Structural and catalytic properties of immobilized α-amylase from Laceyella sacchari TSI-2

Shukla, Rushit J.; Singh, Satya P.

doi:10.1016/j.ijbiomac.2015.12.079

Cited by 28 publications

(10 citation statements)

References 28 publications

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“…It also leads to increase the temperature optimum and thermal stability of the enzymes from 60°to 70 °C. 67 Similar results with 84% efficiency of α-amylase immobilized on DEAE cellulose were reported by Kikani et.al. 68 Synthetic polymers are often applied for lipase immobilization.…”

Section: ■ Carrier Materialssupporting

confidence: 85%

“…Use of the DEAE cellulose with glutaraldehyde as a cross-linking agent for α-amylase immobilization provides maximum (68%) of enzyme efficiency and reusability during six cycles keeping 49% of the initial activity. It also leads to increase the temperature optimum and thermal stability of the enzymes from 60° to 70 °C . Similar results with 84% efficiency of α-amylase immobilized on DEAE cellulose were reported by Kikani et.al …”

Section: Organic Carrierssupporting

confidence: 85%

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Application of Immobilized Enzymes in Food Industry

Yushkova

Nazarova

Matyuhina

et al. 2019

J. Agric. Food Chem.

144

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Enzymes are macromolecular biocatalysts, widely used in food industry. In applications, enzymes are often immobilized on inert and insoluble carriers, which increase their efficiency due to multiple reusability. The properties of immobilized enzymes depend on the immobilization method and the carrier type. The choice of the carrier usually concerns the biocompatibility, chemical and thermal stability, insolubility under reaction conditions, capability of easy regeneration and reusability, as well as cost efficiency. In this review, we provide an overview of various carriers for enzyme immobilization, with the primary focus on food industry.

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Section: ■ Carrier Materialssupporting

confidence: 85%

Section: Organic Carrierssupporting

confidence: 85%

Application of Immobilized Enzymes in Food Industry

Yushkova

Nazarova

Matyuhina

et al. 2019

J. Agric. Food Chem.

144

View full text Add to dashboard Cite

show abstract

“…Immobilized and soluble enzymes showed optima activities at 70 °C and 68 °C, respectively [166]. On the other hand, Shukla [167] activated DEAE-cellulose with glutaraldehyde and found that α-amylase immobilized by covalent attachment to this support improved its optimal temperature, from 60 °C to 70 °C. The maxima activities of free and immobilized enzymes were observed at pH 7.0.…”

Section: The Gh13 Family Of Enzymesmentioning

confidence: 99%

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

et al. 2016

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Glycoside hydrolases (GH) are enzymes capable to hydrolyze the glycosidic bond between two carbohydrates or even between a carbohydrate and a non-carbohydrate moiety. Because of the increasing interest for industrial applications of these enzymes, the immobilization of GH has become an important development in order to improve its activity, stability, as well as the possibility of its reuse in batch reactions and in continuous processes. In this review, we focus on the broad aspects of immobilization of enzymes from the specific GH families. A brief introduction on methods of enzyme immobilization is presented, discussing some advantages and drawbacks of this technology. We then review the state of the art of enzyme immobilization of families GH1, GH13, and GH70, with special attention on the enzymes β-glucosidase, α-amylase, cyclodextrin glycosyltransferase, and dextransucrase. In each case, the immobilization protocols are evaluated considering their positive and negative aspects. Finally, the perspectives on new immobilization methods are briefly presented.

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“…The α-amylases from Bacillus licheniformis AT70 , A. Niger strains , R. oryzae FSIS4 , Fusarium sp. and Laceyella sacchari TSI-2 have been reported to retain residual activity of 70-90% at temperatures between 40-60 °C [ 34 – 38 ]. The α-amylase produced from thermophilic fungal strains STG3E and STG6E showed maximum amylase activity at 55 °C after 10 min incubation [ 26 ].…”

Section: Discussionmentioning

confidence: 99%

Random mutagenesis of super Koji (Aspergillus oryzae): improvement in production and thermal stability of α-amylases for maltose syrup production

et al. 2018

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BackgroundAlpha-amylases hydrolyze 1,4 α-glycosidic bonds of starch and produce malto-oligosaccharides. It is an important enzyme generally applied in textile, food and brewing industries. Enhancement in thermal stability and productivity of enzymes are the two most sought after properties for industrial use. The Aspergillus oryzae (Koji) has Generally Recognized as Safe (GRAS) status and safe for use in food industry. Hence, Koji strain’s development for the screening of potent mutants, hyper producer of thermostable α-amylases, with desired attributes is the need of the time.ResultsA process has been developed to improve super Koji (A. oryzae cmc1) strain through γ-rays treatment. The doses i.e. 0.60, 0.80, 1.00, 1.20 & 1.40 KGy gave more than 3.0 log kill. Initially, 52 Koji mutants resistant to 1% (w/v) Triton X-100 were selected. 2nd screening was based on α-amylases hyper production and 23 mutants were sorted out by measuring clearing zones index (CI). Afterwards nine potent mutants, resistant to 2-deoxy D-glucose, were screened based on CI. These were further analyzed for thermal stability and productivity of α-amylase under submerged conditions. The mutants’ M-80(10), M-100(6) & M-120(5) gave about four fold increases in α-amylases productivity. The half life of M-100(6) α-amylase at 55 °C was 52 min and was highest among the mutants. Liquid Chromatography-Mass Spectrometry (LC-MS) analysis confirmed that mutants did not produce aflatoxins. Field Emission Scanning Electron Microscopy (FESEM) of Koji mycelia depicted that exposure to gamma rays increased rigidity of the mycelium. The potent Koji mutant M-100(6) was grown on soluble starch in 10L fermenter and produced 40.0 IU ml-1 of α-amylases with specific activity of 2461 IU mg-1 protein. Growth kinetic parameters were: μ = Specific growth rate= 0.069 h-1, td = Biomass doubling time= 10.0 h, Yp/x = Product yield coefficient with respect to cell mass = 482 U g-1; qp= Specific rate of product formation= 33.29 U g-1 h-1.ConclusionIt was concluded that the developed five step screening process has great potential to generate potent mutants for the hyper production of thermostable enzymes through γ-rays mediated physical mutagenesis. The developed thermostable α-amylases of super Koji mutantM-100(6) has immense potential for application in saccharification process for maltose syrup production. Moreover, the developed five step strain’s development process may be used for the simultaneous improvement in productivity and thermal stability of other microbial enzymes.Electronic supplementary materialThe online version of this article (10.1186/s12866-018-1345-y) contains supplementary material, which is available to authorized users.

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Structural and catalytic properties of immobilized α-amylase from Laceyella sacchari TSI-2

Cited by 28 publications

References 28 publications

Application of Immobilized Enzymes in Food Industry

Application of Immobilized Enzymes in Food Industry

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

Random mutagenesis of super Koji (Aspergillus oryzae): improvement in production and thermal stability of α-amylases for maltose syrup production

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