Two enzymes, named E-1 and E-2, were purified from the culture supernatant of a β-glucanase (1, 3;1, 4-β-D-glucan 4-glucanohydrolase; EC 3.2.1.73) hyperproducing strain, Bacillus subtilis HL-25. Both purified enzymes were found to be homogeneous on SDS-polyacrylamide gel electrophones!s and to have an identical molecular weight of 24, 000. E-1 and E-2 have similar amino acid compositions, but their isoelectric points are pH 8.55 and 8.75, respectively. N-Terminal amino acid analyses showed that the N-terminal amino acid of E-2 is glutamine, which might be converted to pyroglutamic acid through spontaneous cyclization to yield E-1. Comparison of the amino acid sequence with that determined on DNA sequence analysis indicated that β-glucanase was produced as a precursor composed of 242 amino acid residues, including a signal peptide part consisting of 28 amino acids.
Detailed investigation of the crude enzyme preparation from the host strain, B. subtilis Y-25, also indicated the presence of two enzymes.

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