Information on EC 5.4.99.11 - Isomaltulose synthase

Word Map on EC 5.4.99.11
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.4.99.11
-
RECOMMENDED NAME
GeneOntology No.
Isomaltulose synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Sucrose = 6-O-alpha-D-glucopyranosyl-D-fructofuranose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
SYSTEMATIC NAME
IUBMB Comments
Sucrose glucosylmutase
The enzyme simultaneously produces isomaltulose (6-O-alpha-D-glucopyranosyl-D-fructose) and smaller amounts of trehalulose (1-O-alpha-D-glucopyranosyl-beta-D-fructose) from sucrose.
CAS REGISTRY NUMBER
COMMENTARY hide
159940-49-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Bemisia argentifolia
-
-
-
Manually annotated by BRENDA team
strain FMB1
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain NK33-98-8
-
-
Manually annotated by BRENDA team
strain NK33-98-8
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain CBS 574.77
-
-
Manually annotated by BRENDA team
Z12
-
-
Manually annotated by BRENDA team
strain UQ14S
Swissprot
Manually annotated by BRENDA team
strain UQ14S
Swissprot
Manually annotated by BRENDA team
gene smuA
UniProt
Manually annotated by BRENDA team
i.e. Protaminobacter rubrum CBS 574.77, gene smuA
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
saccharose
isomaltulose
show the reaction diagram
-
-
-
-
-
Sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
show the reaction diagram
sucrose
6-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
show the reaction diagram
sucrose
alpha-D-glucopyranosyl-1,1-D-fructofuranose
show the reaction diagram
sucrose
alpha-D-glucopyranosyl-1,6-D-fructofuranose + alpha-D-glucopyranosyl-1,1-D-fructofuranose
show the reaction diagram
sucrose
alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
show the reaction diagram
-
-
-
?
sucrose
isomaltulose
show the reaction diagram
sucrose
isomaltulose + trehalulose
show the reaction diagram
sucrose
isomaltulose + trehalulose + D-glucose
show the reaction diagram
sucrose
palatinose
show the reaction diagram
-
-
-
-
-
sucrose
palatinose + trehalulose + D-glucose + D-fructose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Sucrose
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
show the reaction diagram
sucrose
6-O-alpha-D-glucopyranosyl-D-fructofuranose + alpha-D-glucosylpyranosyl-1,6-D-fructofuranose
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
115% relative activity at 5 mM
EDTA
119% relative activity at 5 mM
Fe2+
126% relative activity at 5 mM
additional information
-
Mg2+ and Zn2+ show no significant influence on enzyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
-
castanospermine
-
competitive, crystal structure in complex with enzyme
Co2+
-
20-30% inhibition at 1 mM
Cu2+
-
20-30% inhibition at 1 mM
CuSO3
-
14% inhibition at 1 mM, 23% inhibition at 5 mM
deoxynojirimycin
FeCl2
-
25% inhibition at 1 mM, 51% inhibition at 5 mM
glucono-1,5-lactone
-
-
Glutaraldehyde
SDS
-
3 mM, complete inactivation
sodium dodecylsulfate
-
1 mM, complete inhibition
Tris(hydroxymethyl)aminomethane
additional information
-
not inhibitory: acarbose
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Sucrose
-
the production of isomaltulose with alginate-immobilized Protaminobacter rubrum at 30 C is influenced by sucrose concentration. Isomaltulose yields above 90% in 8 h are reached in 40-65% sucrose solutions, and yields up to 82% in 24 h were obtained with 70% sucrose. At higher concentrations (75%) a significant decrease in the isomaltulose yield (42.7-55%) is observed
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43 - 240
D-glucose
30 - 500
isomaltulose
0.0192 - 257
Sucrose
30 - 185
Trehalulose
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
15 - 44
D-glucose
1.7 - 1947
isomaltulose
0.2 - 10430
Sucrose
11.5 - 1144
Trehalulose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.76
D-glucose
35
0.042 - 8.6
isomaltulose
5690
1.4
Sucrose
Serratia plymuthica
D0VX20
pH 7.0, 30C, recombinant wild-type enzyme
55
0.15 - 36
Trehalulose
4573
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
castanospermine
-
-
0.01 - 0.04
deoxynojirimycin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0072
pH 7.0, 30C, purified recombinant mutant F297A+P
0.046
pH 7.0, 30C, purified recombinant mutant F297A
0.14
pH 7.0, 30C, purified recombinant mutant R333K
1.1
pH 7.0, 30C, purified recombinant wild-type enzyme
2
-
crude extract, in 25 mM PBS (pH 5.8), at 30C
2.16
-
crude enzyme, pH 6.3, 33C
38.75
-
purified native enzyme, pH 6.3, 33C
65.3
-
sucrose
181
Bemisia argentifolia
-
sucrose
280
-
sucrose
427.1
-
after 213.6fold purification, in 25 mM PBS (pH 5.8), at 30C
500
-
pH 5.5, 25C
562
pH 6.0, 30C
2362
-
pH 6.0, 30C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
the activity diminishes significantly at a pH above 9.0 or below 5.0, and completely inactivates at pH 10.0
4 - 9
-
89%, 86%, 80%, 34%, and 30% of maximum activity at pH 4.0, pH 6.0, pH 7.0, pH 8.0, and pH 9.0
4.2 - 7.8
-
pH 4.2: about 30% of maximal activity, pH 7.8: about 50% of maximal activity
5
-
80% residual activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 35
additional information
-
the ratio of trehalulose to isomaltulose increases at lower temperatures. The optimum for trehalulose production is 20C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
20 - 60
-
20C: about 50% of maximal activity, 40C: about 40% of maximal activity
35 - 60
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface shows higher activity than the enzyme expressed in Escherichia coli strain DH10B
50
-
25% residual activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.9
-
calculated
5.96
sequence calculation
7
mature gene product, calculated
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63000
-
x * 63000, SDS-PAGE
63750
MALDI-TOF mass spectrometry
64000
-
x * 64000, SDS-PAGE and calculated
64290
mature MutB, calculated from amino acid sequence
65600
-
gel filtration
65819
x * 65819, mature gene product, calculated
66000
-
x * 66000, SDS-PAGE
67000
-
x * 69980, calculated, x * 67000, SDS-PAGE
67300
-
x * 67300, SDS-PAGE
68800
x * 68800, about, sequence calculation
69980
-
x * 69980, calculated, x * 67000, SDS-PAGE
70180
calculated from amino acid sequence
79500
-
gel filtration
80000
-
determined by SDS-PAGE, in the range of 70-80 kDa
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type NX-5 and enzyme mutant complexes E295Q-sucrose and D241A-glucose, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml protein solution with 0.001 ml of reservoir solution containing 0.1 M trisodium citrate, pH 5.6, 0.2 M ammonium acetate, and 30% PEG 4000, and for sucrose-complexed mutant enzyme crystal 20 mM sucrose, 0.1 M bicine, pH 9.0, and 30% PEG 6000. The D241A-glucose complex and R335H/R336T/K337I/D338P-glucose complex are co-crystallized in the presence of 20 mM sucrose, 0.1 M sodium cacodylate, pH 6.5, and 29% PEG 8000, 20C, 3-5 days, X-ray diffraction structure determination and analysis at 1.70 A, 1.70 a, and 2.00 A resolutions, respectively
-
hanging-drop vapour-diffusion method at 295 K
-
hanging-drop vapor diffusion method, structure solved at 2.2 A resolution
-
native enzyme, crystals belong to space group P212121 and diffract to 1.95 A resolution
-
expression in Escherichia coli
-
wild-type in native state and in complex with competitive inhibitors Tris, deoxynojirimycin, and castanospermine, and inactive mutants D200A, and E254Q, in complex with D-glucose and sucrose
-
purified recombinant enzyme mutants R284C in complex with transition-state mimic deoxynojirimycin, and F164L in complex with glucose, sucrose, trehalulose, or isomaltulose, X-ray diffraction structure determination and analysis at 1.7-2.15 A resolution
in complex with deoxynojirimycin, sitting drop vapor diffusion method, using
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface, stable at
727181
5 - 6
the enzymatic activity is significantly lower outside the optimal pH range of 5.0-6.0 implying that the enzyme is very sensitive to pH
704227
5 - 8
-
1 h, more than 80% residual activity
679557
5.1 - 6.7
-
highest stability
3468
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 70
about 50% activity at 20C, about 80% activity at 30C, 100% activity at 40-50C, about 20% activity at 55C, complete loss of activity at 60-70C
30 - 60
-
the enzyme is stable for longer than 48 h at 30C. The stability of the enzyme decreases drastically at 50C and 60C with a half-life duration of 90 min and 5 min, respectively
35 - 55
-
recombinant enzyme displayed on Saccharomyces cerevisiae surface, stable at, half-life at 50C is 2.4 h
40
-
1 h, pH 5.6, stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the isomaltulose synthase immobilized only with alginate remains stable for eight 24 h batch cycles or 192 h total time
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 50% glycerol, stable for at least 6 months
22C, 50% glycerol, 60% residual activity after 15 days
30C, purified enzyme in 25 mM PBS (pH 5.8), 2 weeks, 35% loss of activity
-
30C, stable for 2 weeks
-
4C, purified enzyme in 25 mM PBS (pH 5.8), 2 weeks, 23% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, SP-Sepharose column chromatography, and Sephacryl S-300 gel filtration
-
expression in Escherichia coli
-
native enzyme 17.9fold by adsorption on a chromatographic resin
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography, gel filtration
purification and immobilization in a single step
-
recombinant enzyme from Escherichia coli strain BL21(DE3); recombinant enzyme from Escherichia coli strain BL21(DE3)
D0VX20, L0W308
recombinant enzyme from Escherichia coli strain BL21(DE3); recombinant enzyme from Escherichia coli strain BL21(DE3); recombinant enzyme from Escherichia coli strain BL21(DE3)
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatograhy and gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli by nickle affinity chromatography and gel filtration
recombinant protein
recombinant wild-type and mutant enzymes
using subsequently a Sephadex G-25, a DEAE-cellulose and a Sephadex G-75 column
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning and expression in Escherichia coli strain DH10B, expression on cell surface of Saccharomyces cerevisiae strain FMB-1
-
DNA and amino acid sequence determination and analysis, sequence comparisons, functional expression of His6-tagged enzyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli JM109 cells
expressed in sugarcane (Saccharum sp.) cultivar Q117 embryogenic callus
expression in Escherichia coli
expression in Escherichia coli, with His-tag
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene mutB, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning and expression of wild-type and insertional disruption mutant in Escherichia coli strain BL21 (DE3); gene mutB, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning and expression of wild-type and insertional disruption mutant in Escherichia coli strain BL21 (DE3); gene mutB, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning and expression of wild-type and insertional disruption mutant in Escherichia coli strain BL21 (DE3)
gene mutB, recombinant expression of wild-type and mutant enzymes
gene smuA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning of full-length gene including the periplasmic signal sequence and expression of wild-type and insertional disruption mutant in Escherichia coli strain BL21 (DE3); gene smuA, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning of full-length gene including the periplasmic signal sequence and expression of wild-type and insertional disruption mutant in Escherichia coli strain BL21 (DE3)
D0VX20, L0W308
gene smuA, sequence comparison, expression of wild-type and mutant enzymes
recombinant expression in Escherichia coli strain BL21(DE3) periplasmic space using vector pET22b-palI, usage of untreated cane molasses and corn steep liquor for Escherichia coli fermentation
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D241A
-
site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
E295Q
-
site-directed mutagenesis, sucrose binding structure in comparison to the wild-type enzyme by crystal structure analysis
F297A
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
F321A
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R325D
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R328D
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
R335H/R336T/K337I/D338P
-
site-directed mutagenesis, glucose binding structure in comparison to the wild-type enzyme by crystal structure analysis
E295Q
-
site-directed mutagenesis, sucrose binding structure in comparison to the wild-type enzyme by crystal structure analysis
-
F297A
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
-
R325D
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
-
R328D
-
site-directed mutagenesis, the mutant shows an altered product ratio of trehalulose and isomaltulose compared to the wild-type enzyme
-
D140E
-
almost complete loss of catalytic activity
D140G
-
almost complete loss of catalytic activity
D140N
-
almost complete loss of catalytic activity
D329A
-
42% of wild-type activity, no change in major products
L326Y
-
20% of wild-type activity, no change in major products
L326Y/D329A
-
3.4% of wild-type activity, no change in major products
D140E
-
almost complete loss of catalytic activity
-
D140G
-
almost complete loss of catalytic activity
-
D140N
-
almost complete loss of catalytic activity
-
D329A
-
42% of wild-type activity, no change in major products
-
L326Y
-
20% of wild-type activity, no change in major products
-
D327N
-
turnover number for sucrose: 1.4fold decrease, KM-value for sucrose: 1.65fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 43.7% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 41.0% increase
D327R
-
turnover number for sucrose: 2.45fold decrease, KM-value for sucrose: 2.2fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 26.5% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 17.7% increase
D329N
-
turnover number for sucrose: 1.17fold decrease, KM-value for sucrose: 2.9fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 52.4% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 54.7% increase
E498P
-
temperature-optimum is 40C compared to 35C for the wild-type enzyme, maximal specific activity increases by 7%. Half-life at 50C is 9.45 min compared to 1.81 min for wild-type enzyme. Mutation slightly increases the ratio of turnover number to KM-value. Percent content of monosaccharide decreases from 5.9% of the wild-type enzyme to 3.4%
E498P/R310P
-
temperature-optimum is 45C compared to 35C for the wild-type enzyme, maximal specific activity increases by 16%. Half-life is 13.61 min compared to 1.81 min for wild-type enzyme. Mutation slightly increases the ratio of turnover number to KM-value. Percent content of monosaccharide decreases from 5.9% of the wild-type enzyme to 3.3%
R325D
-
turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 1.2fold decrease, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 67% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 43.6% increase
R325L
-
turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 1.1fold decrease, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 54.3% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 31.3% increase
R328D
-
turnover number for sucrose: 11.9fold decrease, KM-value for sucrose: 2fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 65.6% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 61.2% increase
R328L
-
turnover number for sucrose: 14.5fold decrease, KM-value for sucrose: 5fold increase, alpha-D-glucopyranosyl-1,6-D-fructofuranose content: 51.9% decrease, alpha-D-glucopyranosyl-1,1-D-fructofuranose content: 50.3% increase
D442N
the mutant favors the transfer reaction with an isomer preference for isomaltulose
R311C
the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
D442N
-
the mutant favors the transfer reaction with an isomer preference for isomaltulose
-
R311C
-
the mutant demonstrates higher catalytic efficiency for D-glucose production over trehalulose production
-
F164L
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics
R284C
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics. Presence of Mg2+, Ca2+ and Zn2+ ions and glucose have no effect on the activity of the R284C mutant
F164L
-
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics
-
R284C
-
site-directed mutagenesis, three-dimensional structure from crystal structure analysis, comparison to the wild-type. The mutant shows hydrolytic activity converting sucrose to glucose and fructose, kinetics. Presence of Mg2+, Ca2+ and Zn2+ ions and glucose have no effect on the activity of the R284C mutant
-
E428D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F297A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F297P
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F297P/R333K
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
F321A
site-directed mutagenesis, the mutant shows only hydrolytic activity
F321A/F319A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R333K
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R456K
site-directed mutagenesis, inactive mutant
E428D
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
F297A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
F297P
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
-
F297P/R333K
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
-
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
synthesis