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Enzymatic Hydrolysis of α- and β-Oligo(L-aspartic acid)s by Poly(aspartic acid) Hydrolases-1 and 2 from Sphingomonas sp. KT-1

  1. Tomohiro Hiraishi1,*,
  2. Mariko Kajiyama1,2,
  3. Ichiro Yamato2,
  4. Yoshiharu Doi1,3

Article first published online: 23 MAR 2004

DOI: 10.1002/mabi.200300085

Issue

Macromolecular Bioscience

Macromolecular Bioscience

Special Issue: Highlights from the First IUPAC International Conference on Bio-based Polymers (ICBP 2003) in Saitama, Japan

Volume 4, Issue 3, pages 330–339, March 15, 2004

Additional Information

How to Cite

Hiraishi, T., Kajiyama, M., Yamato, I. and Doi, Y. (2004), Enzymatic Hydrolysis of α- and β-Oligo(L-aspartic acid)s by Poly(aspartic acid) Hydrolases-1 and 2 from Sphingomonas sp. KT-1. Macromol. Biosci., 4: 330–339. doi: 10.1002/mabi.200300085

Author Information

  1. 1

    Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan

  2. 2

    Department of Biological Science and Technology, Science University of Tokyo, 2641 Yamazaki, Noda, Chiba 278-8510, Japan

  3. 3

    Department of Innovative and Engineered Materials, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, Kanagawa 226-8502, Japan

*Polymer Chemistry Laboratory, RIKEN Institute, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan. Fax: +81-48(462)4667

Publication History

  1. Issue published online: 23 MAR 2004
  2. Article first published online: 23 MAR 2004
  3. Manuscript Accepted: 7 JAN 2004
  4. Manuscript Revised: 29 DEC 2003
  5. Manuscript Received: 4 NOV 2003

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Keywords:

  • degradation;
  • enzymes;
  • oligomers;
  • polyamides;
  • water-soluble polymers

Abstract

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Summary: The enzymatic hydrolysis of α- and β-oligo(L-aspartic acid)s by PAA hydrolase-1 and PAA hydrolase-2 (purified from Sphingomonas sp. KT-1) was performed to elucidate the mechanism of the microbial degradation by Sphingomonas sp. KT-1 of the thermally synthesized α,β-poly(D,L-aspartic acid) (tPAA). GPC analysis of the hydrolyzed products of α- and β-tetra(L-aspartic acid)s by PAA hydrolase-1 has showed that PAA hydrolase-1 is capable of hydrolyzing only the specific amide bonds between β-aspartic acid units. The RP-HPLC analysis of the enzymatic hydrolysis of β-oligo(L-aspartic acid)s (4 and 5 mers) by PAA hydrolase-1 has suggested that the enzymatic hydrolysis of β-oligo(L-aspartic acid)s occurs via an endo-mode cleavage. In contrast, PAA hydrolase-2 hydrolyzed both α- and β-oligo(L-aspartic acid)s via an exo-mode cleavage to yield L-aspartic acid as a final product. A kinetic study on the enzymatic hydrolysis of α-oligo(L-aspartic acid)s (3 to 7 mers) by PAA hydrolase-2 has indicated that Km values are almost independent of the number of monomer units in oligomers of 4 to 7 mers, while that Vmax values are markedly dependent on the chain length and show a maximum value at 5 mer.

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