Microbial Alpha-Amylase Production: Progress, Challenges and Perspectives

Far, Babak Elyasi; Ahmadi, Yassin; Khosroshahi, Ahmad Yari; Dilmaghani, Azita

doi:10.34172/apb.2020.043

Cited by 88 publications

(34 citation statements)

References 65 publications

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“…In the present study, RSM-mediated optimization of process parameters for α-amylase production was performed using edible oil cakes with SSF. Previous studies on the optimization of α-amylase production have considered factors such as modifying nutritional parameters (C:N ratio, supplements, and other nutrients), physiological conditions (temperature, pH, inoculum load, and incubation time), the superiority of organisms (fungi and bacteria), and the method of fermentation (SSF and SmF) [1,12]. One factor at a time (OFAT) optimization was predominantly used to optimize α-amylase production [12,[20][21][22][23][24][25].…”

Section: Discussionmentioning

confidence: 99%

“…Amylases, identified in the eighteenth century, are found in animals, plants, insects, and microorganisms [ 1 ]. They belong to the family of GH13, with eight subfamilies known for hydrolyzing starch into glucose, maltose, and maltodextrins [ 2 ].…”

Section: Introductionmentioning

confidence: 99%

“…Commercial production of α-amylases using microorganisms such as fungi and bacteria represents around 30% of the world market on enzymes [ 1 ]. Fungi are more potential as α-amylase producers than bacteria.…”

Section: Introductionmentioning

confidence: 99%

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Optimization and scale-up of α-amylase production by Aspergillus oryzae using solid-state fermentation of edible oil cakes

et al. 2021

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Background Amylases produced by fungi during solid-state fermentation are the most widely used commercial enzymes to meet the ever-increasing demands of the global enzyme market. The use of low-cost substrates to curtail the production cost and reuse solid wastes are seen as viable options for the commercial production of many enzymes. Applications of α-amylases in food, feed, and industrial sectors have increased over the years. Additionally, the demand for processed and ready-to-eat food has increased because of the rapid growth of food-processing industries in developing economies. These factors significantly contribute to the global enzyme market. It is estimated that by the end of 2024, the global α-amylase market would reach USD 320.1 million (Grand View Research Inc., 2016). We produced α-amylase using Aspergillus oryzae and low-cost substrates obtained from edible oil cake, such as groundnut oil cake (GOC), coconut oil cake (COC), sesame oil cake (SOC) by solid-state fermentation. We cultivated the fungus using these nutrient-rich substrates to produce the enzyme. The enzyme was extracted, partially purified, and tested for pH and temperature stability. The effect of pH, incubation period and temperature on α-amylase production using A. oryzae was optimized. Box–Behnken design (BBD) of response surface methodology (RSM) was used to optimize and determine the effects of all process parameters on α-amylase production. The overall cost economics of α-amylase production using a pilot-scale fermenter was also studied. Results The substrate optimization for α-amylase production by the Box–Behnken design of RSM showed GOC as the most suitable substrate for A. oryzae, as evident from its maximum α-amylase production of 9868.12 U/gds. Further optimization of process parameters showed that the initial moisture content of 64%, pH of 4.5, incubation period of 108 h, and temperature of 32.5 °C are optimum conditions for α-amylase production. The production increased by 11.4% (10,994.74 U/gds) by up-scaling and using optimized conditions in a pilot-scale fermenter. The partially purified α-amylase exhibited maximum stability at a pH of 6.0 and a temperature of 55 °C. The overall cost economic studies showed that the partially purified α-amylase could be produced at the rate of Rs. 622/L. Conclusions The process parameters for enhanced α-amylase secretion were analyzed using 3D contour plots by RSM, which showed that contour lines were more oriented toward incubation temperature and pH, having a significant effect (p < 0.05) on the α-amylase activity. The optimized parameters were subsequently employed in a 600 L-pilot-scale fermenter for the α-amylase production. The substrates were rich in nutrients, and supplementation of nutrients was not required. Thus, we have suggested an economically viable process of α-amylase production using a pilot-scale fermenter.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Optimization and scale-up of α-amylase production by Aspergillus oryzae using solid-state fermentation of edible oil cakes

et al. 2021

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“…Hitherto, microbial α -amylase is used commercially as biocatalysts in various industries, such as detergent, syrup, bread and cake, dairy products, starch processing, animal feed, textile and leather, pulp and paper, candy, sugar, bioethanol, pharmaceuticals, and waste treatment [ 1 , 2 ]. Furthermore, it has a 25% demand in the global market [ 3 ].…”

Section: Introductionmentioning

confidence: 99%

The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

Yandri

Tiarsa

Suhartati

et al. 2022

Biochemistry Research International

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The stability of the α-amylase enzyme has been improved from Aspergillus fumigatus using the immobilization method on a bentonite matrix. Therefore, this study aims to obtain the higher stability of α-amylase enzyme from A. fumigatus; hence, it is used repeatedly to reduce industrial costs. The procedures involved enzyme production, isolation, partial purification, immobilization, and characterization. Furthermore, the soluble enzyme was immobilized using 0.1 M phosphate buffer of pH 7.5 on a bentonite matrix, after which it was characterized with the following parameters such as optimum temperature, Michaelis constant (KM), maximum velocity V max , thermal inactivation rate constant (ki), half-life (t1/2), and the change of energy due to denaturation (ΔGi). The results showed that the soluble enzyme has an optimum temperature of 55°C, KM of 3.04 mg mL−1 substrate, V max of 10.90 μmole mL−1 min−1, ki of 0.0171 min−1, t1/2 of 40.53 min, and ΔGi of 104.47 kJ mole−1, while the immobilized enzyme has an optimum temperature of 70°C, KM of 8.31 mg mL−1 substrate, V max of 1.44 μmole mL−1 min−1, ki of 0.0060 min−1, t1/2 of 115.50 min, and ΔGi of 107.37 kJ mole−1. Considering the results, the immobilized enzyme retained 42% of its residual activity after six reuse cycles. Additionally, the stability improvement of the α-amylase enzyme by immobilization on a bentonite matrix, based on the increase in half-life, was three times greater than the soluble enzyme.

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“…In automatic dishwasher and laundry, detergent formulations are fortified with alkaline amylases (higher than 8.0) [6,7] to improve the ability of the detergents to remove tough stains, making the detergent environmentally friendly [8]. Detergent enzymes represent one of the largest and most successful applications of modern industrial biotechnology since they account for about 40% of the total worldwide enzyme production [9].…”

Section: Introductionmentioning

confidence: 99%

An Alkalothermophilic Amylopullulanase from the Yeast Clavispora lusitaniae ABS7: Purification, Characterization and Potential Application in Laundry Detergent

et al. 2021

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In the present study, α-amylase and pullulanase from Clavispora lusitaniae ABS7 isolated from wheat seeds were studied. The gel filtration and ion-exchange chromatography revealed the presence of α-amylase and pullulanase activities in the same fraction with yields of 23.88% and 21.11%, respectively. SDS-PAGE showed a single band (75 kDa), which had both α-amylase (independent of Ca2+) and pullulanase (a calcium metalloenzyme) activities. The products of the enzymatic reaction on pullulan were glucose, maltose, and maltotriose, whereas the conversion of starch produced glucose and maltose. The α-amylase and pullulanase had pH optima at 9 and temperature optima at 75 and 80 °C, respectively. After heat treatment at 100 °C for 180 min, the pullulanase retained 42% of its initial activity, while α-amylase maintained only 38.6%. The cations Zn2+, Cu2+, Na+, and Mn2+ increased the α-amylase activity. Other cations Hg2+, Mg2+, and Ca2+ were stimulators of pullulanase. Urea and Tween 80 inhibited both enzymes, whereas EDTA only inhibited pullulanase. In addition, the amylopullulanase retained its activity in the presence of various commercial laundry detergents. The performance of the alcalothermostable enzyme of Clavispora lusitaniae ABS7 qualified it for the industrial use, particularly in detergents, since it had demonstrated an excellent stability and compatibility with the commercial laundry detergents.

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Microbial Alpha-Amylase Production: Progress, Challenges and Perspectives

Cited by 88 publications

References 65 publications

Optimization and scale-up of α-amylase production by Aspergillus oryzae using solid-state fermentation of edible oil cakes

Optimization and scale-up of α-amylase production by Aspergillus oryzae using solid-state fermentation of edible oil cakes

The Stability Improvement of α-Amylase Enzyme from Aspergillus fumigatus by Immobilization on a Bentonite Matrix

An Alkalothermophilic Amylopullulanase from the Yeast Clavispora lusitaniae ABS7: Purification, Characterization and Potential Application in Laundry Detergent

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