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Published on: September 23, 2021
Citrate Metabolism by Pediococcus halophilus
1Soy Sauce Research Laboratories, Kikkoman Corporation, Noda-shi, Chiba-ken 278, Japan.
Abstract:
Several strains of non-citrate-metabolizing Pediococcus halophilus have previously been isolated from soy sauce mash or moromi. The factors controlling the metabolism of citrate in soy pediococci were studied. All the soy pediococcal strains tested which failed to decompose citrate did not possess citrate lyase [citrate (pro-3S)-lyase; EC 4.1.3.6] activity. In P. halophilus, citrate lyase was an inducible enzyme, and the optimum pH for activity was 7.0. The metabolism of citrate in P. halophilus was different from that observed in lactic streptococci. The main products from citrate were acetate and formate, and this bacterium produced no acetoin or diacetyl. Formate production from citrate was greatly reduced in the presence of glucose. P. halophilus 7117 (Cit) was proved to contain citrate lyase, pyruvate formate-lyase (EC 2.3.1.54) phosphotransacetylase (phosphate acetyltransferase; EC 2.3.1.8), and acetate kinase (EC 2.7.2.1), i.e., all the enzymes necessary to convert citrate to acetate and formate.
Insights
Soy pediococci that cannot metabolize citrate lack citrate lyase activity. Pediococcus halophilus utilizes citrate lyase to produce acetate and formate, with glucose reducing formate production.
Area of Science:
- Microbiology
- Food Science
- Biochemistry
Background:
- Soy sauce fermentation involves Pediococcus halophilus.
- Some strains of P. halophilus do not metabolize citrate.
- Citrate metabolism in these bacteria is not fully understood.
Purpose of the Study:
- Investigate factors controlling citrate metabolism in soy pediococci.
- Characterize the enzyme responsible for citrate decomposition.
- Elucidate the metabolic pathway of citrate in P. halophilus.
Main Methods:
- Enzyme assays for citrate lyase activity.
- pH optima determination for citrate lyase.
- Analysis of metabolic products from citrate using P. halophilus 7117 (Cit).
Main Results:
- Non-citrate-metabolizing strains lacked citrate lyase activity.
- Citrate lyase in P. halophilus is an inducible enzyme with optimal activity at pH 7.0.
- P. halophilus converts citrate to acetate and formate, lacking acetoin/diacetyl production; glucose inhibits formate production.
Conclusions:
- Citrate lyase is essential for citrate decomposition in P. halophilus.
- The citrate metabolism pathway in P. halophilus differs from lactic streptococci.
- P. halophilus 7117 (Cit) possesses all necessary enzymes for converting citrate to acetate and formate.
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