Purification and Properties of a Novel sp . R 48 Enzyme , Trehalose Synthase , from Pimelobacter

transglucosy]ation. The enzyme also converted trehatose into ma]tose but was inactive on o-ther saccharides. The N-termina] amino acid of the enzyme was serine. The optimum pH and temperature were pH 7.5 and 200C, respective]y, The enzyme was stab]e in the range of pH 6,O-9.0 and up to 30eC for 60 min. The rate of conyeTsion of maltose ;nto trehalose was independent of the mattose concentration. The maximum yietd of L'.e,hl.:OhSiebif:ti'MbyMca.tt,OS,r HWge:e, ,8k',/IX.': z80.',9.`{',..a:dTl 6,:7`Zi at 5. 15, and 250C, respectively. The hctivity