Generally, plant specialized metabolism is characterized by gene duplication events and gene diversifications leading to modified/optimized product specificity and modified tissue specific expression [ 75].
Thus, CGTases most likely evolved from a common ancestor to diversify in product specificity by acquisition of specific mutations at the substrate binding sites.
This is consistent with a structural biological analysis that correlates specific amino acid replacements with specific changes in the substrate and product specificity of the protein [ 57].
High product specificity, low costs of substrates, low production temperature and low energy consumption are all advantages of the biotechnological methods for lactic acid production over the chemical methods [3], [5].
Target specific primers were initially tested for product specificity by PCR using genomic DNA as a template.
These identified specific amino acid replacements that were associated with changing substrate and product specificity during the time of presumed adaptive change.
The factors affecting the product specificity are also discussed in the paper.
All the parameters involved have been shown to affect the product specificity of the mutant H43T CGTase transglycosylation mechanism.
They include: low product specificity, need for high pressure and/or temperature, and inability to use crude glycerol with high levels of contaminants (Yazdani and Gonzalez, 2007).
Whereas this can in part be attributed to product specificity, other experimental and cellular factors are likely important contributors to these conflicting results.
