Nano-coating of beta-galactosidase onto the surface of lactose by using an ultrasound-assisted technique.

Natalja Genina; Heikki Räikkönen; Jyrki Heinämäki; Peep Veski; Jouko Yliruusi

doi:10.1208/s12249-010-9462-4

Nano-coating of beta-galactosidase onto the surface of lactose by using an ultrasound-assisted technique.

Natalja Genina, Heikki Räikkönen, Jyrki Heinämäki, Peep Veski, Jouko Yliruusi

4 Citations (Scopus)

Abstract

We nano-coated powdered lactose particles with the enzyme β-galactosidase using an ultrasound-assisted technique. Atomization of the enzyme solution did not change its activity. The amount of surface-attached β-galactosidase was measured through its enzymatic reaction product D-galactose using a standardized method. A near-linear increase was obtained in the thickness of the enzyme coat as the treatment proceeded. Interestingly, lactose, which is a substrate for β-galactosidase, did not undergo enzymatic degradation during processing and remained unchanged for at least 1 month. Stability of protein-coated lactose was due to the absence of water within the powder, as it was dry after the treatment procedure. In conclusion, we were able to attach the polypeptide to the core particles and determine precisely the coating efficiency of the surface-treated powder using a simple approach.

Original language	English
Journal	AAPS PharmSciTech
Volume	11
Issue number	2
Pages (from-to)	959-965
Number of pages	7
ISSN	1530-9932
DOIs	https://doi.org/10.1208/s12249-010-9462-4
Publication status	Published - Jun 2010

Keywords

lactose
nano-coating
protein
ultrasound
β -galactosidase

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10.1208/s12249-010-9462-4

http://www.mendeley.com/research/nanocoating-betagalactosidase-onto-surface-lactose-using-ultrasoundassisted-technique

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title = "Nano-coating of beta-galactosidase onto the surface of lactose by using an ultrasound-assisted technique.",

abstract = "We nano-coated powdered lactose particles with the enzyme β-galactosidase using an ultrasound-assisted technique. Atomization of the enzyme solution did not change its activity. The amount of surface-attached β-galactosidase was measured through its enzymatic reaction product D-galactose using a standardized method. A near-linear increase was obtained in the thickness of the enzyme coat as the treatment proceeded. Interestingly, lactose, which is a substrate for β-galactosidase, did not undergo enzymatic degradation during processing and remained unchanged for at least 1 month. Stability of protein-coated lactose was due to the absence of water within the powder, as it was dry after the treatment procedure. In conclusion, we were able to attach the polypeptide to the core particles and determine precisely the coating efficiency of the surface-treated powder using a simple approach.",

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T1 - Nano-coating of beta-galactosidase onto the surface of lactose by using an ultrasound-assisted technique.

AU - Genina, Natalja

AU - Räikkönen, Heikki

AU - Heinämäki, Jyrki

AU - Veski, Peep

AU - Yliruusi, Jouko

PY - 2010/6

Y1 - 2010/6

N2 - We nano-coated powdered lactose particles with the enzyme β-galactosidase using an ultrasound-assisted technique. Atomization of the enzyme solution did not change its activity. The amount of surface-attached β-galactosidase was measured through its enzymatic reaction product D-galactose using a standardized method. A near-linear increase was obtained in the thickness of the enzyme coat as the treatment proceeded. Interestingly, lactose, which is a substrate for β-galactosidase, did not undergo enzymatic degradation during processing and remained unchanged for at least 1 month. Stability of protein-coated lactose was due to the absence of water within the powder, as it was dry after the treatment procedure. In conclusion, we were able to attach the polypeptide to the core particles and determine precisely the coating efficiency of the surface-treated powder using a simple approach.

AB - We nano-coated powdered lactose particles with the enzyme β-galactosidase using an ultrasound-assisted technique. Atomization of the enzyme solution did not change its activity. The amount of surface-attached β-galactosidase was measured through its enzymatic reaction product D-galactose using a standardized method. A near-linear increase was obtained in the thickness of the enzyme coat as the treatment proceeded. Interestingly, lactose, which is a substrate for β-galactosidase, did not undergo enzymatic degradation during processing and remained unchanged for at least 1 month. Stability of protein-coated lactose was due to the absence of water within the powder, as it was dry after the treatment procedure. In conclusion, we were able to attach the polypeptide to the core particles and determine precisely the coating efficiency of the surface-treated powder using a simple approach.

KW - lactose

KW - nano-coating

KW - protein

KW - ultrasound

KW - β -galactosidase

U2 - 10.1208/s12249-010-9462-4

DO - 10.1208/s12249-010-9462-4

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Nano-coating of beta-galactosidase onto the surface of lactose by using an ultrasound-assisted technique.

Abstract

Keywords

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