1308  Watanabe & Bito: Journal of AOAC International Vol. 101, No.
5, 2018
SPECIAL GUEST EDITOR SECTION
Determination of Cobalamin and Related Compounds
in Foods
Fumio Watanabe and Tomohiro Bito
Tottori University, Faculty of Agriculture, Department of Agricultural, Life and Environmental Sciences, 4-101 Koyama-Minami,
Tottori, Japan 680-8553
Cobalamin, also known as the red-colored vitamin
B12, is found in animal-based foods such as meat,
milk, and fish. Various cobalamin compounds
are extracted from foods and converted into
cyanocobalamin, which is most stable, to be
analyzed by various methods. Traditionally, the
cobalamin content of foods is determined by
microbiological assay with Lactobacillus delbrueckii
subsp. lactis American Type Culture Collection
7830. However, this lactic acid bacterium can
substitute deoxyribosides or deoxynucleotides
(known as an alkali-resistant factor) for cobalamin.
Therefore, cobalamin contents determined by
this microbiological assay are often incorrect in
some foods. The difficulty of evaluating whether
certain foods contain cobalamin or inactive
corrinoids (or both) may be easily resolved by the
use of bioautography with a cobalamin-dependent
Escherichia coli after separation of the sample
by silica gel TLC. LC/electrospray ionization–
tandem mass spectrometry is also used to analyze
corrinoid compounds, and various inactive corrinoid
compounds have been identified in foods.
C
obalamin (Cbl), which has the largest molecular mass
(1355.4) and most complex structure of all the vitamins,
is more commonly known as the red-colored vitamin
B12 (1). However, scientific use of the term “vitamin B12” is
usually restricted to cyanocobalamin (CN-Cbl). Cbl has a
lower axial ligand containing a cobalt-coordinated nucleotide
(5,6-dimethylbenzimidazole) as the base (Figure 1). In this
review, Cbl refers to all potentially biologically active Cbl
compounds. CN-Cbl is used in most dietary supplements and
is readily converted to the coenzyme forms, methylcobalamin
(MeCbl) and 5´-deoxyadenosylcobalamin (AdoCbl), in the
body (2). CN-Cbl is also available for pharmaceutical use such
as eyedrops and skin cream products (3, 4).
In all animals, from nematodes (5) to humans (6), MeCbl
and AdoCbl function as coenzymes. MeCbl is a coenzyme
of methionine synthase (EC 2.1.1.13), which is involved
Guest edited as a special report on “Analysis and Applications of
Colorants and Optical Sensing Markers” by Paweł K. Zarzycki.
This work was supported by JSPS KAKENHI Grant No. 25450168
(F.W.) and 16K07736 (F.W.)
Corresponding author’s e-mail: watanabe@muses.tottori-u.ac.jp
DOI: https://doi.org/10.5740/jaoacint.18-0045
in methionine biosynthesis, and AdoCbl is a coenzyme of
methylmalonyl-CoA mutase (EC 5.4.99.2), which is involved in
amino acid and odd-chain fatty acid metabolism in mammalian
cells (7, 8).
Cbl is synthesized only by certain bacteria and archaea but not
by plants. Cbl accumulates in animal tissues through microbial
interaction in the natural food chain (9). Thus, animal-based
foods, but not plant foods, are considered to be major dietary
sources of Cbl (10). Many studies have shown that intake of
meat, milk, and fish (or shellfish) significantly increases serum
Cbl levels, suggesting that these foods are excellent sources
of Cbl for humans (11, 12). Strict vegetarians (vegans) cannot
ingest any animal-based foods and are reportedly at risk of
developing Cbl deficiency (13). However, various plant-based
foods that naturally contain large quantities of Cbl have been
identified (14). Additionally, microbiological assays identified
various plant-based foods containing substantial amounts of
inactive corrinoid compounds, such as pseudovitamin B12
(adenyl cobamide or factor IV and PseudoCbl; 9, 14).
The microbiological assay using Lactobacillus delbrueckii
subsp. lactis (formerly L. leichmannii) American Type Culture
Collection (ATCC) 7830 has been widely used in Cbl analysis
of foods (15–17). However, the values determined by this
method are often incorrect in some foods (18, 19) because
the bacterium can utilize inactive PseudoCbl (20) and/or
substitute deoxyribosides or deoxynucleotides (known as an
alkali-resistant factor) for Cbl (15, 21).
Therefore, more precise measurements of biologically active
Cbl in food are needed. In this review, we cover the important
points of the microbiological Cbl assay method and provide
up-to-date information on inactive corrinoid compounds found
in foods and methods to analyze these compounds.
Extraction and Determination of Cbl from Food and
Biological Samples by the Microbiological Assay
To determine the Cbl content of food and biological
samples, highly sensitive methods that can detect picograms of
Cbl are needed. The L. delbrueckii ATCC 7830 microbiological
method is officially used in Cbl analysis of food, and a good
standard curve can be generated, ranging approximately from
10 to 80 pg (22). AdoCbl and hydroxocobalamin (OH-Cbl) are
reportedly the predominant Cbl compounds in foods, but content
and type vary (23, 24). Most Cbl compounds (e.g., MeCbl,
AdoCbl, OH-Cbl) are chemically more labile than CN-Cbl (25).
In food and biological samples, Cbl is bound to enzymes
and transport proteins (26, 27), but it is not protein bound
(as a free form) in vitamin supplements and drugs. Although
pharmaceutical levels of free Cbl can be directly determined
 Watanabe & Bito: Journal of AOAC International Vol. 101, No. 5, 2018  1309

HO OH
N
Protein-bound forms
N
H
N O X H (Food and biological samples)
H NH
O H N NH2
NH O
(1) N
H
H
CH3
HN H O CH3
O N N (2)
Co+
O H N
X= OH
N O
H (3)
HN H
N
H H H -
N (4) SO3
H
N O N
H
O
H H (5) CN
O
H O OH SO3-
P O H H
-O O O
H

Figure 1.  Structural formula of cobalamin and partial structures

of cobalamin-related compounds: (1) 5´-Deoxyadenosylcobalamin;
(2) Methylcobalamin; (3) Hydroxocobalamin; (4) Sulfitcobalamin;
(5) Cyanocobalamin (vitamin B12).

by HPLC (28), protein-bound Cbl in food and biological KCN-boiling Na2SO5-boiling

samples must be converted into the free form before detection. extraction extraction
Naturally occurring Cbl compounds are liberated from proteins
and converted into a single and stable form, either CN-Cbl or
sulfitocobalamin (SO3-Cbl; Figure 2). The potassium cyanide Free form
(KCN)-boiling extraction method is used as an official CN SO3-
Cbl bioassay in Standard Tables of Food Composition in
Japan  (29), and the sodium metabisulfite (Na2S2O5)-boiling Purification
extraction method is adopted as an AOAC Official MethodSM
of Cbl determination using the L. delbrueckii ATCC 7830
bioassay (16). Boiling with KCN at pH 4.0–4.5 for 30 min is TLC
commonly used as a Cbl extraction method (22, 30, 31). HPLC
The KCN-boiling method is often modified to include LC/MS-MS
treatment with proteinase or α-amylase (or both) before boiling Bioassay
treatment to improve extraction efficiency (32). However, the Figure 2.  Outline of extraction and measurement of cobalamin
KCN-boiling extraction method must be performed in a fume compounds in food and biological samples.
hood because KCN is toxic. Therefore, Na2S2O5 is used to
convert naturally occurring Cbl compounds to SO3-Cbl to avoid
the use of toxic KCN. Authentic CN-Cbl is used as a standard factor (19, 34). However, other foods appear to contain low
in the Na2S2O5-boiling extraction method because authentic (several percentages of total Cbl content) or trace amounts of
SO3-Cbl is not commercially available; however, SO3-Cbl has the alkali-resistant factor.
identical activity to CN-Cbl in the bacterial growth (33).
Effect of Pseudovitamin B12 on the Values
Effect of Alkali-Resistant Factor on the Values ­Determined by the Microbiological Assay
­Determined by the Microbiological Assay
Various methanogenic bacteria (35, 36) as well as mammalian
The AOAC official Na2S2O5-boiling extraction method does intestinal digesta (37) or feces (38) contain a substantial amount
not correct for alkali-resistant factor (16). Even in the KCN- of PseudoCbl (molecular weight of 1344.3), which is also called
boiling method, the Cbl content of food is often overestimated adenyl cyanocobamide or factor IV.
if treatment for the alkali-resistant factor is not added to the Edible cyanobacteria are produced by both food and
procedure. Therefore, Cbl values may be overestimated in pharmaceutical companies and used as dietary supplements (39).
food containing deoxyribosides or deoxynucleotides because PseudoCbl, which functions as a cofactor for Cbl-dependent
L. delbrueckii ATCC 7830 substitutes these compounds for Cbl methionine synthase (40), has been purified from various edible
(15, 21). Indeed, a considerable amount of Cbl (approximately cyanobacteria and identified (39–43).
5  μg/100  g wet weight of edible portion) was detected in Shellfish is one of the most popular food items worldwide and
edible bamboo shoots, but all the values were derived from the is a major dietary source of Cbl (44). The Cbl found in shellfish
alkali-resistant factor, indicating that edible bamboo shoots do is derived from microorganisms living in the sea and fresh
not contain Cbl (18). Edible portions of some vegetables and water (45). Cbl has been purified from popular types of shellfish
mushrooms contain trace amounts of Cbl (<0.1  μg/100  g wet (i.e., short-necked clams, oysters, and mussels; 46, 47). However,
weight and several μg/100  g dry weight, respectively), most certain types of edible shellfish (e.g., abalone, turban shell)
of which (50−100%) was attributable to the alkali-resistant contain substantial amounts of PseudoCbl (48, 49). Therefore,
1310  Watanabe & Bito: Journal of AOAC International Vol. 101, No. 5, 2018

other than Cbl, PseudoCbl is the only cobamide commonly found
in food. Accuracy of the microbiological method for detecting Cbl
is considerably low because PseudoCbl and Cbl have reportedly
shown similar growth curves for L. delbrueckii ATCC 7830 (20).
Additional Methods for Detecting Cobalamin
Compounds
In the case of samples containing interfering substances or
substances with high salts and viscosity, phenol-extraction
method (50), Amberlite XAD-2 or -4 column chromatography
(39, 51), or C18 solid-phase extraction (22, 52) methods are
used. Moreover, Cbl in diluted samples or in samples with
very low content can be concentrated several times using C18
solid-phase extraction columns (19, 36).
The KCN-boiling extraction method has significant
advantages in TLC, HPLC, or LC/electrospray ionization–
tandem mass spectrometry (LC-MS/MS) analyses because
commercially available CN-Cbl is readily used as a standard.
The difficulty of evaluating whether certain foods contain Cbl or
inactive corrinoid compounds, such as PseudoCbl, should be easily
resolved using bioautography with a Cbl-dependent Escherichia
coli mutant after separation of the sample by silica gel 60 TLC
(detection limit, approximately 10 pg; 53). This bioautography has
great advantages for simplicity, flexibility, speed, and relative low
cost for the analysis of Cbl compounds in foods (Figure 3).

1 2
A B

1 2 1 2
Figure 3.  Simplified analytical methods of pseudovitamin B12. Upper: Structural formula of (1) cyanocobalamin and (2) adenyl
cyanocobamide (pseudovitamin B12). Lower A: Bioautography with a Cbl-dependent E. coli mutant after separation on silica gel 60 TLC.
(1) Cyanocobalamin and (2) adenyl cyanocobamide (pseudovitamin B12; each 100 pg) were treated with silica gel 60 TLC sheet (migration,
10 cm). 2-Propanol/NH4OH (28%)–water (7+1+2, v/v) was used as a solvent. Lower B: Lichrospher silica gel 60 HPTLC F254s chromatogram;
(1) cyanocobalamin and (2) adenyl cyanocobamide (pseudovitamin B12; each 100 ng) were spotted on the HPTLC sheet, developed with
2-propanol/NH4OH (28%)–water (7+1+2, v/v; migration, 5 cm), and visualized at 254 nm.
 Watanabe & Bito: Journal of AOAC International Vol. 101, No. 5, 2018  1311

Our previous study indicates that HPTLC sheets are the most
suitable for analyzing Cbl compounds in foods. The advantages
of this miniaturized HPTLC method is short migration (5 cm),
short development times (<45 min), and high sensitivity
(detection limit approximately 34 ng at 254 nm; 54).
Moreover, CN-Cbl is specifically purified from an extract using
commercially available CN-Cbl-immunoaffinity columns and then
analyzed using HPLC or LC-MS/MS. LC-MS/MS has been widely
used to analyze Cbl compounds (55) and has led to various newly
identified inactive corrinoid compounds from foods (22, 56, 57).
Escargot contains a small amount of Cbl (approximately
2.2  μg/100  g wet weight) and two inactive corrinoids, which
have been identified as 5-methoxybenzimidazolyl cobamide and
2-methylmercaptoadenyl cobamide (56). A cobalt-free corrinoid
and 5-methoxybenzimidazolyl cyanocobamide (or factor IIIm)
were found in high Cbl-containing Chlorella tablets (22). An
unnatural corrinoid compound, Cbl[c-lactone], was found
in certain dried mushrooms (57; Figure 4). Cbl[c-lactone] is
generated by the incubation of Cbl and chloramine-T used
as a biocide (57). Although the potentially harmful effects of
Cbl[c-lactone] in mammals have not been reported, the compound
may disrupt the metabolism of mammalian Cbl because a similar
compound, Cbl[c-lactam], acts as a Cbl antagonist (58).
Conclusions
The Cbl content of foods is commonly determined by the classical
and principal microbiological assay with L. delbrueckii subsp.
lactis ATCC 7830. However, Cbl contents determined by this assay
are often overestimated because this lactic bacterium can utilize

1 2

3 4
Figure 4.  Inactive corrinoid compounds found in food. (1) 5-Methoxybenzimidazolyl cobamide; (2) 2-Methylmercaptoadenyl cobamide; (3)
Cobalt-free corrinoid; (4) Cobalamin[c-lactone].
1312  Watanabe & Bito: Journal of AOAC International Vol. 101, No. 5, 2018
PseudoCbl and substitute deoxyribosides or deoxynucleotides
(the alkali-resistant factor) for Cbl. Thus, correcting the alkali-
resistant factor is necessary to obtain more accurate data. If foods
contain naturally occurring inactive corrinoids (PseudoCbl)
and/or artificially formed inactive corrinoids (Cbl[c-lactone]), the
Cbl extracts must be analyzed using other identification methods
(TLC, HPLC, or LC/MS-MS). In the case of further analysis
of Cbl compounds using TLC, HPLC, and LC/MS-MS, the
KCN-boiling extraction method is preferably used.
Author Contributions
All authors contributed equally to the preparation of this
manuscript and have approved the final version.
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