BioChem - DOS

Biochemical characterization of a novel thermophilic α-galactosidase from Talaromyces leycettanus JCM12802 with significant transglycosylation activity

Journal of bioscience and bioengineering

Wang, C.; Wang, H.; Ma, R.; Shi, P.; Niu, C.; Luo, H.; Yang, P.; Yao, B.

Thermophilic &alpha;-galactosidases have great potentials in biotechnological and medicinal applications due to their high-temperature activity and specific stability. In this study, a novel &alpha;-galactosidase gene of glycoside hydrolase family 27 (aga27A) was cloned from Talaromyces leycettanus JCM12802 and successfully expressed in Pichia pastoris GS115. Purified recombinant Aga27A (rAga27A) was thermophilic and thermotolerant, exhibiting the maximum activity at 70<SUP>o</SUP>C and retaining stability at 65<SUP>o</SUP>C. Like most fungal &alpha;-galactosidases, rAga27A had an acidic pH optimum (pH 4.0) but retained stability over a boarder pH range (pH 3.0-11.0) at 70<SUP>o</SUP>C. Moreover, the enzyme exhibited strong resistance to most metal ions and chemicals tested (except for Ag<SUP>+</SUP> and SDS) and great tolerance to galactose (19 mM). The preferable transglycosylation capacity of rAga27A with various substrates further widens its application spectrum. Thus rAga27A with excellent enzymatic properties will be ideal for applications in various industries, especially for the synthesis of galactooligosaccharides.

2016

Society for Bioscience and Bioengineering, Japan ; Distributed outside Japan by Elsevier Science

publisher-specific-oa

1389-1723

1347-4421

121

1

pp.7-12

10.1016/j.jbiosc.2015.04.023

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART74647441

http://manuscript.elsevier.com/S1389172315001978/pdf/S1389172315001978.pdf

Talaromyces leycettanus JCM12802; α-Galactosidase; Thermophilic; Transglycosylation; Galactose tolerance