PMID: 2121480Oct 5, 1990Paper

Purification and characterization of an exo-1,4-beta-galactanase from a strain of Bacillus subtilis

European Journal of Biochemistry
H NakanoY Watanabe

Abstract

An arabinogalactan 4-beta-D-galactanohydrolase was purified to a homogeneous state from the culture filtrate of a strain of Bacillus subtilis. The enzyme have a molecular mass of 36 kDa and an isoelectric point of pH 7.9. The enzyme is most active at around pH 6.5-7 and at 60 degrees C, and is stable between pH 6-10 and below 55 degrees C. Hg2+ and Cu2+ inhibit the activity. The enzyme hydrolyze soybean arabinogalactan which contains beta-1,4-galactosidic linkages in its main chain structure, but not other polysaccharides with beta-1,3-galactosidic linkages. The hydrolysis products from soybean arabinogalactan are predominantly galactobiose with a small amount of galactotetraose. The enzyme is an exo-enzyme and the ability to transfer galactobiose to other galactobiose molecules is indicated by the formation of galactotetraose.

Citations

May 15, 2013·Applied Microbiology and Biotechnology·Tatsuji Sakamoto, Megumi Ishimaru
Dec 1, 1995·International Journal of Biological Macromolecules·E BonninJ F Thibault
Jun 27, 2001·Applied and Environmental Microbiology·T Sakamoto, J F Thibault
Sep 10, 2005·Applied and Environmental Microbiology·Sandra W A HinzAlphons G J Voragen
Nov 26, 2013·Applied Microbiology and Biotechnology·Estelle BonninMarie-Christine Ralet
Mar 8, 2011·Microbial Biotechnology·Mary O'Connell MotherwayDouwe van Sinderen

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