Extraction of amylase from fermentation broth in poly (Ethylene Glycol) salt aqueous two-phase system

Bezerra, Raquel Pedrosa; Borba, Fernanda Katharine Sousa Lins; Moreira, Keila Aparecida; Lima-Filho, J. L.; Porto, Ana Lúcia Figueiredo; Chaves, A. C.

doi:10.1590/s1516-89132006000500003

Cited by 34 publications

(17 citation statements)

References 28 publications

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“…6, the optimum temperature for activity was 50 8C in both the samples. In general, these results were in agreement with previous studies [40][41][42]. The results demonstrated that after the purification with PEG 4000-phosphate salt ATPS there was no change in the optimum pH and temperature of the a-galactosidase.…”

Section: Effect Nacl Concentration On A-galactosidase Partitioningsupporting

confidence: 93%

Aqueous two-phase extraction (ATPE): An attractive and economically viable technology for downstream processing of Aspergillus oryzae α-galactosidase

Naganagouda

Mulimani

2008

Process Biochemistry

108

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Section: Effect Nacl Concentration On A-galactosidase Partitioningsupporting

confidence: 93%

Aqueous two-phase extraction (ATPE): An attractive and economically viable technology for downstream processing of Aspergillus oryzae α-galactosidase

Naganagouda

Mulimani

2008

Process Biochemistry

108

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“…The temperature optima observed during the present investigations is in accordance with the temperature optima reported in B. cereus (Yoshigi et al, 1985). Thermostable amylases having temperature optima between 50 to 60°C have also been isolated from a number of sources including Bifidobacterium adolescentis (Lee et al, 1997), Aspergillus oryzea (Ramachandran et al, 2004), B. subtilis (Bezerra et al, 2006) and Bacillus sp. AB68 (Aygan et al, 2008).…”

Section: Temperature and Ph Optima And Km Valuesupporting

confidence: 89%

Purification and characterization of extracellular acidophilic -amylase from Bacillus cereus MTCC 10205 isolated from soil

Kumari¹,

Jain²,

Malhotra³

2013

Afr. J. Microbiol. Res.

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Amylase from Bacillus cereus MTCC 10205 was purified 20.41 with 11.82% recovery by ammonium sulfate precipitation, gel filtration chromatography through Sephadex G-100 and ion-exchange chromatography on diethylaminoethyl (DEAE)-cellulose. The final enzyme preparation was pure to near homogeneity as judged by native-polyacrylamide gel electrophoresis (PAGE). The enzyme had a molecular weight of 55 kDa as determined by gel filtration and a single band of 55 kDa as determined by sodium dodecyl sulfate-polycrylamide gel electrophoresis showing it to be a monomer. The purified enzyme had temperature optima of 55°C and pH optima of 5.5. The enzyme retained 72% of its original activity after 90 min of incubation and exhibited gradual loss in activity when incubated at higher temperature. At 60°C after 90 min of incubation, the enzyme was completely inactive. The enzyme appeared to be quite stable at 4°C as it could be stored upto five days with 10% loss in activity, whereas at 35°C, the enzyme lost 28% of its activity just after three days of storage. Inhibition studies revealed SH groups to be involved at the active site of the enzyme.

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“…As a general rule, positively charged proteins partition to the bottom phase, while negatively charged proteins are directed to the top phase [30]. Partitioning of the total proteins and the enzyme to these phases is dependent on their isoelectric points (pI).…”

Section: Influence Of Phmentioning

confidence: 99%

Purification of lipase produced by a new source of Bacillus in submerged fermentation using an aqueous two-phase system

Barbosa

Souza

Fricks

et al. 2011

Journal of Chromatography B

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Extraction of amylase from fermentation broth in poly (Ethylene Glycol) salt aqueous two-phase system

Abstract: ABSTRACT

Cited by 34 publications

References 28 publications

Aqueous two-phase extraction (ATPE): An attractive and economically viable technology for downstream processing of Aspergillus oryzae α-galactosidase

Aqueous two-phase extraction (ATPE): An attractive and economically viable technology for downstream processing of Aspergillus oryzae α-galactosidase

Purification and characterization of extracellular acidophilic -amylase from Bacillus cereus MTCC 10205 isolated from soil

Purification of lipase produced by a new source of Bacillus in submerged fermentation using an aqueous two-phase system

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