Regulation by amino acids of α-amylase and endo-β(1→4)-glucanase induction in mycelial culture of the mushroom Termitomyces clypeatus

Termitomyces clypeatus constitutively liberated amyloglucosidase; the liberation was not repressed by glucose. Growth of the mushroom in synthetic medium was slow with starch, and only amyloglucosidase was liberated. Yeast extract stimulated growth and enzyme production in starch medium, and α-amylase along with amyloglucosidase was detected extracellularly. The mushroom could not utilise cellulose or liberate endo-β(1 → 4)-glucanase even when inducer cellobiose or glucose was added to cellulose at different concentrations. Cellobiose alone also failed to induce any extracellular endo-β(1 → 4)-glucanase production. Yeast extract in both cellulose and cellobiose media supported liberation of endo-β(1 → 4)-glucanase. Lactose was found to be a poor inducer even in yeast extract medium. However, both α-amylase and endo-β(1 → 4)-glucanase were detected intracellularly at a basal level even when the enzymes were absent extracellularly under inducing and noninducing conditions. The intracellular enzymes were only freely liberated into the medium in the presence of yeast extract. It appeared that induction of α-amylase and endo-β(1 → 4)-glucanase was largely inhibited by the restricted liberation of the enzymes in absence of yeast extract. Of the yeast extract components, amino acids were the active ingredient mimicking the role of yeast extract in induction. Yeast extract was found to relieve catabolic inhibition observed at the late phase of enzyme production. It is proposed that catabolic inhibition might have a role in the enzyme liberation and that amino acids supported extracellular enzyme production by relieving this inhibition. Key words: mushroom, Termitomyces clypeatus, catabolic inhibition, polysaccharidase induction, amino acid.