Information on EC 1.8.1.2 - assimilatory sulfite reductase (NADPH)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY
1.8.1.2
-
RECOMMENDED NAME
GeneOntology No.
assimilatory sulfite reductase (NADPH)
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+
show the reaction diagram
-
-
-
-
hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+
show the reaction diagram
electron flow sequence: NADPH-FAD-FMN
-
hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+
show the reaction diagram
ping-pong mechanism
-
hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+
show the reaction diagram
mechanism of electron transfer
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
additional information
-
sodium salts of thiosulfate and sulfate do not serve as the electron acceptor for reduced F420 oxidation by Fsr. Also, Fsr can not use NADH and NADPH for the reduction of sulfite.; the N-terminal half of Fsr represents a H2F420 dehydrogenase and the C-terminal half a dissimilatory-type siroheme sulfite reductase, and Fsr catalyzes the corresponding partial reactions
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
sulfate reduction I (assimilatory)
-
-
sulfate reduction III (assimilatory)
-
-
sulfate reduction
-
-
Sulfur metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen-sulfide:NADP+ oxidoreductase
An iron flavoprotein (FAD and FMN).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
coenzyme F420-dependent sulfite reductase
-
-
desulforubidin
-
-
-
-
H2S-NADP oxidoreductase
-
-
-
-
NADPH-dependent sulfite reductase
-
-
-
-
NADPH-sulfite reductase
-
-
-
-
NADPH-sulfite reductase
-
-
reductase, sulfite (reduced nicotinamide adenine dinucleotide phosphate)
-
-
-
-
SIR-FP
-
-
-
-
SIR-HP
-
-
-
-
SIRHP
-
-
-
-
sulfite reductase
-
-
sulfite reductase
-
-
sulfite reductase
-
-
sulfite reductase
-
-
sulfite reductase hemo-subunit
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-35-0
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
furfural inhibits sulfate assimilation by interfering with the reduction of sulfite by CysIJ
physiological function
-
furfural inhibits sulfate assimilation by interfering with the reduction of sulfite by CysIJ
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,1'-dimethyl-4,4'-bipyridinium dichloride + NADPH
NADPH + oxidized 1,1'-dimethyl-4,4'-bipyridinium dichloride
show the reaction diagram
-
i.e. paraquat, a herbicide
-
-
hydrogen sulfide + 3 NADP+ + 3 H2O
sulfite + 3 NADPH + 3 H+
show the reaction diagram
-
-
-
?
hydrogen sulfide + NADP+ + H2O
sulfite + NADPH + H+
show the reaction diagram
-
-
-
?
hydroxylamine + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
-
hydroxylamine + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
hydroxylamine + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
hydroxylamine + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
-
hydroxylamine + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
-
NADP+ + reduced methyl viologen
NADPH + oxidized methyl viologen
show the reaction diagram
-
-
-
-
NADP+ + reduced methyl viologen
NADPH + oxidized methyl viologen
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
-
-
?
nitrite + NADPH
ammonia + NADP+
show the reaction diagram
-
NADPH can be replaced by reduced methyl viologen, the latter reaction is catalyzed by hemoprotein subunit alone
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
ir
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
reduction of sulfite by reduced methyl viologen is catalyzed by hemoprotein subunit alone
-
-
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
NADPH can be replaced by reduced methyl viologen
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
NADPH can be replaced by reduced methyl viologen
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
NADPH can be replaced by reduced methyl viologen, benzyl viologen
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
sole compound reduced
-
-
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
ir
sulfite + NADPH
hydrogen sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
?
sulfite + NADPH + H+
sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
?
sulfite + NADPH + H+
sulfide + NADP+ + H2O
show the reaction diagram
-
no physiological nitrite reductase
-
?
sulfite + reduced F420
sulfide + oxidized F420
show the reaction diagram
-
-
-
?
hydroxylamine + NADPH
ammonia + NADP+
show the reaction diagram
-
NADPH can be replaced by reduced methyl viologen
-
?
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
-
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
-
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
-
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
-
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
-
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
-
additional information
?
-
-
reactions of FMN depleted enzyme
-
-
-
additional information
?
-
-
overview on assay methods
-
-
-
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
-
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
-
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
-
additional information
?
-
-
by production of the population synchronizer H2S involved in ultradian metabolic oscillation
-
-
-
additional information
?
-
-
can generate tyrosil radicals e.g. for transfer of electrons to the iron center of metR2, small subunit of ribonucletide reductase
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
hydrogen sulfide + 3 NADP+ + 3 H2O
sulfite + 3 NADPH + 3 H+
show the reaction diagram
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
ir
sulfite + NADPH + H+
sulfide + NADP+ + H2O
show the reaction diagram
-
-
-
?
sulfite + NADPH + H+
sulfide + NADP+ + H2O
show the reaction diagram
-
no physiological nitrite reductase
-
?
hydrogen sulfide + NADP+ + H2O
sulfite + NADPH + H+
show the reaction diagram
-
-
-
?
additional information
?
-
-
by production of the population synchronizer H2S involved in ultradian metabolic oscillation
-
-
-
additional information
?
-
-
can generate tyrosil radicals e.g. for transfer of electrons to the iron center of metR2, small subunit of ribonucletide reductase
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
-
2 FAD and 2 FMN per mol of enzyme
flavin
-
treatment with p-chloromercuriphenylsulfonate causes dissociation of FMN but retetion of FAD and heme
flavin
-
treatment with ammonium sulfate causes dissociation of FMN but retetion of FAD and heme
heme
-
siroheme
heme
-
hemoprotein subunit contains one siroheme and one Fe4S4 center per polypeptide
heme
-
tetrahydroporphyrin of isobacteriochlorin type with eight carboxylic side chains
heme
-
2 fully metallated sirohemes per mol of enzyme, S=9/2 EPR iron-sulfur cluster
iron-sulfur centre
-
-
iron-sulfur centre
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron-sulfur cluster
-
4Fe-4S, 4 mol per tetramer of hemoprotein subunit, bound to hemoprotein subunit
Iron-sulfur cluster
-
hemoprotein subunit contains one siroheme and one Fe4S4 center per polypeptide, heme is in high spin Fe3+ state
Iron-sulfur cluster
-
S=9/2 EPR iron-sulfur cluster
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2'-AMP
-
NADPH-sulfite reductase and NADPH-cytochrome c reductase
8-hydroxyquinoline
-
-
Ca2+
-
strong inhibition
CN-
-
severe inhibition of NADPH-sulfite,-nitrite,-hydroxylamine reductase, no inhibition of methyl viologen-sulfite reductase, small extent of inhibition of NADPH dependent reduction of cytochrome c, ferricyanide, quinones etc.
CN-
-
only when added with NADPH prior to substrate, sulfite prevents NADPH-reduced form from irreversible conversion by CN-; severe inhibition of NADPH-sulfite,-nitrite,-hydroxylamine reductase, no inhibition of methyl viologen-sulfite reductase, small extent of inhibition of NADPH dependent reduction of cytochrome c, ferricyanide, quinones etc.
CO
-
binding to siroheme
Co2+
-
strong inhibition
Cu2+
-
strong inhibition
Fe2+
-
strong inhibition
Fe3+
-
strong inhibition
Hg2+
-
strong inhibition
iodoacetic acid
-
-
iodonium diphenyl chloride
-
acts on NADPH- and FAD-binding domain of flavoprotein component
KCN
-
complete inhibition at 1 mM
Low ionic strength
-
NADPH-dependent activities
-
NADP+
-
competitive to NADPH, noncompetitive to sulfite
NADP+
-
NADPH-dependent activities
NADP+
-
NADPH-dependent activities
o-phenanthroline
-
-
p-chloromercuribenzoate
-
NADPH-dependent activities
p-Mercuriphenylsulfonate
-
-
p-Mercuriphenylsulfonate
-
NADPH-dependent reactions
PCMB
-
complete inhibition at 1 mM
sulfate
-
-
Sulfide
-
reduction of sulfite, nitrite, hydroxylamine by reduced methyl viologen
Sulfide
-
reduction of sulfite, nitrite, hydroxylamine by reduced methyl viologen
additional information
-
inhibitory potency of metal ions, overview, no inhibition by Na+, K+, and Mg2+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06
cytochrome c
-
-
4.5 - 10.5
hydroxylamine
-
-
4.5 - 10.5
hydroxylamine
-
-
0.005
NADPH
-
-
0.018
NADPH
-
-
0.018
NADPH
-
reduction of cytochrome c
0.021
NADPH
-
reduction of sulfite
0.08
NADPH
-
-
0.8 - 1.5
nitrite
-
-
0.8 - 1.5
nitrite
-
-
0.07
paraquat
-
-
0.021
reduced F420
-
at a fixed sulfite concentration of 0.29 mM and within a reduced F420 concentration range of 0.004-0.06 mM
0.0043 - 0.0074
sulfite
-
-
0.012 - 0.017
sulfite
-
-
0.012 - 0.017
sulfite
-
-
0.0122
sulfite
-
within a sulfite concentration range of 0.0014-0.3 mM and with a fixed reduced F420 concentration of 0.04 mM
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
150
FAD
Escherichia coli
-
cosubstrate NADPH
605
NADP+
Escherichia coli
-
-
1.25
NADPH
Escherichia coli
-
cosubstrate O2
158
NADPH
Escherichia coli
-
cosubstrate 3-acetylpyridineadenine dinucleotide phosphate
172
NADPH
Escherichia coli
-
cosubstrate FMN
318
NADPH
Escherichia coli
-
cosubstrate cytochrome c
462
NADPH
Escherichia coli
-
cosubstrate dichlorphenolindophenol
468
NADPH
Escherichia coli
-
cosubstrate ferricyanide
43.3 - 51.7
nitrite
Escherichia coli
-
cosubstrate NADPH
605
reduced methyl viologen
Escherichia coli
-
-
30 - 40
sulfite
Escherichia coli
-
cosubstrate NADPH
65
sulfite
Escherichia coli
-
cosubstrate reduced methyl viologen
98.3 - 217
hydroxylamine
Escherichia coli
-
cosubstrate NADPH
additional information
additional information
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
-
values for reactions catalyzed by holoenzyme, hemoprotein subunit alone, and flavoprotein subunit alone with various electron acceptors
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08 - 0.12
arsenite
-
-
0.006 - 0.009
cyanide
-
-
0.018
iodonium diphenyl chloride
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0013
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced F420, and 1.5 mM sodium sulfite, from cell extract
0.0182
-
in 50 mM potassium phosphate buffer (pH 7), 0.044 mM reduced F420, and 1.5 mM sodium sulfite, after 14fold purification
2.73 - 2.87
-
-
10.02
-
purified enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 7.5
-
NADPH-sulfite reductase
7.2
-
electron donor NADPH
7.5 - 7.9
-
NADPH-cytochrome c reductase
7.7 - 8.5
-
methyl viologen-sulfite reductase
7.9
-
sulfite
8.6
-
nitrite
9.5
-
hydroxylamine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
75% activity at pH 6.5 and pH 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
-
determined by SDS-PAGE
696893
70000
-
SDS-PAGE
674504
119000
-
gel filtration
656421
200000 - 208000
-
gel filtration
392979
300000
-
gel filtration, sedimentation analysis at low ionic strength, dissociated
392956
350000
-
calculation from FAD and FMN content, sedimentation coefficient
392969, 392971
350000
-
gel filtration
674504
488000
-
sedimentation under nondenaturing conditions
392952
604000
-
gel filtration
392957
650000
-
gel filtration, sedimentation analysis
392956
670000
-
sedimentation equilibrium centrifugation, sedimentation and diffusion coefficients
392967
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 60000, determined by SDS-PAGE
dodecamer
-
alpha8,beta4, 8 * 58000-60000 + 4 * 54000-57000, sedimentation under denaturing conditions
dodecamer
-
alpha8,beta4, 8 * 58000-60000 + 4 * 54000-57000, sedimentation under denaturing conditions; SDS-PAGE
dodecamer
-
SDS-PAGE
heterotetramer
-
two alpha- and two beta-subunits, encoded by the MET10 and MET5 gene, respectively
tetramer
-
alpha2,beta2, 2 * 116000 + 2 * 167000, SDS-PAGE
hexamer
-
alpha2,beta2,gamma2, 2 * 50000 + 2 * 42000 + 2 * 12500, SDS-PAGE
additional information
-
dissociation of enzyme by 5 m urea into flavoprotein octamer and hemoprotein monomers
additional information
-
alpha chain is composed of 2 distinct domains, one binding FAD and the other binding FMN, the FMN binding domains cooperate for a head-to-head subunit interaction
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
FNR-like domain of flavoprotein
-
hemoprotein subunit
-
hemoprotein subunit; x-ray structure of hemoprotein subunit
-
recombinant monomeric fragment of flavoprotein, having 3 domains and binding FAD and NADPH
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
-
75% activity at pH 6.5 and pH 8.0 after 30 min at 25C
656421
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
inactivation above
392974
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
low ionic strength such as 0.01 M phosphate buffer destroys NADPH-dependent activities
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acetone
-
inactivation
Ethanol
-
inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 0.05 M potassium phosphate buffer pH 7.7, 0.1 mM EDTA, 2 years stable
-
-15C, 0.05 M potassium phosphate buffer pH 7.7, 10 mM EDTA, at least 6 months
-
-15C, reduced hemoprotein subunit or reduced flavoprotein subunit
-
4C, 0.05 M potassium phosphate buffer pH 7.7, 0.1 mM EDTA, 1 month stable
-
-20C, 0.3 M phosphate buffer pH 7.3, 1 year stable stable
-
4C, 0.3 M phosphate buffer pH 7.3, 1 week stable
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using a His-Trap column
-
579.5fold to homogeneity by ammoniums sulfate fractionation, DEAE ion exchange chromatography, and gel filtration
-
preparation of FMN depleted enzyme
-
phenyl-Sepharose chromatography, F420-Sepharose chromatography and QAE-Sephadex gel filtration
-
preparation of mutant form lacking FAD and hence with no NADPH-sulfite reductase activity but with methyl viologen-sulfite reductase activity
-
var. ellipsoideus (partial)
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the sulfite reductase hemo-subunit is cloned into the vector pLM1 for expression in Escherichia coli BL21DE3 cells
-
homology to cysI of Escherichia coli, i.e. alpha subunit
-
alpha and beta subunits
-
FMN-binding domain of flavoprotein component
-
NADPH- and FAD-binding domain of flavoprotein component
-
the MET5 and Met10 coding sequences are cloned into the vector pGEM-T-easy and subsequently into the centromeric Saccharomyces cerevisiae expression plasmid pRS416
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C427A
-
mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C433A
-
mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C472A
-
mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
C476A
-
mutation of the highly conserved cysteine 427, crucial residue for iron-sulfur cluster binding
A979T
-
Met5p mutant
E1356K
-
Met5p mutant
E929K
-
Met10p mutant
G1115D
-
Met5p mutant
T990I
-
Met10p mutant
T997I
-
Met10p mutant
W59X
-
Met10p mutant
W841X
-
Met10p mutant
L606F
-
Met10p mutant
additional information
-
4 mutants blocked in sulfite reduction, 3 containing only FMN, 1 lacking both flavins
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mixing isolated hemoprotein and flavoprotein in appropriate proportions reconstituts activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
potential use of vaccine against Actinobacillus pleuropneumoniae infections
nutrition
-
quality determination of surimi, purified enzyme increases the reactive SH and gel strength of surimi prepared from frozen mackerel, processing of surimi-based products
brewing
-
mutations in the sulfite reductase genes, MET5 and MET10, are responsible for low H2S phenotypes, yeast strains with reduced H2S production offer promising solutions to H2S-related taints generated during wine production