Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation

Slivinski, Christiane Trevisan; Machado, Alencar; Iulek, J.; Ayub, Ricardo Antônio; Almeida, Mareci Mendes de

doi:10.1590/s1516-89132011000300018

Cited by 29 publications

(17 citation statements)

References 24 publications

(19 reference statements)

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“…used commercially for the production of 6.0 and 7.0 for growth and enzyme production. However, this differs from the work carried out by Slivinski et al [29] and Nyamful [30]. In Nyamful's experiments [30], crude enzyme from A. niger had the highest amylase activity of 3.34 U/ml at pH 5.0, and when pH was increased beyond 5.0, activity declined to 2.60 U/ml at pH 6.0 and further down to 2.24 U/ml at pH 7.0.…”

Section: Discussioncontrasting

confidence: 91%

Characterization of Amylase from Some Aspergillus and Bacillus Species Associated with Cassava Waste Peels

Ayansina¹,

Adelaja²,

Mohammed³

2017

AiM

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Cassava peels are generated as waste on soils during cassava processing in many tropical countries. This work set out to isolate some microorganisms associated with cassava peel degradation and characterize amylase enzymes responsible for the degradation under some physiological conditions. A total of 30 bacteria was isolated from the peels with Bacillus species occurring the most (46.5%) and Enterobacter species (13.3%) being the next. Frequencies of fungal isolations was Rhizopus sp. (35%); Aspergillus niger (25%); Aspegillus flavus (20%) and Penicillium species (20%). Bacillus cereus, Bacillus substilis Bacillus pumillus, Aspergillus niger and Apergillus flavus were selected and screened for their abilities to produce amylase. Amylase activity was highest at day 4 for B. substilis (39.4 units/ml) and A. flavus (66.1 units/ml); at day 3 for B. cereus (55.6 units/ml) and A. niger (44.6 units/ ml). While maximum amylase activity was obtained at day 6 for B. pumilus (80.2 units/ml). Optimum pH for amylases from the two fungal isolate was 6.0 (A. niger = 53.5 units/ml and A. flavus = 65.4 units/ml). While optimum pH for B.cereus (51.7 units/ ml) and B. pumilus (44.6 units/ml) was 6.5 and for B. substilis (56.1 units/ml) at pH 7.0. Amylase activities increased from 20˚C to 40˚C for amylase from Bacillus sp. and 20˚C to 50˚C for amylase from the Aspergillus sp. after which there was a decline in activities as temperature increased to 80˚C. Effect of heating duration (at 70˚C for 5 minutes) on the amylase showed that A. niger has the highest activity of 127 units/ml. Effect of substrate concentration on amylase activity showed that amylase form A. flavus had the highest activity of 72.2 units/ml at 0.4% substrate concentration. The implications of the findings were discussed.

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Section: Discussioncontrasting

confidence: 91%

Characterization of Amylase from Some Aspergillus and Bacillus Species Associated with Cassava Waste Peels

Ayansina¹,

Adelaja²,

Mohammed³

2017

AiM

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“…Fold purification of both α-amylase and amyloglucosidase increased up to 4.1 and 4.2 times with a specific activity of 9.2 kUmg -1 and 393 kUmg -1 , respectively. Previously, Slivinski et al [29] and da Silva and Peralta [30] have also reported precipitation of amyloglucosidase using ammonium sulfate produced by A. niger and A. fumigatus , respectively . Ammonium sulfate precipitation method was also used for purification of α-amylase from Pencillium chrysogenum and A. niger JGI 24, respectively [31,32].…”

Section: Resultsmentioning

confidence: 99%

Saccharification and liquefaction of cassava starch: an alternative source for the production of bioethanol using amylolytic enzymes by double fermentation process

et al. 2014

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BackgroundCassava starch is considered as a potential source for the commercial production of bioethanol because of its availability and low market price. It can be used as a basic source to support large-scale biological production of bioethanol using microbial amylases. With the progression and advancement in enzymology, starch liquefying and saccharifying enzymes are preferred for the conversion of complex starch polymer into various valuable metabolites. These hydrolytic enzymes can selectively cleave the internal linkages of starch molecule to produce free glucose which can be utilized to produce bioethanol by microbial fermentation.ResultsIn the present study, several filamentous fungi were screened for production of amylases and among them Aspergillus fumigatus KIBGE-IB33 was selected based on maximum enzyme yield. Maximum α-amylase, amyloglucosidase and glucose formation was achieved after 03 days of fermentation using cassava starch. After salt precipitation, fold purification of α-amylase and amyloglucosidase increased up to 4.1 and 4.2 times with specific activity of 9.2 kUmg-1 and 393 kUmg-1, respectively. Concentrated amylolytic enzyme mixture was incorporated in cassava starch slurry to give maximum glucose formation (40.0 gL-1), which was further fermented using Saccharomyces cerevisiae into bioethanol with 84.0% yield. The distillate originated after recovery of bioethanol gave 53.0% yield.ConclusionAn improved and effective dual enzymatic starch degradation method is designed for the production of bioethanol using cassava starch. The technique developed is more profitable due to its fast liquefaction and saccharification approach that was employed for the formation of glucose and ultimately resulted in higher yields of alcohol production.

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“…However, higher K m value was observed in C. thermosaccharolyticum (18 mg/ ml) [60], P. oshimae (4.35 mg/ml) [32], and other bacterial glucoamylases [40]. Under similar substrate concentrations, the V max of A. niger was found to be lower 160.22 U/ ml [27], when compared our strain which exhibited 239.2 U/ ml. The hydrolysis rate of glucoamylase is affected by structure and size of the substrate, and exhibits an increase in reaction rate with increase in chain length [32].…”

Section: Discussionmentioning

confidence: 49%

Purification and biochemical characterization of extracellular glucoamylase from Paenibacillus amylolyticus strain

Lincoln

More²,

2019

J Basic Microbiol

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In the present study, glucoamylase produced from a soil bacterium Paenibacillus amylolyticus NEO03 was cultured under submerged fermentation conditions. The extracellular enzyme was purified by starch adsorption chromatography and further by gel filtration, with 2.73‐fold and recovery of 40.02%. The protein exhibited molecular mass of ∼66,000 Da as estimated by SDS–PAGE and depicted to be a monomer. The enzyme demonstrated optimum activity at pH range 6.0–7.0 and temperature range 30–40 °C. Glucoamylase was mostly activated by Mn2+ metal ions and depicted no dependency on Ca2+ ions. The enzyme preferentially hydrolyzed all the starch substrates. High substrate specificity was demonstrated towards soluble starch and kinetic values Km and Vmax were 2.84 mg/ml and 239.2 U/ml, respectively. The products of hydrolysis of soluble starch were detected by thin layer chromatography which showed only D‐glucose, indicating a true glucoamylase. The secreted glucoamylase from P. amylolyticus strain possesses properties suitable for saccharification processes such as biofuel production.

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Biochemical characterisation of a glucoamylase from Aspergillus niger produced by solid-state fermentation

Abstract: In this work, glucoamylase was produced by

Cited by 29 publications

References 24 publications

Characterization of Amylase from Some Aspergillus and Bacillus Species Associated with Cassava Waste Peels

Characterization of Amylase from Some Aspergillus and Bacillus Species Associated with Cassava Waste Peels

Saccharification and liquefaction of cassava starch: an alternative source for the production of bioethanol using amylolytic enzymes by double fermentation process

Purification and biochemical characterization of extracellular glucoamylase from Paenibacillus amylolyticus strain

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