Production, purification and characterization of α-amylase from Trichoderma harzianum grown on mandarin peel

Mohamed, Saleh A.; Azhar, Esam I.; Baakdah, Morooj M.; Tashkandy, Nisreen R; Kumosani, Taha

doi:10.5897/ajmr10.890

Cited by 7 publications

(3 citation statements)

References 42 publications

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“…As compared to the present study conducted for effect of cultivation time on production of amylase, similar result was reported by Negi and Banerjee (2010) for amylase biosynthesis using A. awamori . Mohamed et al (2011) reported 96 h and 30°C for biosynthesis of amylase which is in accordance with present finding. However, Han et al (2013) have reported a multifunctional α-amylase from Malbranchea cinnamomea on the fifth day when wheat bran, rice bran and glutinous rice flour were employed as the carbon source under the optimized conditions.…”

Section: Discussionsupporting

confidence: 93%

Production of α-Amylase by Aspergillus terreus NCFT 4269.10 Using Pearl Millet and Its Structural Characterization

Sethi

Jana

Nanda³

et al. 2016

Front. Plant Sci.

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In this investigation, Aspergillus terreus NCFT4269.10 was employed in liquid static surface (LSSF) and solid state (SSF) fermentation to assess the optimal conditions for α-amylase biosynthesis. One-variable-at-a-time approach (quasi-optimum protocol) was primarily used to investigate the effect of each parameter on production of amylase. The maximum amylase production was achieved using pearl millet (PM) as substrate by SSF (19.19 ± 0.9 Ug−1) and also in presence of 1 mM magnesium sulfate, 0.025% (w/v) gibberellic acid, and 30 mg/100 ml (w/v) of vitamin E (~60-fold higher production of amylase) with the initial medium pH of 7.0 and incubation at 30 °C for 96 h. In addition, maltose, gelatin and isoleucine also influenced the α-amylase production. Amylase was purified to homogeneity with molecular mass around 15.3 kDa. The enzyme comprised of a typical secondary structure containing α-helix (12.2%), β-pleated sheet (23.6%), and β-turn (27.4%). Exploitation of PM for α-amylase production with better downstream makes it the unique enzyme for various biotechnological applications.

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Section: Discussionsupporting

confidence: 93%

Production of α-Amylase by Aspergillus terreus NCFT 4269.10 Using Pearl Millet and Its Structural Characterization

Sethi

Jana

Nanda³

et al. 2016

Front. Plant Sci.

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“…The Talaromyces pinophilus α-amylase (TpAA) was most active at pH 4.0-5.0 [50] and the maximum activity of α-amylase from Trichoderma harzianum against soluble starch was determined at pH 4.5 and 40 • C [51].…”

Section: Effect Of Ph On α-Amylase and Pullulanase Activitiesmentioning

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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“…Optimum neural pH was recorded for xylanase from Aspergillus caespitosus (pH 6.5-7.0) 41 . At pH 4.5, the maximum production of α-amylase was detected for Trichoderma harzianum 42 . α-amylase producing yeast strains such as Saccharomyces cerevisiae and S. kluyveri exhibited maximum enzyme production at pH 5.0 43 .…”

Section: Discussionmentioning

confidence: 97%

Production and Optimization of Xylanase and α-Amylase from Non-Saccharomyces Yeasts (Pichia membranifaciens)

Salah¹,

Temerk²,

Salah³

et al. 2021

J Pure Appl Microbiol

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The xylanolytic and amylolytic yeasts were qualitatively determined by Cong red xylan agar and soluble starch agar plates, respectively. The most xylanase and α-amylase inducible strain (AUN-02) was selected and identified using PCR amplification of 26S rRNA gene and sequence analysis. The comparison of the alignment results and phylogenetic analysis of the sequences of the isolated yeast to published rRNA gene sequences in GenBank, confirmed the identification of the isolate as Pichia membranifaciens. Xylanase and α-amylase production by isolated P. membranifaciens were investigated at different pH values (4-8), temperature degrees (20-45°C), incubation time (1-7 days) and various substrates.A higher production of xylanase (38.8 U/mL) and a-amylase (28.7 U/mL) was obtained after 4 days of fermentation of P. membranifaciens. Higher activity of xylanase (36.83 U/mL) and a-amylase (27.7 U/mL) was obtained in the fermentation of P. membranifaciens in a culture medium adjusted to pH 7.0. The optimum temperature showed maximum xylanase and a-amylase activity (42.6 and 32.5 units/mL, respectively) was estimated at 35 °C. The xylanase and a-amylase activities of P. membranifaciens were estimated and compared for the different substrates tested. The strain revealed 100% relative activity of xylanase and a-amylase on beechwood and potato starch, respectively. The affinity of enzymes towards substrate was estimated using Km values. The Km values of xylanase and α-amylase increased in the order of pH’s 7.0, 6.0 and 4.5 (0.85, 1.6 and 3.4 mg xylan/mL and 0.22, 0.43 and 2.8 mg starch/mL, respectively). the yeast P. membranifaciensis is suitable for produce neutral xylanase and α-amylase enzymes. So, it could be used as a promising strain for production of these enzymes in industrial field.

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Production, purification and characterization of α-amylase from Trichoderma harzianum grown on mandarin peel

Cited by 7 publications

References 42 publications

Production of α-Amylase by Aspergillus terreus NCFT 4269.10 Using Pearl Millet and Its Structural Characterization

Production of α-Amylase by Aspergillus terreus NCFT 4269.10 Using Pearl Millet and Its Structural Characterization

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

Production and Optimization of Xylanase and α-Amylase from Non-Saccharomyces Yeasts (Pichia membranifaciens)

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