Optimal immobilization of β-galactosidase from Pea (PsBGAL) onto Sephadex and chitosan beads using response surface methodology and its applications

Dwevedi, Alka; Kayastha, Arvind M.

doi:10.1016/j.biortech.2008.12.048

Cited by 90 publications

(47 citation statements)

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“…Ozdural [7,21,22,24]. 고정화 방법으로는 효소와 담체 사이에 공유결합 방법 [3,4], 담체에 효소를 물리적 흡착 방법 [28], 그리고 효소 를 알지네이트와 같은 고분자 매트릭스에 캡슐화하는 방법 등이 있다 [9,10]. 고정화 효소에 대한 반응기로는 충진층 (packed bed) 반응기, 유동층 반응기 그리고 막(membrane) 반응기 등이 있다 [11,26,27].…”

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Analysis of an Immobilized β-Galactosidase Reactor with Competitive Product Inhibition Kinetics

Kang

2013

Journal of Life Science

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The present study deals with the immobilization of Kluyveromyces lactis β-galactosidase on a weak ionic exchange resin (Duolite A568) as polymer support. β-Galactosidase was immobilized using the adsorption method. A kinetic study of the immobilized enzyme was performed in a packed-bed reactor. The adsorption of the enzyme followed a typical Freundlich adsorption isotherm. The adsorption parameters of k and n were 14.6 and 1.74, respectively. The initial rates method was used to characterize the kinetic parameters of the free and immobilized enzymes. The Michaelis-Menten constant (Km) for the immobilized enzyme (120 mM) was higher than it was for the free enzyme (79 mM). The effect of competitive inhibition kinetics was studied by changing the concentration of galactose in a recycling packed-bed reactor. The kinetic model with competitive inhibition by galactose was best fitted to the experimental results with Vm, Km, and KI values of 46.3 mmolmin -1 mg -1 , 120 mM, and 24.4 mM, respectively. In a continuous packed-bed reactor, increasing the flow rate of the lactose solution decreased the conversion efficiency of lactose at different input lactose concentrations. Continuous operation of 11 days was conducted to investigate the stability of a long-term operation. The retained activity of the immobilized enzymes was 63% and the half-life of the immobilized enzyme was found to be 15 days.

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Analysis of an Immobilized β-Galactosidase Reactor with Competitive Product Inhibition Kinetics

Kang

2013

Journal of Life Science

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“…However, an efficiency of 48.2% β-glucosidase immobilisation has been reported from almonds on chitosan activated with 0.5% glutaraldehyde (Chang and Juang 2007). Immobilisation of mature seeds soybean urease and of pea β-galactosidase on chitosan activated with 1.0% glutaraldehyde resulted in 65 and 67% efficiency, respectively (Kumar et al 2009;Dwevedi and Kayastha 2009). These differences in immobilisation efficiencies could be attributed to the diversity of enzymes used and the type of interactions between the enzyme and matrix.…”

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confidence: 99%

Soybean β-Glucosidase immobilisated on chitosan beads and its application in soy drink increase the aglycones

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Moreira

Varéa

et al. 2014

Braz. arch. biol. technol.

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“…Po 10 izpiranjih je bila izguba aktivnosti pri hitozan imobilizirani PsBGal zanemarljiva, medtem ko se je pri dekstran imobilizirani PsBgal aktivnost zmanjšala za 70 %. To kaže, da se encim močneje veže na hitozan kot na dekstran (Dwevedi in Kayastha, 2009). Duarte in sod.…”

Section: Imobilizacijaunclassified

Potential applicaton of β-galactosidase in food science and nutrition

Žibrat

Skrt

Jamnik

2017

AAS

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3 Isti naslov kot: 1 Uporaba β-galaktozidaze na področju živilstva in prehrane β-galaktozidaza je encim s hidrolitično in transgalaktozilacijsko aktivnostjo. Vrsta aktivnosti je odvisna od izvora encima. V industriji uporabljene β-galaktozidaze so pridobljene z rekombinantno produkcijo iz nitastih gliv Aspergillus sp. in kvasovk Kluyveromyces sp. V zadnjem času se vedno bolj preučujejo β-galaktozidaze, ki optimalno delujejo pri nizkih ali visokih temperaturah. V industrijskih procesih se β-galaktozidaza uporablja v obliki prostega encima ali v imobilizirani obliki. Imobilizacija pogosto ponuja večjo stabilnost encima, možnost ponovne uporabe ter znižanje stroškov. β-galaktozidaza se pretežno uporablja na področju živilstva in prehrane, v zadnjem času pa ima znatno vlogo tudi v medicini. Hidrolitična aktivnost β-galaktozidaze se že dolgo izkorišča za zmanjšanje vsebnosti laktoze v mleku, medtem ko z reakcijami transgalaktozilacije iz laktoze lahko sintetiziramo različne produkte, kot so galaktooligosaharidi, laktosaharoza in drugi. Prav slednji imajo velik potencial v živilski industriji zaradi pridobivanja izdelkov z zmanjšano vsebnostjo laktoze in izboljšanja prehranske vrednosti živil s proizvodnjo galaktooligosaharidov. Kljub temu je potrebno bolje razumeti reakcijske mehanizme kot tudi optimizirati procese, da bo uporaba encima za ta namen dosegla industrijsko raven.Ključne besede: prehrana ljudi; živilska industrija; živil-stvo; encimi; beta-galaktozidaza Potential applicaton of β-galactosidase in food science and nutrition β-galactosidase is an enzyme with hydrolytic and transgalactosylation activity. The origin of the enzyme dictates the balance between both activities. Industrially used β-galactosidases are obtained with recombinant production from filamentus funghi Aspergillus sp. and yeasts Kluyveromyces sp. Recently thermostabile β-galactosidases have been subject of many research. The enzyme can be industrially used in free or immobilized form. Immobilization often provides better stability, reusability and lower expenses. Application of β-galactosidase is most common in food processing and nutrition, it is also used in medicine and ecology. Hydrolytic activity of the enzyme has long been used for reducing lactose content in milk, while transgalactosylitic activity is used for synthesis of products such as galactooligosaccharides, lactosucrose and others. The latter have a great potential in food industry for obtaining products with reduced lactose content and increasing of nutritional value by adding dietetic fibers such as galactooligosaccharides. Despite the potential it is vital that reaction mechanisms become better understood and optimization is in place in order to reach the usability of this enzyme at industrial level.

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Optimal immobilization of β-galactosidase from Pea (PsBGAL) onto Sephadex and chitosan beads using response surface methodology and its applications

Cited by 90 publications

References 29 publications

Analysis of an Immobilized β-Galactosidase Reactor with Competitive Product Inhibition Kinetics

Analysis of an Immobilized β-Galactosidase Reactor with Competitive Product Inhibition Kinetics

Soybean β-Glucosidase immobilisated on chitosan beads and its application in soy drink increase the aglycones

Potential applicaton of β-galactosidase in food science and nutrition

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