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Enhanced ß-galactosidase production from whey powder by a mutant of the psychrotolerant yeast Guehomyces pullulans 17-1 for hydrolysis of lactose.
Xu, Jin-Li; Zhao, Jun; Wang, Ling-Fei; Sun, Huai-Yong; Song, Chun-Li; Chi, Zhen-Ming.
Afiliação
  • Xu JL; UNESCO Chinese Center of Marine Biotechnology and Institute of Marine Biodiversity and Evolution, Ocean University of China, Yushan Road, No. 5, Qingdao 266003, China.
Appl Biochem Biotechnol ; 166(3): 599-611, 2012 Feb.
Article em En | MEDLINE | ID: mdl-22086565
ABSTRACT
In order to isolate ß-galactosidase overproducers of the psychrotolerant yeast Guehomyces pullulans 17-1, its cells were mutated by using nitrosoguanidine (NTG). One mutant (NTG-133) with enhanced ß-galactosidase production was obtained. The mutant grown in the production medium with 30.0 g/l lactose and 2.0 g/l glucose could produce more ß-galactosidase than the same mutant grown in the production medium with only 30.0 g/l lactose while ß-galactosidase production by its wild type was sensitive to the presence of glucose in the medium. It was found that 40.0 g/l of the whey powder was the most suitable for ß-galactosidase production by the mutant. After optimization of the medium and cultivation conditions, the mutant could produce 29.2 U/ml of total ß-galactosidase activity within 132 h at the flask level while the mutant could produce 48.1 U/ml of total ß-galactosidase activity within 144 h in 2-l fermentor. Over 77.1% of lactose in the whey powder (5.0% w/v) was hydrolyzed in the presence of the ß-galactosidase activity of 280 U/g of lactose within 9 h while over 77.0% of lactose in the whey was hydrolyzed in the presence of ß-galactosidase activity of 280 U/g of lactose within 6 h. This was the first time to show that the ß-galactosidase produced by the psychrotolerant yeast could be used for hydrolysis of lactose in the whey powder and whey.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ascomicetos / Beta-Galactosidase / Lactose / Mutação Idioma: En Ano de publicação: 2012 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Ascomicetos / Beta-Galactosidase / Lactose / Mutação Idioma: En Ano de publicação: 2012 Tipo de documento: Article