Production and some properties of invertase isozymes of Fusarium oxysporum.
- 1 January 1979
- journal article
- research article
- Published by Microbiology Research Foundation in The Journal of General and Applied Microbiology
- Vol. 25 (6) , 361-366
- https://doi.org/10.2323/jgam.25.361
Abstract
Two forms of invertase, isolated from F. oxysporum, were designated P-1 and P-2 enzymes according to their respective elution profiles on DEAE-cellulose column. P-1 was produced mainly at an early stage in the cell culture; P-2 was produced at a late stage and its production agreed with the appearance of microconidia. Mycelia separated from microconidia contained only P-1. Optimum pH, substrate specificity and transferase activity of P-1 enzyme were somewhat different from those of P-2 enzyme. Invertase (M) secreted into the medium at a late stage in the culture showed similar properties to P-2 enzyme. All 3 enzymes contained carbohydrates and showed .beta.-fructofuranosidase activity. P-1 and P-2 enzymes were both inhibited by Ca2+, Zn2+ and Cu2+ but not by Ni2+ and Co2+.This publication has 2 references indexed in Scilit:
- Surface localization of enzymes in mycelia and microconidia of Fusarium oxysporum.The Journal of General and Applied Microbiology, 1979
- The carbohydrates of the Jerusalem artichoke and other CompositaeBiochemical Journal, 1950