2.3 Research on High-Efficient Anaerobic Fermentation Technology …
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Fig. 2.20 Relative number and distribution of bacterial (a) and archaeal (b) proteins in different
stages of the SHPT process, based on taxonomic bins for proteome-derived proteins with taxonomic
annotation. Distributions in c and d are at the level of classes within the phyla Proteobacteria and
Firmicutes, respectively. e Is at the level of the orders within the Euryarchaeota (Jia et al. 2017b)
of pyruvate dehydrogenase; (ii) dihydrolipoamide dehydrogenase; (iii) pyruvateferredoxin/flavodoxin oxidoreductase; (iv) formate C-acetyltransferase; and (v)
acetyl-CoA synthetase, as displayed in Fig. 2.22. The E1 component of pyruvate
dehydrogenase found in Stage II and involved in pyruvate metabolism, is able to
change pyruvic acid into acetyl-CoA and CO 2 and stems from Escherichia. The
dihydrolipoamide dehydrogenase appears in the decarboxylase pathway of pyruvic acid for biohydrogen production belonging to Pseudomonas and Zymomonas in
Stages II and III, separately. Pyruvate-ferredoxin/flavodoxin oxidoreductase which
is found in Pelosinus and Kluyvera bacteria in Stage I is a critical enzyme for the
equivilibrium regulation of NADH/NAD
+ in hydrogen production. These results
indicated that although these identified proteins belonged to disparate genera, they
probably can happen simultaneously with biogydrogen production together. This
pathway contains non-native hydrogenase linked with NAD(P) and H 2 generation
from NAD(P)H provided rapidly from glucose degradation via the pentose phosphate pathway. Formate C-acetyltransferase (pyruvate formate lyase, PFL) belongs
41
Fig. 2.20 Relative number and distribution of bacterial (a) and archaeal (b) proteins in different
stages of the SHPT process, based on taxonomic bins for proteome-derived proteins with taxonomic
annotation. Distributions in c and d are at the level of classes within the phyla Proteobacteria and
Firmicutes, respectively. e Is at the level of the orders within the Euryarchaeota (Jia et al. 2017b)
of pyruvate dehydrogenase; (ii) dihydrolipoamide dehydrogenase; (iii) pyruvateferredoxin/flavodoxin oxidoreductase; (iv) formate C-acetyltransferase; and (v)
acetyl-CoA synthetase, as displayed in Fig. 2.22. The E1 component of pyruvate
dehydrogenase found in Stage II and involved in pyruvate metabolism, is able to
change pyruvic acid into acetyl-CoA and CO 2 and stems from Escherichia. The
dihydrolipoamide dehydrogenase appears in the decarboxylase pathway of pyruvic acid for biohydrogen production belonging to Pseudomonas and Zymomonas in
Stages II and III, separately. Pyruvate-ferredoxin/flavodoxin oxidoreductase which
is found in Pelosinus and Kluyvera bacteria in Stage I is a critical enzyme for the
equivilibrium regulation of NADH/NAD
+ in hydrogen production. These results
indicated that although these identified proteins belonged to disparate genera, they
probably can happen simultaneously with biogydrogen production together. This
pathway contains non-native hydrogenase linked with NAD(P) and H 2 generation
from NAD(P)H provided rapidly from glucose degradation via the pentose phosphate pathway. Formate C-acetyltransferase (pyruvate formate lyase, PFL) belongs