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org (E-ISSN 2348-1269, P- ISSN 2349-5138)

PATATIN AND ITS VALORIZATION FROM

POTATO JUICE WASTE
Jaspreet Singh* & Balwinder Singh

Assistant Professor
P.G. Department of Biotechnology,
Khalsa College, Amritsar-143002, India
*Email:jpsrattan@rediffmail.com

ABSTRACT : Potato [Solanum tuberosum] tuber is a good source of high-value proteins as it provides dietary essential amino acids.
In terms of hectare-1 protein production, the potato ranks second to wheat, which is at the top position. Among three groups of potato
proteins, patatin is of considerable importance, two others being high molecular weight proteins and protease inhibitors. Patatin offers
several health benefits including antioxidant in LDL peroxidation, a potential agent in blood pressure and blood cholesterol
regulation. Apart from these activities, the properties like foaming and the emulsifying agent have broadened its functional
applications in the food industry. Potato juice discharged as effluent by potato starch manufacturing industry is a rich source of
patatin, which can be utilized as a resource for its isolation. Valorization of Potato juice for patatin production includes the
application of various techniques viz. anion-exchange, size exclusion, affinity chromatography along with certain precipitation
methods viz. ferric chloride, ethanol, ammonium sulphate and carboxymethyl cellulose complexation. Patatin so produced can be
utilized as a value-added component in various food products and can further be exploited in designing novel products for human use.

Keywords : Patatin, Valorization, Potato juice, Solanum tuberosum, Potato protein.

I. INTRODUCTION
The potato [Solanum tuberosum] is the fourth most important food crop throughout the world after wheat, maize and rice
[Arvanitoyannis et al., 2008]. Its recorded global annual production exceeded 376 million metric tones [MMT] in 2013, China is the
top producer [FAOSTAT, 2015]. Regarded as a major tuber crop of temperate regions that account for about 45% of the total tuber
crops production around the globe [Shewry et al., 2003], potato is an excellent source of starch. Apart from starch, potato is also a
dietary source of a significant amount of proteins along with vitamins viz. thiamine [B1], pyridoxine [B6], folate [B9] and ascorbic
acid [C]; minerals viz. potassium[K] , phosphorus[P], calcium [Ca] and magnesium[Mg] and other micronutrients viz. Iron [Fe] and
zinc [Zn]. The average protein content of potato tuber is 20 g kg-1 of its fresh weight. A daily basis dietary recommendation of the
good-quality proteins for human use is 0.80 g kg-1 adult body weight [Trumbo et al., 2002]. As a source of essential amino acids like
lysine, threonine, tryptophan, and methionine; the nutritional value of potato proteins is towards the high side [Flachowsky & Bohme,
2005]. Being a storage glycoprotein that constitutes more than 40% of the total soluble proteins present in the potato tuber, the
patatin, has specific pharmaceutical, biotechnological, food and feed applications [Jørgensen et al., 2006].

II. POTATO AS SOURCE OF PROTEINS

Potato tuber comprises about 2% [w/w] of the nitrogen compounds that account for 35–75% protein contents. Potato proteins
are highly digestible and have a nutritionally favorable amino acid composition [Bárta & Curn, 2004]. In comparison to the proteins
from dietary vegetables and cereals, the potato proteins are recognized as the better quality proteins due to the presence of high contents
of lysine amino acid residue [Kamnerdpetch et al., 2007]. Potato proteins are a good source of essential amino acids namely threonine,
tryptophan and methionine [Kärenlampi &White, 2009] along with high contents of amino acids having branched side chains i.e.
isoleucine, leucine and valine as well as aromatic side chains i.e. phenylalanine and tyrosine [Refstie & Tiekstra, 2003]. Because of
their amino acid compositions, the potato proteins have been graded as equivalent to the animal proteins [Ralet & Guéguen, 2000].
These proteins are relatively safer as the chances towards allergy are very rare [minute allergenicity] in comparison to other dietary
sources like egg, fish, gluten and soy proteins [Fu et al., 2002]. Potato proteins are isolated in three fractions as patatin, protease
inhibitors and other high molecular weight proteins. Among potoato proteins, patatin alone constitutes 40% of the total protein content
and is the well-studied potato protein [Shewry, 2003].

III. PATATIN
Patatin also known as tuberin, is present inside the vacuoles located in the parenchymal tissue of potato tubers [Straetkvern
et al., 1999]. Well recognized as a primary storage protein, it constitutes 40% of the total soluble proteins of tuber [Shewry, 2003] and
is nutritionally equivalent to the egg albumin [Løkra et al., 2008]. Basically, patatin is a glycoprotein that ranges from 40-45 kDa in
molecular weight [Kärenlampi and White, 2009]. Sodium dodecyl sulfate [SDS] gel electrophoresis revealed its existence as an 88-
kDa dimer [Ralet and Guéguen, 2000]. Patatin is a polypeptide of 366 amino acids [Pots et al., 1998] possessing isoelectric point 4.9
[van Koningsveld et al., 2001]. Being a glycoprotein, it contains three glycosylation sites at the asparagine residues i.e. asparagine-

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linked oligosaccharides. Glycosylation functions in the intracellular signaling, protein stability and protect patatin from the
proteolytic digestion [Sonnewald et al., 1989].
Structurally, patatin is a tertiary protein composed of 33% α-helices and 45% β-strands [secondary conformations] that
remain stable up to 45°C. Further increase in temperature leads to the unfolding of its tertiary structure and beyond 55°C patatin
finally denature [Pots et al., 1998]. Parallel β-sheets with the catalytic serine residue within a nucleophilic elbow loop constitute the
core of the patatin protein [Rydel et al., 2003]. In the potato genome, patatin exists as a multicopy gene family that is organized as a
single cluster confined to a single locus on chromosome 8 which is expressed during tuber growth. [Stupar et al., 2006]. DNA-
binding protein viz. Storekeeper [STK], acts as a transcription factor and regulate its expression [Zourelidou et al., 2002].
Patatin is a complex protein which is composed of four isoforms viz. Patatin- A, B, C and D that constitute 62%, 26%, 5% and
7%, respectively. These isoforms show [85-98%] sequence homology [Mignery et al., 1988]. These homologous and immunologically
identical isoforms vary in charge and molecular mass [Pots et al., 1999]. Exceptionally, the isoform contents vary with potato varieties
e.g. 9 isoforms in cv. Désirée [Lehesranta et al., 2005] and 17 isoforms in cv. Kuras [Bauw et al., 2006]. The isoforms ratio is
considered as an important parameter to differentiate between patatin families in various potato species [Bohac, 1991]. Patatin isoforms
can be separated from each other by various techniques based upon charge separation i.e. anion-exchange column. Isoform-A possesses
the lowest surface charge as compared to the other three isoforms viz. B, C and D; therefore, show low affinity with the anion-
exchanger in the column. The isoelectric focusing technique reveals that isoform A contains maximum positive charge at pH 3 and a
strong negative charge at pH 8 as compared to other isoforms [Pots et al., 1999]. However, the isoelectric point of patatin is 4.9.

IV. FUNCTIONAL ROLES

4.1 Antioxidant in LDL peroxidation
In vitro antioxidative activity of the purified patatin was tested by DPPH [1,1-diphenyl-2-picrylhydrazyl] radical antioxidant
assay, employing butylated hydroxytoluene [BHT] and reduced glutathione as controls. Results reported the dose-dependent
antioxidant response of patatin. Upon reducing the particle size to nanomolar level, the response reported by purified patatin was
similar to the antioxidant BHT but better than the reduced glutathione. A repeated peroxidation study using the TBARS assay on the
low-density lipoproteins [LDL] reported the dose-dependent impact against human LDL oxidation as with an increment in the patatin
levels lead to the reduced oxidized LDL levels. Thereby, patatin may be considered as particularly important in cardiac health as LDL
peroxidation is closely linked to the development of human atherosclerosis [Liu et al., 2003].
4.2 Antioxidant in foods
Peroxide value and TBARS [thiobarbituric acid reactive substances] antioxidant assays were performed by using cooked
beef patties to study the antioxidant ability of potato protein hydrolysate fraction. Results concluded that potato protein hydrolysate
fraction possesses substantial reducing power attributed to the peptide cleavage, leading to the product having higher hydrogen ions
availability that stabilizes the free radicals to a greater extent. Therefore, the potato protein hydrolysate fraction has the ability to
improve the oxidative stability of the ground beef patties which may be utilized during their prolonged storage [Wang and Xiong,
2005].
4.3 Cholesterol-lowering impact
The impact of potato peptides on the lipid metabolism of the rats fed with cholesterol-free diet was studied by using the
soybean, casein and potato proteins. The lowest weight gain was reported in the rats fed solely with potato proteins. A correlation was
also observed between the dietary soybean, potato peptides and serum cholesterol levels. Both potato and soy peptides exhibited
similar effects i.e. low non-HDL cholesterol concentration, low apolipoprotein-B mRNA and high excretory lipid levels in the fecal
matter in comparison to the casein-fed rat. On the basis of above observations, it was concluded that low levels of apoB mRNA,
triggers the liver to maximize the LDL cholesterol clearance through excretion in the feces that leads to a reduction in the serum
cholesterol levels. Therefore, this study clarified the role of dietary potato peptides in lowering the serum cholesterol levels [Liyanage
et al., 2008].
4.4 Antihypertensive agent
A study to find the role of potato peptides on the angiotensin-converting enzyme-I [ACE] inhibition concluded that the
potato protein isolates from tuber tissue inhibit the ACE which in turn reduce the blood pressure by decreasing the peripheral vascular
resistance as well as by stabilizing the renal functions. As ACE raises the blood pressure firstly by converting angiotensin-I to
angiotensin-II [a potent vasoconstrictor] that influence the kidneys to retain water and secondly by deactivating the bradykinin [a
potent vasodilator] leading to hypertension. The study also revealed that both autolysis, as well as hydrolysis of the potato proteins,
result in the enhanced ACE inhibition [Mäkinen et al. [2008].
4.5 Emulsifying agent
Emulsion-forming and stabilizing effects were studied by using five unique protein samples prepared from potato juice of cv.
Elkana potato [patatin, ethanol-precipitated patatin, potato protein isolate, protease inhibitor pool and [NH4]2SO4 protein precipitates]
Under microscopic observations, no droplet aggregation was noticed in the emulsion containing patatin, whereas severe droplet
aggregations were visible in case of the other proteins; indicating unstable emulsion van [Koningsveld et al., 2006]. In another study
carried out to test the stability of emulsions of different potato protein fractions over a range of pH 4–8 reported that under acidic
conditions, the patatin emulsion that does not contain sodium chloride salt was more stable than the emulsions containing salt [Ralet
and Guéguen, 2000].

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4.6 Foaming agent

Foam forming and stabilizing ability of various potato proteins viz. patatin, potato protein isolates precipitated using 15%
and 20% ethanol as well as by [NH4]2SO4 fractionation, protease inhibitors along with 20% ethanol precipitated protease inhibitors
was studied by using the foams prepared with sparging and whipping techniques. On the basis of observations at the standard
whipping time of the 70s it was concluded that patatin and protease inhibitors both extracted with 20% ethanol along with [NH4]2SO4
isolates had an optimum whipping speed of 4000 rpm. Whereas, potato protein isolates extracted using 20% ethanol resulted in foam
formation at 3000 rpm. In contrary to these, the protease inhibitors showed no optimal whipping speed at all. However, for patatin
the optimum values reported were 3000 rpm at whipping time of the 30s. Also, with an increase in the whipping speeds and whipping
times, both the foam formation and the volume became better for all the proteins [van Koningsveld et al., 2002].

V. VALORIZATION
A large quantity of the potato juice [5–12 m3 per ton potatoes] is released as waste by the potato processing industry
involved in manufacturing of the starch from potato tuber. Potato juice as effluent creates disposal related issues as it is highly
polluting in nature [Vikelouda & Kiosseoglou, 2004]. Compositionally, potato juice is rich in proteins as well as free amino acids and
minerals, therefore, may be utilized as an important resource of high-value ingredients having economic importance. Such as proteins
that constitute 30-41% of the total solids in potato juice [Wojnowska et al., 1982] that corresponds to 20-60% of the total proteins
present in the tuber [Ralet & Guéguen, 2000].
The recovery of protein from the potato juice by applying heat coagulation method is much productive but has the
drawbacks of imparting an unacceptable flavor and functionality to the product [Zwijnenberg et al., 2002]. Applying a combination of
thermal coagulation along with acidic precipitation technique also recover the large proportion of the proteins. However, the
application of this combined technology is challenging as it may completely deteriorate the functional aspect of the recovered
proteins [Cheng et al., 2010; Miedzianka et al., 2012]. The same was reported in case of patatin isolation, as the simultaneous thermal
and acidic precipitation completely denatured the protein with the complete loss of its functional activity [Waglay et al., 2014] i.e.
non-specific lipid acyl hydrolase activity characterized by the potent insecticidal action against the insect pest corn rootworm [Rydel
et al., 2003]. Interestingly, the various other better techniques for patatin extraction that prominently preserve its functional activity
include salt precipitation, ethanol precipitation, ammonium sulphate fractionation, carboxymethyl cellulose complexation along with
a number of chromatographic techniques.
5.1 Ferric chloride precipitation
FeCl3 is the most commonly used salt to precipitate proteins from potato juice. In low concentrations, the FeCl 3 is reported
to have a strong affinity for potato proteins and extract a high proportion of patatin. At 5mM concentrations, FeCl3 is able to achieve a
purification factor of 6 with 60% yield [Waglay et al., 2014].
5.2 Theoretical framework
Precipitation with the use of ethanol is comparatively easier and better as it results in recovery of the high nutritional value
based proteins with minimal denaturation in comparison to the FeCl3 precipitation [Bártova and Bárta, 2009]. For patatin, a
purification factor of 4 with more than 50% yield is achievable using 20% ethanol [Waglay et al., 2014].
5.3 Ammonium sulfate fractionation
Addition of [NH4]2SO4 to potato juice extracts the proteins on the basis of their solubility differences and recover proteins in
their natural form. The 60% saturation of [NH4]2SO4 is able to extract the highest proportion of patatin from the acidified potato juice
[pH 5.7] with yield more than 90% in comparison to the other precipitation techniques [van Koningsveld et al., 2001].
5.4 Carboxymethyl Cellulose Complexation
Addition of CMC to potato juice coagulates the proteins that may be collected after employing simple centrifugation
technique. Both complexation and precipitation are based upon the electrostatic interactions between the protein molecules and
negatively charged carboxyl groups of the CMC. However, the strength of interactions is influenced by various factors like pH, ionic
strength and net charges as well as the size and shape of the protein molecule. It was observed that over a large range of pH, the CMC
to protein ratio of 0.3 resulted in more than 70% yield [Vikelouda & Kiosseoglou, 2004].
5.5 Anion-exchange chromatography
Anion-exchange chromatography successfully isolated the patatin from the potato juice of cv. Bintje by employing
diethylaminoethanol [DEAE] fast flow column [25 mM phosphate buffer, pH 8]. The bound acidic fraction [~67%] was recovered
using sodium chloride [NaCl] linear gradient at pH4 and the unbound fraction was further chromatographed through SPSepharose fast
flow column [25 mM phosphate buffer, pH 8] and was recovered using a NaCl linear gradient at pH 8. However, patatin [40 kDa]
was recovered in the acidic fraction [Ralet & Guéguen, 2000].
5.6 Size exclusion column chromatography
Potato proteins from the potato juice of cv. Kuras were fractionated by size exclusion chromatography technique using
Superdex 200 HR 10/30 gel filtration column [50 mM sodium phosphate buffer containing 40 mM NaCl at pH 7.0]. Out of the total
eight fractions, the fraction V constitute the patatin [25%]. Potato juice cv. Kuras was reported to contain 37.5% of the patatin
contents [Jørgensen et al., 2006].
5.7 Affinity chromatography
Purification of patatin from potato tubers was achieved by affinity chromatography, using concanavalin-A Sepharose column
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[25mM phosphate buffer, pH7]. Concanavalin-A is a tetrameric metalloprotein that has a strong affinity for the sugar residues. The
eluate from DEAE-cellulose [Schleicher and Schull] column [25mM pH7 phosphate buffer] using eluant [0.25M NaCl- 25mM
phosphate buffer] was further purified through Concanavalin-A affinity column. The electrophoresis of the affinity eluate through
SDS-PAGE gel confirmed the patatin corresponding to the protein band of 45 KD [Racusen & Foote, 1980].
5.8 Combined anion-exchange and affinity chromatography
A combination of anion-exchange chromatography along with affinity chromatography was employed for the purification of
the potato proteins. The eluate from gel filtration chromatography through Bio-Gel P-100 column [phosphate running buffer] when
subjected to anion-exchange chromatography using DEAE-Sephacel column [linear-gradient NaCl as mobile phase] followed by a
glycoprotein-specific affinity chromatography using concanavalin-A-Sepharose column [25 mM, pH 7.0] [phosphate, 0.5 M NaCl as
running buffer] resulted in the 21-fold increase in the specific activity of patatin [Bohac, 1991].

VI. CONCLUSION AND FUTURE PERSPECTIVES

The various studies suggested that potato juice can be processed using various biochemical and biophysical techniques for
patatin isolation. Patatin has the potential to be used in value addition of food products and as a supplement in health products.
However, its utilization in pharmaceutical applications requires its full characterization employing the recombinant as well as other
biotechnological techniques. Realizing the wide spectrum of patatin usage, the in-depth knowledge concerning safety aspects as well
as other pros and cons is required for designing its novel products for human use.

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