Purification and characterization of theromohalophilic chitinase producing by halophilic Aspergillus flavus isolated from Suez Gulf

Beltagy, Ehab A.; Rawway, Mohammed; Abdul‐Raouf, Usama M.; El-Shenawy, Mohamed A.; Kelany, Mahmoud S.

doi:10.1016/j.ejar.2018.08.002

Cited by 19 publications

(13 citation statements)

References 27 publications

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“…Overnight, the crude was accelerated by ammonium sulfate with precipitated proteins separated at different saturation percentages (25%, 50%, 75%, and 90%). The precipitated sample was dialyzed overnight against water and barium chloride [ 33 ]. The ultimate purification process was performed using Sephadex G-50 with column dimension (2.6 × 20 cm), utilizing a test with 90% immersion precipitation.…”

Section: Methodsmentioning

confidence: 99%

Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Al-Agamy

Alhuzani

Kelany

et al. 2021

BioMed Research International

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Amylase producing actinobacteria were isolated and characterized from terrestrial environment. There are a limited number of reports investigating the marine environment; hence, in the present study, four marine enzymes were tested for their amylase production ability. On starch agar plates, the Streptomyces rochei strain showed a higher hydrolytic zone (24 mm) than the other isolates. Growth under optimized culture conditions using Plackett-Burman’s experimental design led to a 1.7, 9.8, 7.7, and 3.12-fold increase for the isolates S. griseorubens, S. rochei, S. parvus, and Streptomyces sp., respectively, in the specific activity measurement. When applying the Box-Behnken design on S. rochei using the most significant parameters (starch, K2HPO4, pH, and temperature), there was a 12.22-fold increase in the specific activity measurement 7.37 U/mg. The α-amylase was partially purified, and its molecular weight was determined using sodium dodecyl sulfate-polyacrylamide gel electrophoresis. α-Amylase was particularly active at pH 6 and 65°C. The purified enzyme was most active at 65°C and pH 6, thermal stability of 70°C for 40 min, and salt concentration of 1 M with Km and Vmax of 6.58 mg/ml and 21.93 μmol/ml/min, respectively. The α-amylase was improved by adding Cu+2, Zn+2, and Fe+2 (152.21%, 207.24%, and 111.89%). Increased production of α-amylase enzyme by S. rochei KR108310 leads to production of significant industrial products.

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Section: Methodsmentioning

confidence: 99%

Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Al-Agamy

Alhuzani

Kelany

et al. 2021

BioMed Research International

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“…Varied amounts of chitinolytic activity (0.0261 U mL −1 to 0.1340 U mL −1 ) were detected from different isolates of Metarhizium anisopliae cultivated in diverse culture media (Braga et al 1998). A. flavus was isolated as halophile fungus with chitinolytic activity at 0.8 M of NaCl (Beltagy et al 2018).…”

Section: Fig 5 Chitinase Activity Of Fungal Isolates Using Chitin Wit...mentioning

confidence: 99%

“…Recently, chitinase activity reached stability for Penicillium chrysogenum after 60 min at 50 °C, then declined with increased temperature (Atalla et al 2020). In another study, thermal stability of halophile A. flavus was recorded at 50 °C for 15 min (Beltagy et al 2018). A loss of chitinase activity for A. niger was observed after 3 h at 60 °C (Brzezinska and Jankiewicz 2012).…”

Section: Fig 5 Chitinase Activity Of Fungal Isolates Using Chitin Wit...mentioning

confidence: 99%

Halostability and thermostability of chitinase produced by fungi isolated from salt marsh soil in subtropical region of Saudi Arabia

Abboud

Al-Rajhi

Shater

et al. 2022

BioRes

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Strategies based on halo- and thermostable enzymes are promising and attractive for biotechnological applications. Three fungal isolates, namely Aspergillus flavus, Cladosporium cladosporioides, and Alternaria alternata, and were subjected to chitinase production using a medium with different concentrations of NaCl up to 10%. C. cladosporioides was found to be the main chitinase producer at high concentration of NaCl; therefore, its identification was confirmed using 18S rDNA. The highest chitinase production (88.67 U/mL) was obtained by C. cladosporioides, followed by A. flavus (76.17 U/mL), and A. alternata (70.67 U/mL) at 5% NaCl, while their production without NaCl was 35.07 U/mL, 22.83 U/mL, and 21.33 U/mL, respectively. Thermal stability of chitinase was recorded at 50 °C at 20 min. Chitinase halostability at 20 min indicated that 10% NaCl was the optimum level, with activity 88.3 U/mL. Safranin dye decolorization by C. cladosporioides was enhanced to 88.25% via the addition of 5% NaCl to growth medium containing chitin. The inhibitory activity of chitinase was detected against C. lunata and F. oxysporium with or without NaCl. Culex pipiens larvae were more affected by C. cladosporioides chitinase produced at 5% than 10% NaCl. Energy scores of the molecular docking investigations confirmed the insecticidal activity of chitinase against C. pipiens larvae.

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“…Overnight, the crude was accelerated by ammonium sulfate with precipitated proteins separated at different saturation percentages (25%, 50%, 75%, and 90%). The precipitated sample was dialyzed overnight against water and barium chloride (Beltagy et al 2018). The ultimate purification process was performed using Sephadex G-50, employing a test with 90% immersion precipitation.…”

Section: Puri Cation Of Amylase Enzymementioning

confidence: 99%

Production optimization using Plackett-Burman and Box-Behnken designs with partial characterization of amylase from marine actinomycetes

Bukhari

Al-Agamy

Kelany

et al. 2021

Preprint

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Amylase is an industrial enzyme that is used in the food and biofuel industries. We screened four actinomycetes strains for amylase biosynthesis. The Streptomyces rochei strain had a larger hydrolytic zone (24 mm) on starch agar plates, than the other isolates. Plackett-Burman’s experimental design was implemented to optimize the conditions for amylase production by the selected strains. Growth under optimized culture conditions led to 1.7, 9.8, 7.7, and 3.12 -fold increases for the isolates S. griseorubens, S. rochei, S. parvus, and Streptomyces sp., respectively, in the specific activity measurement in comparison with growth under primary conditions. When applying the Box-Behnken design on S. rochei using the most significant parameters starch, K2HPO4, pH, and temperature, there was a 12.22-fold increase in the specific activity measurement: 7.37 U/mg. The optimal fermentation medium formula was kept at 30.6°C for seven days. The amylase from S. rochei was partially purified, and its molecular weight was determined using Sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight was found to be 45, 43, and 53 kDa. Amylase was particularly active at pH 6 and 65°C. The purified enzyme was most active at 65°C and a pH of 6, thermal stability of 70°C for 40 min and salt concentration of 1 M with a Km and Vmax of 6.58 mg/ml and 21.93 mg/ml/min, respectively. The amylase improved by adding Cu + 2, Zn + 2, and Fe + 2 (152.21%, 207.24%, and 111.89%). Increased production of amylase enzyme by Streptomyces rochei KR108310 attracts the production of industrially significant products.

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Purification and characterization of theromohalophilic chitinase producing by halophilic Aspergillus flavus isolated from Suez Gulf

Cited by 19 publications

References 27 publications

Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Production and Partial Characterization of α-Amylase Enzyme from Marine Actinomycetes

Halostability and thermostability of chitinase produced by fungi isolated from salt marsh soil in subtropical region of Saudi Arabia

Production optimization using Plackett-Burman and Box-Behnken designs with partial characterization of amylase from marine actinomycetes

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