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Response surface methodology was used to enhance the production of α-galactosidase from  Fusarium moniliforme  NCIM 1099 in solid-state fermentation. Plackett–Burman design was employed for selection of critical media constituents which were optimized by central composite rotatable design. Wheat bran, peptone and FeSO 4 ·7H 2 O were identified as significant medium components using PB design. Further CCRD optimized medium components as wheat bran; 4.62 μg, peptone; 315.42 μg, FeSO 4 ·7H 2 O; 9.04 μg. RSM methodological optimization increased the enzyme production from 13.17 to 207.33 U/g showing 15.74-fold enhancement. The α-galactosidase was purified by 70% fractionation followed by DEAE anion exchange column chromatography which yields 23.33% with 28.68-fold purification. The molecular weight of α-galactosidase was 57 kDa which was determined by SDS-PAGE analysis. Purified enzyme has optimum pH of 4.0 and was found to be stable in wide pH range of 3.0–9.0. Its optimum temperature was 50 °C, whereas its activity remains above 50% up to 2 h at 75 °C. Hg 2+  was found to be a potent inhibitor and Mg 2+  acted as an activator of enzyme. No significant change was observed in enzyme activity for galactose concentration, ranging from 1 to 100 mM. The  K   m  values of enzyme for substrates  p -nitrophenyl-α- d -galactopyranoside, melibiose and raffinose were 0.20, 1.36, and 3.66 mM, respectively. Low  K   m  and stability to various physiological conditions of enzyme represents its potential which can be exploited in various industrial applications.   Electronic supplementary material  The online version of this article (doi:10.1007/s13205-016-0575-7) contains supplementary material, which is available to authorized users.

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Response surface methodology-based optimization of production media and purification of α-galactosidase in solid-state fermentation by Fusarium moniliforme NCIM 1099