified through the multistage in silico screening pipeline from the rumen metagenomic data. The long-term storage of PersiAmy1 in low and high temperatures demonstrated 82.13 and 71.01% activities after 36 days of incubation at 4 and 50°C, respectively. The stable α-amylase retained 61.09% of its activity after 180 min of incubation at 90°C and was highly stable in a broad pH range, showing 60.48 and 86.05% activities at pH 4.0 and pH 9.0 after 180 min of incubation, respectively. Also, the enzyme could resist the high-salinity condition and demonstrated 88.81% activity in the presence of 5 M NaCl. PersiAmy1 showed more than 74% activity in the presence of various metal ions. The addition of the detergents, surfactants, and organic solvents did not affect the α-amylase activity considerably. Substrate spectrum analysis showed that PersiAmy1 could act on a wide array of substrates. PersiAmy1 showed high stability in inhibitors and superb activity in downstream conditions, thus useful in detergent and baking industries. Investigating the applicability in detergent formulation, PersiAmy1 showed more than 69% activity after incubation with commercial detergents at different temperatures (30–50°C) and retained more than 56% activity after incubation with commercial detergents for 3 h at 10°C. Furthermore, the results of the wash performance analysis exhibited a good stain removal at 10°C. The power of PersiAmy1 in the bread industry revealed soft, chewable crumbs with improved volume and porosity compared with control. This study highlights the intense power of robust novel PersiAmy1 as a functional bio-additive in many industrial applications.

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“…The most diverse groups of fungi isolated and identified were Aspergillus, Penicillium and Fusarium. Penicillium, Aspergillus and Trichoderma species have been reported in the recent past as a microbial source for producing alpha-amylases (Erdal and Taskin, 2010;Abdulaal, 2018;Lemo et al, 2019). found to be the most diverse group.…”

Section: Resultsmentioning

confidence: 99%

Amylase-Producing Fungi and Bacteria Associated with Some Food Processing Wastes

Okunwaye¹,

Uadia²,

Okogbenin³

et al. 2021

Nig. J. Biotechnol

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Amylases are enzymes that catalyze the hydrolysis of glycosidic bonds present in starch to release simple sugars. They are one of the most important enzymes in numerous commercial processes. In this investigation, fungal and bacterial strains from the following agro-industrial wastes were isolated and screened for amylolytic ability: soil from oil palm plantation, shea seed, date fruit, coconut meat, cassava effluent, cassava peel, cassava tubers, yam and potato tubers, starch medium, parboiled water from noodles and rice. The results revealed the presence of Geotrichum, Aspergillus, Penicillium, Trichoderma, Rhizopus and Fusarium spp. Five major genera of bacterial species namely Corynebacterium, Pseudomonas, Lactobacillus, Micrococcus and Bacillus were isolated and screened for amylase activity. Cassava soil had the highest heterotrophic bacterial count of 5.7 x105cfu/g and coconut meat waste had the lowest heterotrophic bacterial count of 1.3 x105cfu/g. All isolated microorganisms had the amylolytic ability. The fungal isolates had higher amylase activity when compared with the bacterial isolates. This investigation reveals organisms with high amylase activity.

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Purification and characterization of α-amylase from Trichoderma pseudokoningii

Cited by 47 publications

References 26 publications

Produção e caracterização da amilase obtida de Rhizopus microsporus var. oligosporus

Produção e caracterização da amilase obtida de Rhizopus microsporus var. oligosporus

Highly Efficient Computationally Derived Novel Metagenome α-Amylase With Robust Stability Under Extreme Denaturing Conditions

Amylase-Producing Fungi and Bacteria Associated with Some Food Processing Wastes

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