A soluble, cytoplasmic decycling maltodextrinase with a relative molecular mass (M(r)) of around 62 000, and an isoelectric point (pI) of about 4 was purified to 93% homogeneity from a Lactobacillus species? strain 26X, that was isolated from the waste water of a kitchen and resembled Lactobacillus plantarum in its physiological and biochemical characteristics, but differed from this species in producing exclusively L(+)-lactic acid. The enzyme exhibited higher activities with maltotetraose to maltoheptaose than with cyclodextrins, in which cyclomaltohexaose was hydrolysed fastest, and the amounts of the linearized cyclic substrates were in the order cyclomaltohexaose < cyclomaltoheptaose

Keywords:ESCHERICHIA-COLI;NUCLEOTIDE-SEQUENCE;BACILLUS-SPHAERICUS;BETA-CYCLODEXTRIN;GENE;CYCLOMALTODEXTRINASE;ENZYME;AMYLOVORUS;EXPRESSION;CLONING