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. 1992 Aug;58(8):2474–2478. doi: 10.1128/aem.58.8.2474-2478.1992

Two types of bacterial alginate lyases.

M Kitamikado 1, C H Tseng 1, K Yamaguchi 1, T Nakamura 1
PMCID: PMC195806  PMID: 1514793

Abstract

The extracellular alginate lyases were purified from Vibrio harveyi AL-128 and V. alginolyticus ATCC 17749. The former enzyme appears to be specific for alpha-1,4 bonds involving L-guluronate units in alginate, whereas the latter exhibits specificity for beta-1,4 bonds involving D-mannuronate units. The molecular weights of the enzymes were estimated to be 57,000 and 47,000, and they had isoelectric points of 4.3 and 4.6, respectively. The enzyme from strain AL-128 was most active at NaCl concentrations of 0.3 to 1.0 M. Optimum activity of the enzyme from strain ATCC 17749 was found in the presence of 5 to 10 mM CaCl2.

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Selected References

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