Thermal Stability of α-Amylase from <i>Aspergillus oryzae </i>Entrapped in Polyacrylamide Gel

Raviyan, Patcharin; Tang, Juming; Rasco, Barbara

doi:10.1021/jf020906j

Cited by 34 publications

(14 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The relative molecular mass of the enzymes determined by this method were 57 kDa and 32 kDa. These results were supported by the author's collectives (10,2). It is necessary to use other methods to purify the enzymes α-amylase and endoxylanase, because by the SDS -PAGE electrophoresis were obtained a lot of bands.…”

Section: Resultsmentioning

confidence: 53%

Identification and Characterization of α-Amylase and Endoxylanase, Produced byAspergillusMutant Strains

Evstatieva¹,

Nikolova²,

Ilieva³

et al. 2010

Biotechnology & Biotechnological Equipment

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 53%

Identification and Characterization of α-Amylase and Endoxylanase, Produced byAspergillusMutant Strains

Evstatieva¹,

Nikolova²,

Ilieva³

et al. 2010

Biotechnology & Biotechnological Equipment

View full text Add to dashboard Cite

show abstract

“…7) was found to be 74.85 kJ mol -1 , which was considerably lower than other reported enzymes [13]. The glucoamylase presented z value of 6.19, which indicates that to reduce 90 % of decimal reduction time, it is necessary to increase temperature by 6.19°C [26].…”

Section: Thermostability and Thermodynamics Of The Glucoamylasementioning

confidence: 60%

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

2013

View full text Add to dashboard Cite

Extracellular glucoamylase of Colletotrichum sp. KCP1 produced through solid state fermentation was purified by two steps purification process comprising ammonium sulphate precipitation followed by gel permeation chromatography (GPC). The Recovery of glucoamylase after GPC was 50.40 % with 19.3-fold increase in specific activity. The molecular weight of enzyme was found to be 162.18 kDa by native-PAGE and was dimeric protein of two sub-units with molecular weight of 94.62 and 67.60 kDa as determined by SDS-PAGE. Activation energy for starch hydrolysis was 26.45 kJ mol -1 while temperature quotient (Q 10 ) was found to be 1.9. The enzyme was found to be stable over wide pH range and thermally stable at 40-50°C up to 120 min while exhibited maximum activity at 50°C with pH 5.0. The pKa 1 and pKa 2 of ionisable groups of active site controlling V max were 3.5 and 6.8, respectively. V max , K m and K cat for starch hydrolysis were found to be 58.82 U ml -1 , 1.17 mg (starch) ml -1 and 449 s -1 , respectively. Activation energy for irreversible inactivation (E a(d) ) of glucoamylase was 74.85 kJ mol -1 . Thermodynamic parameters of irreversible inactivation of glucoamylase and starch hydrolysis were also determined.

show abstract

“…Polymers, sugar residues and even graphite (Pan et al, 2004) were attached to antibodies and proteins. A wide range of applications is known: clinical (Yavuz and Denizli, 2005;Acevedo et al, 2006), agricultural and food-chemical (Raviyan et al, 2003;Tumturk et al, 1999), affinity-and ion-exchange chromatography-related (Ruhn et al, 1994;Pessela et al, 2006;van Sommeren et al, 1993) and biotechnological (Kumada et al, 2006;Ong et al, 1991;Ong et al, 1989;Reetz et al, 1996).…”

Section: Immobilization On Beadsmentioning

confidence: 99%

Current Advances in Antibody Immobilization on Different Surfaces and Beads

Hahn¹,

Bakry²,

Huck³

et al. 2008

View full text Add to dashboard Cite

Antibody immobilization is of considerable interest for miscellaneous fields of interest, e.g. detecting biomarkers in cancer diagnostics, e.g. prostate specific antigen (PSA) for prostate cancer and pathogens like Escherichia coli, a foodborne pathogen. For this purpose, specific antibody captures are required and all of them should guarantee highest reproducibility and capacity possible. Especially in clinical applications very complex and specific immunoassays are needed. However, the complexity of pinning antibodies necessitates particular methods concerning the immobilization technique itself-because of their structure and specificity-and of course the analyzing methods. Glass, polymers, gold and even fullerene beads have been used as carriers, treated with various spacers and activation steps within the last few years. Furthermore, considerable attention is drawn to the regeneration of matrices and their capabilities for further antibody attachment. Commonly applied verification tools for the detection of the trapped antibodies include impedance spectroscopy (IS), atomic fluorescence microscopy (AFM), electrophoresis (EP), enzyme linked immunosorbent assays (ELISA), quartz crystal microbalance (QCM) and infrared spectroscopy (IR). Matrix assisted laser desorption/ionization-time-offlight mass spectrometry (MALDI-TOF/MS) is also a useful tool for proving the success of new antibody fixing procedures. Immobilization techniques have been improved concerning their reproducibility, binding capacity and high specificity. In this review, recent developments of antibody (Ab) immobilization are summarized, the individual applications are mentioned, advantages and disadvantages are discussed in detail.

show abstract

Thermal Stability of α-Amylase from Aspergillus oryzae Entrapped in Polyacrylamide Gel

Cited by 34 publications

References 24 publications

Identification and Characterization of α-Amylase and Endoxylanase, Produced byAspergillusMutant Strains

Identification and Characterization of α-Amylase and Endoxylanase, Produced byAspergillusMutant Strains

Kinetic and Thermodynamic Characterization of Glucoamylase from Colletotrichum sp. KCP1

Current Advances in Antibody Immobilization on Different Surfaces and Beads

Contact Info

Product

Resources

About