Isolation and characterization of a novel thermostable α-amylase from Korean pine seeds

Azad, Md. Abul Kalam; Bae, Jung Hoon; Kim, Jong-Sang; Lim, Jin Kyu; Song, Kyung‐Sik; Shin, Beomsu; Kim, Hak-Ryul

doi:10.1016/j.nbt.2009.09.006

Cited by 36 publications

(27 citation statements)

References 26 publications

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“…The amylase enzyme activity was evaluated after the storage following the standard assay condition. The ratio of amylase activity after storage time to the initial enzyme activity was given the efficiency of enzyme storage stability:

\begin{matrix} Storage stability (%) = \frac{A}{A_{0}} \times 100, \end{matrix}

where A is enzyme activity of amylase after storage time and A 0 is initial enzyme activity of amylase [13]. …”

Section: Methodsmentioning

confidence: 99%

Optimization of Processing Parameters for Extraction of Amylase Enzyme from Dragon (Hylocereus polyrhizus) Peel Using Response Surface Methodology

Amid

Manap

Zohdi

2014

The Scientific World Journal

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The main goal of this study was to investigate the effect of extraction conditions on the enzymatic properties of thermoacidic amylase enzyme derived from dragon peel. The studied extraction variables were the buffer-to-sample (B/S) ratio (1 : 2 to 1 : 6, w/w), temperature (−18°C to 25°), mixing time (60 to 180 seconds), and the pH of the buffer (2.0 to 8.0). The results indicate that the enzyme extraction conditions exhibited the least significant (P < 0.05) effect on temperature stability. Conversely, the extraction conditions had the most significant (P < 0.05) effect on the specific activity and pH stability. The results also reveal that the main effect of the B/S ratio, followed by its interaction with the pH of the buffer, was significant (P < 0.05) among most of the response variables studied. The optimum extraction condition caused the amylase to achieve high enzyme activity (648.4 U), specific activity (14.2 U/mg), temperature stability (88.4%), pH stability (85.2%), surfactant agent stability (87.2%), and storage stability (90.3%).

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\begin{matrix} Storage stability (%) = \frac{A}{A_{0}} \times 100, \end{matrix}

where A is enzyme activity of amylase after storage time and A 0 is initial enzyme activity of amylase [13]. …”

Section: Methodsmentioning

confidence: 99%

Optimization of Processing Parameters for Extraction of Amylase Enzyme from Dragon (Hylocereus polyrhizus) Peel Using Response Surface Methodology

Amid

Manap

Zohdi

2014

The Scientific World Journal

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“…The colonies were then incubated at 41.5°C for 36 h. Single colonies were selected on the basis of the greater ratio of the diameter of the colony to that of the transparent circle. The enzymatic activities of the selected mutant strains and the RL parental strain �ere tested b� culturing in 250�mL flasks (containing the shaking flask culture medium) at 41.5°C for 48 h. The enz�matic acti�it� of the mutant thermostable α-amylase was measured using a spectrophotometric method (Azad et al, 2009).…”

Section: Mutant Screeningmentioning

confidence: 99%

“…α-Amylase is important in the metabolism of maltose and maltodextrins. The potential for commercial application of α-amylases is enormous, and its preparation accounts for approximately 25% of the enzyme production market (Azad et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Improved thermostable α-amylase activity of Bacillus amyloliquefaciens by low-energy ion implantation

Zhang²,

Zhu³

2011

Genet. Mol. Res.

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ABSTRACT. Thermostable α-amylase is of great importance in the starch fermentation industry; it is extensively used in the manufacture of beverages, baby foods, medicines, and pharmaceuticals. Bacillus amyloliquefaciens produces thermostable α�am�lase� ho�e�er� produc� α�am�lase� ho�e�er� produc� -amylase; however, production of thermostable α-amylase is limited. Ion-beam implantation is an effective method for mutation breeding in microbes. We conducted ionbeam implantation experiments using two different ions, Ar + and N + , to determine the survival rate of and dose effect on a high α-amylase activity strain of B. amyloliquefaciens that had been isolated from soil samples. N + implantation resulted in a higher survival rate than Ar + implantation. The optimum implantation dose was 2.08 × 10 15 ions/ cm 2 . Under this implantation condition, we obtained a thermally and genetically stable mutant α-amylase strain (RL-1) with high enzyme activity for degrading α-amylase. Compared to the parental strain (RL), the RL-1 strain had a 57.1% increase in α-amylase activity. We conclude that ion implantation in B. amyloliquefaciens can produce strains with increased production of thermostable α-amylase.

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“…No doubt, amylases represent one of the most important groups of industrial enzymes, and occupy ~ 35% of global enzyme markets at present (Azad et al 2009). These enzymes play tremendous role in diversified industries viz.…”

Section: Introductionmentioning

confidence: 99%

Goat dung as a feedstock for hyper-production of amylase from Glutamicibacter arilaitensis strain ALA4

Aarti¹,

Khusro²,

Agastian³

2017

Bioresour. Bioprocess.

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Background:In modern times, bacteria-associated products; especially enzymes are gaining immense interest among worldwide researchers. Among several enzymes, amylases are of great significance in bioprocess engineering. This investigation was aimed to optimize the amylase production from Glutamicibacter arilaitensis strain ALA4 using goat dung as an inexpensive substrate in solid-state fermentation.Results: Amylase production was initially improved by optimizing physical factors and medium components by one factor at a time method. Two-level full factorial design (2 5 factorial matrix) was applied to screen the selected variables using first-order polynomial model. Parameters such as incubation temperature, moisture, starch, and yeast extract affected the amylase activity significantly (P < 0.05). Central composite design at N = 30 was further employed to evaluate the optimum levels of these variables by a second-order polynomial equation. Maximal amylase activity of 4572.53 ± 41.71 U/g was estimated in the goat dung medium supplemented with 100% moisture, 1% (w/w) starch, and 1% (w/w) yeast extract, being incubated at 40 °C. The optimized parameters revealed approximately twofold increment in the amylase yield (R 2 0.9169) with respect to the original medium. The amylase showed stability at high pH and temperature up to 4 h of incubation with residual activities of 52.32 ± 2.2 and 46.12 ± 3.3%, respectively. Additionally, the enzyme revealed resistant property not only towards various metal ions and organic solvents but also surfactants and inhibitors. Most importantly, the amylases obtained from strain ALA4 depicted remarkable tolerance to commercially available various detergents. Conclusions:This study reports first reference on the hyper-production of amylase from G. arilaitensis using goat dung as the low-cost agro-waste medium. G. arilaitensis strain ALA4 may be utilized for wide spread applications in several bioprocess industries due to the high stability of its amylase towards diversified pH, temperature, solvents, surfactants, and detergents.

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Isolation and characterization of a novel thermostable α-amylase from Korean pine seeds

Cited by 36 publications

References 26 publications

Optimization of Processing Parameters for Extraction of Amylase Enzyme from Dragon (Hylocereus polyrhizus) Peel Using Response Surface Methodology

Optimization of Processing Parameters for Extraction of Amylase Enzyme from Dragon (Hylocereus polyrhizus) Peel Using Response Surface Methodology

Improved thermostable α-amylase activity of Bacillus amyloliquefaciens by low-energy ion implantation

Goat dung as a feedstock for hyper-production of amylase from Glutamicibacter arilaitensis strain ALA4

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