Abstract
In order to improve the production of acarbose, the fermentation medium of acarbose-producing strain Actinoplanes sp. A56 was optimized in this paper. Firstly, fractional factorial design was employed to investigate the influences of glucose, maltose, corn steep liquor, soy bean flour and monosodium glutamate on acarbose production, and the results revealed that maltose and corn steep liquor had significant and positive effects. Then, the two significant factors used the method of the steepest ascent to reach the yield plateau of acarbose. To explore the best condition obtained by the steepest method, the concentrations of maltose and corn steep liquor were further optimized with central composite design and response surface analysis. As a result, the acarbose production was increased from 837 to 1043 mg/L by using this optimization strategy. Key words: Acarbose production, medium optimization, Actinoplanes sp. A56, response surface methodology.
Highlights
Acarbose is a pseudo-oligosaccharide, which acts as a competitive -glucosidase inhibitor
1.4 mono-factor experiments, the following five components of the fermentation medium were optimized for further enhancing acarbose production by Actinoplanes sp
From the results of regression analysis, it is obvious that the significant terms were X2 and corn steep liquor (X3)
Summary
Acarbose is a pseudo-oligosaccharide, which acts as a competitive -glucosidase inhibitor. Because it is hardly digestible and generally have no detectable toxicity (Wehmeier and Piepersberg, 2004), acarbose has widely been used in the therapy of type II diabetes (non-insulindependent), which could better control blood sugar contents of patients after meals (Hanefeld et al, 2008; Kihara et al, 1997; Hanefeld, 2007). 1996; Drepper et al, 1996; Goeke et al, 1996). Acarbose consists of the moieties of acarviose and maltose. Acarviose is the core unit of acarbose, which is mainly responsible for inhibition of - glucosidase. The linkage between acarviose and maltose in acarbose is established by an acarviosyl transferase (Hemker et al., 2001)
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