Hydrolysis of lactose in whey permeate by immobilized β-galactosidase from Kluyveromyces fragilis

Perspectives and applications of immobilised β-galactosidase in food industry - a review

“…On the other hand, β-galactosidase immobilised in fibres composed of alginate and gelatin cross-linked with glutaraldehyde retained only 56% of its activity, but the immobilised enzyme was active for 35 days without any decrease in its activity (Tanriseven & Dogan 2002). Szczodrak (2000) reported more than 90% of initial enzyme activity after covalent binding of the enzyme on porous silanised glass without any notable decrease in enzyme activity during 5 repeated batch conversions. Similar result of good operational stability of immobilised enzyme was obtained with β-galactosidase immobilised in/on poly(2-hydroxyethyl methacrylate) (pHEMA) membranes by two different methods: adsorption on Cibacron F3GA derivatised pHEMA membranes (pHEMA-CB), and entrapment in the bulk of the pHEMA membranes.…”

“…The coupling efficiency was very high, since more than 90% of the enzyme was active and 87.5% of the protein was bound to the support. Dominguez et al (1988) entrapment in a spongy polyvinyl alcohol cryogel - Rossi et al (1999) entrapment in cobalt alginate beads cross-linked with glutaraldehyde 83 Ates & Mehmetoglu (1997) microencapsulation in alginate beads 64 Dashevsky (1998) encapsulation into gelatin and cross-linking with transglutaminase 8-46 Fuchsbauer et al (1996) adsorption on phenol-formaldehyde resin 54 Woudenberg-van Oosterom et al (1998) adsorption on polyvinylchloride (PVC) adsorption on silica gel membrane - Bakken et al (1990) adsorption on celite covalent binding to chitosan cross-linked aggregation by glutaraldehyde 2 18.4 13.5 Gaur et al (2006) covalent binding in polyurethane foams - Hu et al (1993) covalent binding to the tysolated cotton cloth 55 Albayrak & Yang (2002c) A. niger adsorption on a porous ceramic monolith 80 Papayannakos & Markas (1993) Chicken bean immobilised on cross-linked polyacrylamide gel 72 Sun et al (1999) (Szczodrak 2000). As well graphite was used for immobilisation of β-galactosidase (from K. lactis).…”

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

“…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].…”

Functionalized agarose as an effective and novel matrix for immobilizing Cicer arietinum β-galactosidase and its application in lactose hydrolysis

“…It has been well documented that plant and fungal β-galactosidases having acidic pHoptima are suitable for processing acid whey and whey permeate, whereas the enzymes from yeasts and bacteria exhibiting neutral pH-optima are suitable for processing milk. It has been reported earlier that β-galactosidase from Kluveromyces fragilis hydrolyzes whey permeate containing 5% lactose into 96% lactose in 48 h at 35 °C and pH 7.0 (Szczodrak, 2000). Zhou and Chen (2001) Reusability of GFA bound β-galactosidase (100 µL) was monitored for 6 successive days.…”