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Cultured milk products for

lactose-intolerant recipients

Cultured milk
products for
lactose

S. Sarkar
Department of Quality Assurance, Metro Dairy Ltd, Kolkata, West Bengal,
India

357

Abstract
Purpose The purpose of this paper is to enlighten the prophylactic aspect of cultured milk
products, which render it suitable for lactose-intolerant subjects.
Design/methodology/approach The paper outlines the significance of lactase enzyme and the
mechanism of lactase digestion. This is followed by a discussion of lactase activities in starter
cultures and cultured milk products for lactose-intolerant participants. Factors affecting lactase
activity are described.
Findings Starter cultures possess the enzyme b-galactosidase, required for lactose hydrolysis and
their application led to the development of a number of cultured milk products, which are more easily
digestible than milk by lactose-intolerant individuals. Reasons attributable for better digestion of
cultured milk products than milk are reduction in lactose content, increase in microbial lactase
enzyme, stimulation of hosts mucosal lactase activity and slower transit of cultured milk products as
compared to milk.
Originality/value Consumption of cultured milk products by lactose-intolerant recipients is
suggested.
Keywords Milk, Digestive sysytem
Paper type Research paper

Introduction
Inability of human beings to digest lactose is often referred to as Lactose-intolerance
and has been attributed to insufficient amounts of lactase in the small intestine to
hydrolyze lactose consumed in the diet (Littman and Hammond, 1965; Bayless and
Rosenweig, 1966). b-galactosidase, commonly known as lactase is capable of
hydrolyzing b-D-galactoside bond between D-galactose and glucose. The enzyme is
widely distributed in nature and has been isolated from plants, animals and
microorganisms.
Lactobacilli is the normal resident of gastro-intestinal tract (Mitsuoka, 1992) and
capable of restoring the normal microbial balance in the intestine (Garvie et al., 1984);
utilization of lactobacilli during the manufacture of cultured milk products are
proposed to exhibit health-promoting or probiotic effect in humans, which include
improvement of lactose digestion (Gilliland, 1989). Shahani and Chandan (1979)
pointed out that cultured milk products may provide supplementary quantities of
lactase and other constituent enzymes, elaborated by cultures during fermentation,
contributing towards the assimilation of lactose by lactose-intolerant individuals.
In the present article, an endeavor has been made to enlighten the prophylactic
aspect of cultured milk products, which render them more suitable for ingestion by
lactose-intolerant recipients.
Nutrition & Food Science
Significance of lactase enzyme
Vol. 36 No. 5, 2006
Lactose, a disaccharide composed of glucose and galactose, is the major solid
pp. 357-364
Emerald
Group
Publishing Limited
component of milk and must be hydrolyzed into its components under the influence of E
0034-6659
enzyme lactase, a membrane bound enzyme present in the brush border of the small
DOI 10.1108/00346650610703216

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358

intestinal epithelial cell prior to its absorption by humans (Miller and Brand, 1980;
Hourigan, 1984). In case the quantum of lactose ingested exceeds the hydrolytic
capacity of the available intestinal lactase, the undigested portion of lactose is
transported to the large intestine, where it increases the osmolarity of the intestinal
fluids. Undigested lactose undergoes bacterial fermentation in the colon, generating
organic acids, carbondioxide and hydrogen, which along with the large amount of
water is drawn into the intestine, are primarily responsible for various symptoms such
as bloating, flatulence, abdominal cramps, diarrhoea and loss of appetite (Hourigan,
1984; Hofi, 1990). Lactose maldigestion occurs due to either gastro-intestinal disease or
physiological decline in the intestinal lactase activity and may lead to clinical
symptoms of lactose-intolerance. Semenza and Auricchio (1995) registered reduction
in lactase activity due to digestion of lactasephlonizin hydrolase molecule by
pancreatic proteases at the brush border membrane. Deficiency of enzyme lactase may
be of three types (Swaminathan, 1998).
Congenital lactase deficiency
Persons cannot tolerate lactose due to absence of lactase enzyme in the intestine,
resulting in accumulation of lactose in the intestine causing abdominal pain and loose
motion.
Lactase deficiency in premature infants
This condition occurs in premature infants due to decrease lactase enzyme activity in
the intestinal mucosa. Initially, infants cannot utilize lactose efficiently, however
they are able to tolerate and digest milk after one month due to increase in lactase
activity.
Acquired lactase deficiency
Adults and older children cannot tolerate large amounts of milk due to their nonhabitual consumption of milk resulting in low lactase in the intestinal mucosa.
Mechanism of lactose digestion
Lactic acid bacteria must survive the gastro-intestinal tract to provide the beneficial
effect. Cells of yoghurt cultures contain b-galactosidase as an intracellular enzyme,
therefore it is protected during passage through the harsh environment of stomach
and is able to reach the small intestine, while still inside the bacterial cells.
Permeability of yoghurt cultures is altered, when it comes in contact with bile so that
lactose can enter and get hydrolyzed (Gilliland and Kim, 1984). The sensitivity of
yoghurt cultures to bile has been proposed as an advantage for lactose digestion,
because it increases the permeability of the bacterial cell (McDonough et al., 1987).
Shah and Lankaputhra (1997) noted that rupturing of bacterial cells of yoghurt
cultures reduced viable counts but the released intracellular b-galactosidase improved
the viability of probiotic bacteria such as Bifidobacterium spp. and L. acidophilus
which remained above the recommended level of 106 cfu/mL. Microorganisms residing
in the large intestine made themselves tolerant to lactose through modifications of
their metabolic activity (Hertzler and Savaiano, 1996) Efficient utilization of lactose
from cultured milk products than in milk may be attributed to improved digestion of
lactose resulting from lactase activity of bacteria, stimulation of hosts mucosal lactase
activity or slower intestinal transit of cultured milk product compared to milk (Kolars
et al., 1984; Gibson and Fuller, 1998).

Lactase activity in starter cultures

Galactose activity has been demonstrated in many lactobacilli (Mittal et al., 1974) and
differs greatly in their lactase activity (Premi et al., 1972; Fisher et al., 1985). Variation
in lactase activity of different strains of lactobacillus delbrueckii subsp bulgaricus and
streptococcus thermophilus were noted (Gilliand and Kim, 1984) and the later
organism possess higher b-galactosidase activity than the former (Lee, 1992).
Probiotic cultures such as lactobacillus acidophilus and bifidobacterium, possess
lower levels of lactase and being more resistant to bile than yoghurt cultures are less
efficacious in helping lactose digestion (Shah and Jelen, 1992). Lactase activity of L.
acidophilus strains was reported to vary within a range of 0.5 to 9.5 units (Fisher et al.,
1985) and this disparity may be due to micro-heterogeneity in the amino acid
composition of lactose (Styrer, 1988). Higher lactase activity of propionic acid bacteria
than lactic acid bacteria (Kujawski et al., 1990) suggested their conjugated use during
the manufacture of cultured milk products such as dietetic yoghurt (Sarkar and Misra,
1998a, 2001) and Propiono-Acido-Bifido (PAB) milk (Sarkar and Misra, 1998b).
Cultured milk products for lactose-intolerant recipients
Better tolerance of yoghurt and acidophilus milk in comparison to milk by lactase
non-persistent subjects has been reported (Alm, 1982; Sieber, 2000). A decline in
lactose content from 5.26 to 3.19 per cent and an increase in glucose and galactose
from 0.05 to 2.11 per cent in yoghurt (Abd-Rabo et al., 1992) and digestion of .90 per
cent lactose in small intestine of lactase-deficient subjects due to lactase activity of
yoghurt cultures were noted (Streiff et al., 1990). Efficient absorption of lactose by rats
from yoghurt containing viable flora (Goodenough and Kleyn, 1976) and a decline in
faecal lactase activity in lactase non-persistent human subjects consuming nonpasteurized yoghurt (Pochart et al., 1989) indicated that presence of lactase enzyme
and viable flora are necessary for the beneficial effects.
Efficacy of fermented and non-fermented acidophilus milk or bifidus milk is under
debate for their benefits for lactose-intolerant subjects. Short-term ingestion of
acidophilus milk proved to be not better than milk (Newcomer et al., 1983), and less
than yoghurt (Shah et al., 1992; Vesa et al., 1996), however sonication of bacterial cells
induced better tolerance by lactase non-persistent subjects and may be ascribed to
elevation of lactase activity due to lysis of bacterial cells (McDonough et al., 1987).
Kim and Gilliland (1983) reported that addition of a large number of L. acidophilus
(2.5 6 106 to 2.5 6 108 cfu/mL) to milk prior to ingestion improved lactose digestion
and noted a reduction in breath hydrogen due to prolonged consumption of sweet
acidophilus milk for 6 days, which may be related to hydrolysis of lactose by L.
acidophilus or by lactase in gastro-intestinal tract or reduction in hydrogen producing
bacteria (Fernandes and Shahani, 1989). Effect of feeding cultured milk products on
breath hydrogen test in humans is shown in Table I.
A number of cultured milk products, namely Antoshka-L (based on bifidobacterium), Gnomik 2 (based on bifidobacterium), Zdorove 2 (based on L. acidophilus,
lactic streptococci, bifidobacterium), Progurt (based on streptococcus diacetylactis or
S. cremoris, L. acidophilus and/or B. bifidum), butter milk or yoghurt-like product
(based on S. lactis, Leuconostor citrovorum, L. bulgaricus, S. thermoplilus, L.
acidophilus or B. bifidum) and PAB milk (based on L. acidophilus, B. bifidum and
propionibacterium freudenreichii subsp. shermanii) were recommended for lactose
intolerant infants and children (Schacht and Syrazyski, 1975; Roberts, 1977; Lipatov
et al., 1998; Sarkar and Misra, 1998b). Cultured milk products containing

Cultured milk
products for
lactose

359

NFS
36,5

Cultured milk
product
Sweet
acidophilus milk

Lactose
content (%)
6.30
4.80

360
Yoghurt

1427 (mg
glucose/dL)
0.09 (units/g)

28.30

33.00
7

0 (mg/h g)

1.1610

3.60

2.20 (ONPG
units)
6.8 (ONPG
units)
3724 (mg
glucose/dL)
0.64 (mg/h g)

6.06108

4.20
4.80
4.00

Breath
hydrogen (ppm) Reference

16108

4.90

Table I.
Effect of ingesting
cultured milk products
on breath hydrogen test
in humans

Lactase
Cell count
activity (cfu/g)
(cfu/g)

1593
9.90

2.06108
3.0610

< 200.00

5.40
< 50.0

McDonough et al.
(1987)
Onwulata et al.
(1989)
Savaiano et al.
(1984)
Dewit et al.
(1988)
Gilliland and
Kim (1984)
Mc Donough et al.
(1987)
Savaiano et al.
(1984)

bifidobacterium and S. thermophilus were tolerated well by infants and the higher
level of hydrogen exhaled indicated an earlier bacterial colonization in the digestive
tract. (Leke et al., 1999).
Factors affecting lactase activity
Microbial growth conditions
b-galactosidase activity of L. acidophilus depends on the growth temperature and pH
of medium (Seema et al., 1994). Acid tolerant strains have an advantage in surviving
the low pH conditions in the stomach (pH 2.0), where hydrochloric and gastric acids
are secreted (Toit et al., 1998). During incubation of yoghurt cultures up to 4 h, bgalactosidase activity reached a maximum value (8 units/g), followed by lowering to a
level of 3 units/g, before leveling off. A decrease in enzyme activity between 46 h of
incubation is due to an increase in titratable acidity (Kilara and Shahani, 1976; Dave
et al., 1993).
Microbial viability
Strains of starter cultures must survive the gastro-intestinal tract, which is dependent
on buffering capacity of the medium (Conway et al., 1987). Bile-salt tolerance is
important for strains to grow and survive in upper small intestine (Toit et al., 1998)
and survivality of greater number of bile resistant lactobacilli strains in gastrointestinal tract have been reported (Gilliland et al., 1984). A viable population of . 106
cfu/mL is known to exhibit a positive prophylactic effect (Mijacevic et al., 2001).
Product processing and storage conditions
Dave et al. (1993) registered higher b-galactosidase activity in dahi made from milk
with higher total solids. Higher activity was also noted in formulated milk than in
skim milk due to higher total solid content in the former milk (Sarkar and Misra,
1998a). b-galactosidase activity in dahi (Dave et al., 1993) and PAB milk (Sarkar and
Misra, 1998b) decreased during refrigerated storage with increasing periods of storage
due to shift in pH (Dave et al., 1993). Galvao et al. (1995) noted b-galactosidase activity
of 0.58 to 3.3 units in yoghurt, which declined throughout the storage.

Post-processing treatments
Untreated yoghurt containing live and active flora is tolerated better by lactase nonpersistent individuals than pasteurized yoghurt (McDonough et al., 1987; Dewit et al.,
1988; Pochart et al., 1989). Pasteurization of yoghurt reduced viable counts from
3 6 108/g to 3.4 6 106/g and lactase activity from 0.64 to 0.07 units/g (Savaiano et al.,
1984). Thermization of dahi reduced the lactase activity by 50 to 73.68 per cent and
differed with the strains of cultures adopted for dahi manufacture (Sarkar et al., 1992).
Conclusion
Possession of b-galactosidase enzyme required for lactose hydrolysis by starter
cultures led to their utilization for the manufacture of cultured milk products, suitable
for lactose-intolerant individuals. Better tolerance of cultured milk products than milk
by lactose-intolerant subjects may be attributed to reduction in lactose content,
increase in microbial lactase, stimulation of hosts mucosal lactase activity and slower
transit of cultured milk products in comparison to milk. Factors affecting the lactase
activity are growth condition survivability of starter cultures, surviability of starter
cultures, product manufacturing and storage conditions and post-processing
treatments.
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Corresponding author
S. Sarkar can be contacted at: metrocal@cal3.vsnl.net.in

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