ISSN:
1432-0614
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Abstract New thermostable enzyme activities of seven Thermus strains were compared using the API ZYM system. All the strains exhibited high levels of α- and β-glycosidases, esterase (C4) and esterase-lipase (C8) activities intracellularly. Only T. thermophilus HB8 (ATCC 27634) showed α-glucosidase and esterase activities in the supernatant. According to the intensity of β-galactosidase activity, Thermus strains were divided in three groups. Group 0, which showed a weak β-galactosidase activity, included Thermus spp. ATCC 31674 (T351) and 27978 (X-1) as well as T. thermophilus ATCC 27634 (HB8). Group I which consisted of T. aquaticus ATCC 25104 (YT-1), ATCC 25105 (Y-VII-51B) and Thermus sp. ATCC 27737 (T2), had a specific activity of approximately 40.0 U mg-1 and galactose as inducer. T. aquaticus ATCC 31558 (group 2) was particularly effective for β-galactosidase production (2840 U) with a specific activity of 98 U mg-1. For each strain, galactose (0.5%) was a better inducer of β-galactosidase production than lactose (1%). The detection of β-galactosidase activity was dependent on the derivative chromogenic substrates used (naphthyl or nitrophenol coupled to sugar). Oligosaccharides were synthesized from cellobiose, lactulose, maltose or lactose as substrates at high temperature in some strains of Thermus.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s002530050523
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