Alpha-galactosidase Function

Your body makes various enzymes to break down and help digest the foods you eat -- it
produces alpha-galactosidase to break down dietary sugars. Aspergillus niger is the source
found in dietary supplements, and it is also found in especially high quantities in yeast,
according to the NYU Langone Medical Center. Taken as a supplement, alpha-galactosidase
helps prevent intestinal gas. The typical dose is 450 galactosidase units -- or GalU -- taken
with each carbohydrate-containing meal.
Both yeasts and muskmelon/cantaloupe (Muskmelon, Cucumis melo) have high levels of
alpha-glactosidase. Acinetobacter sp [1], E. coli, Thermus sp, Aspergillus niger [2],
Penicillium chrysogenum [3]
-Galactosidases catalyse hydrolysis of terminal -1-6 linked galactose residues from
different galactooligosaccharides, glycosphingolipids and glycoproteins (Dey and Pridham
1972) and also show transgalactosylation (Kato et al. 1982) and hemagglutination activity
(del Campillo and Shannon 1982). Due to its diverse catalytic activity, the enzyme is used in
food processing industry for improvement of nutritional value of legumes and animal feeds
by removing the flatulence-causing factors (Patil et al. 2010), in beet sugar industry for
crystallisation of sugars (Yamane 1971) and -galactosidase producing organisms as
probiotic (Chen and Mustapha 2012; Liu et al. 2014). Recombinant alphagalactosidases
such as Fabrazyme and Replagal are being currently employed in the treatment of
Fabrys disease which is a rare Xlinked lysosomal storage disorder (Tsuboi and Yamamoto
2012; Desnick 2004). The enzyme was reported to be applied for the conversion of Type B
erythrocytes to Type O erythrocytes (Gao et al. 2011) and also in xenotransplantation
(Zeyland et al. 2013). This enzyme is also used in bleaching of softwood in the paper
industry (Clarke et al. 2000). [1]
The -galactosidases (-D-galactoside galactohydrolase) are carbohydrases which catalyse
hydrolysis of -1,6- linked -galactoside residual from simple oligosaccharides such as
melibiose, raffinose, stachyose and from polymeric galactomannans (1). These enzymes are
used in the hydrolysis of raffinose and stachyose present in soy beans and other leguminous
food and feed that cause intestinal discomfort, flatulence and low feed utilization in
monogastrites (12). In beet sugar industry, -galactosidases are used to remove raffinose
from beet molasses increasing the sucrose yield (23). -Galactosidase is also used to
improve the gelling properties of galactomannans to be used as food thickeners (5). The
enzymic conversion of raffinose family oligosaccharides (RO) in soymilk may be a rational
alternative to improve the nutritional quality of this low-cost, high-quality protein
supplement for humans and animals (20). In the pulp and paper industry -galactosidase
could enhance the bleaching effect of -mannanases on softwood pulp (7). In human
medicine this enzyme can be used for the treatment of Fabrys disease (3) or for the blood
type conversion (25). Weignerova et al. (2009) summarizes recent advances in the use of galactosidases in synthetic and biotransformation applications (28). -Galactosidase is
widely distributed in microorganisms, plants and animals. Microorganisms have the
advantage of being highly active producers, and among them the -galactosidases from
filamentous fungi are the most suitable for technological applications because of their
extracellular localization, acidic pH optimum and broad stability profiles (9). [3]
Food processing through the use of biological agents is historically a well-established
approach. The earliest applications go back to 6,000 BC or earlier, with the brewing of beer,
bread baking, and cheese and wine making, whereas the first purposeful microbial oxidation
dates from 2,000 BC, with vinegar production [13]. Coming to modern days, in the late XIX,
century Christian Hansen reported the use of rennet (a mixture of chymosin and pepsin) for

cheese making, and production of bacterial amylases was started at Takamine (latter to
become part of Genencor). Pectinases were used for juice clarification in the 1930s, and for
a short period during World War II, invertase was also used for the production of invert sugar
syrup in a process that pioneered the use of immobilized enzymes in the sugar industry [1].
Still, the large-scale application of enzymes only became really established in the 1960s,
when the traditional acid hydrolysis of starch was replaced by an approach based in the use
of amylases and amyloglucosidases (glucoamylases), a cocktail that some years latter would
include glucose (xylose) isomerase [1, 2, 4, 5]. From then on, the trend for the design and
implementation of processes and production of goods anchored in the use of enzymes has
steadily increased. Enzymes are currently among the well established products
in biotechnology [6], from US $1.3 billion in 2002 to US $4 billion in 2007; it is expected to
have reached US $5.1 billion in a rough 2009 year, and is anticipated to reach $7 billion by
2013 [3, 5, 79]. In the overall, this pattern corresponds to a rise in global demand slightly
exceeding 6% yearly [7, 9]. Part of this market is ascribed to enzymes used in large-scale
applications, among them are those used in food and feed applications [10]. These include
enzymes used in baking, beverages and brewing, dairy, dietary supplements, as well as fats
and oils, and they have typically been dominating one, only bested by the segment assigned
to technical enzymes [11, 12]. The latter includes enzymes in the detergent, personal care,
leather, textile and pulp, and paper industries [10, 13]. A recent survey on world sales of
enzymes ascribes 31% for food enzymes, 6% for feed enzymes and the remaining for
technical enzymes [11]. A relatively large number of companies are involved in enzyme
manufacture, but major players are located in Europe, USA and Japan. Denmark is
dominating, with Novozymes (45%) and Danisco (17%), moreover after the latter taking over
Genencor (USA), with DSM (The Netherlands) and BASF (Germany) lagging behind, with 5%
and 4% [10, 11, 14].
Sirisha E., R. Potumarthi, dan L. N. Mangamoori. 2015. Purification and characterisation of
intracellular alpha-galactosidases from Acinetobacter sp. Biotech. 5(6): 925932
Hui, Y. H. 2006. Food Biochemistry and Food Processing. Oxford: Blackwell Publishing
Aleksieva P., B. Tchorbanov, L. Nacheva. High-Yield Production Of Alpha-Galactosidase
Excreted From Penicillium Chrysogenum and Aspergillus Niger. Bulgaria: Bulgarian Academy
of Sciences
Soysa, D. R. 2004. Structural Studies of Escherichia Coli Alpha-galactosidase. Sri Lanka:
University of Colombo
Fernandes, P. 2010. Enzymes in Food Processing: A Condensed Overview on Strategies for
Better Biocatalysts. Portugal: Institute for Biotechnology and Bioengineering