Research progress of L-aspartate-α-decarboxylase and its isoenzyme in the β-alanine synthesis

World J Microbiol Biotechnol. 2022 Dec 14;39(2):42. doi: 10.1007/s11274-022-03483-2.

Abstract

Driven by the massive demand in recent years, the production of β-alanine has significantly progressed in chemical and biological ways. Although the chemical method is relatively mature compared to biological synthesis, its high cost of waste disposal and environmental pollution does not meet the environmental protection standard. Hence, the biological method has become more prevalent as a potential alternative to the chemical synthesis of β-alanine in recent years. As a result, the aspartate pathway from L-aspartate to β-alanine (the most significant rate-limiting step in the β-alanine synthesis) catalyzed by L-aspartate-α-decarboxylase (ADC) has become a research hotspot in recent years. Therefore, it is vital to comprehensively understand the different enzymes that possess a similar catalytic ability to ADC. This review will investigate the exploratory process of unique synthesis features and catalytic properties of ADC/ADC-like enzymes in particular creatures with similar catalytic capacity or high sequence homology. At the same time, we will discuss the different β-alanine production methods which can apply to future industrialization.

Keywords: Cysteine sulfinic acid decarboxylase; Enzymatic catalysis; L-Aspartate-α-decarboxylase; Whole-cell catalysis; β-Alanine.

Publication types

  • Review

MeSH terms

  • Aspartic Acid / metabolism
  • Glutamate Decarboxylase* / metabolism
  • Isoenzymes*
  • beta-Alanine

Substances

  • aspartate-alpha-decarboxylase
  • Isoenzymes
  • Glutamate Decarboxylase
  • Aspartic Acid
  • beta-Alanine