Penicillium multicolor beta -D-galactosidase - a comparison with Aspergillus oryzae beta -D-galactosidase

Ebata, M.; Miyake, Y.; Narita, M.; Koizumi, K.; Tsuzuki, H.; Fujiwara, T.; Morihara, K.

Saishin Igaku 39(1): 192-201

1984


Accession: 001426298

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Abstract
Penicillium multicolor beta -D-galactosidase was studied with a view to using it to produce low-lactose milk. It gave a single band on polyacrylamide gel disc electrophoresis at pH 4 and pH 8. Slab electrophoresis on SDS-polyacrylamide gel indicated that it was composed of a single glycoprotein unit with mol. wt. about 135 000. Its isoelectric point was pH 5.7 vs. 4.8 for Aspergillus oryzae beta -D-galactosidase. The amino acid compositions and IR and UV absorbance spectra of the P. multicolor and A. oryzae enzymes were similar. The 2 enzymes differed slightly in their elution times on HPLC. Compared with the A. oryzae enzyme, the P. multicolor enzyme had the same pH optimum of 4.5 but a wider pH stability (2-9 vs. 4-9), a higher temp. optimum of 65 vs. 45 degrees C and greater heat stability (usable at up to 80 degrees C vs. 60 degrees C). The 2 enzymes were also immunologically different.