Surimi Park et al., 1988). There are several steps

Surimi
is a Japanese term which can be defined as the minced fish flesh, washed to
remove most of lipids, blood, enzymes and sarcoplasmic proteins and stabilized
for frozen storage by cryoprotectants. The myofibrillar proteins, which possess
gel forming ability, are concentrated in the resulting product (Benjakul, et al., 2003). Surimi possesses the
functionalities including gelling, binding and emulsifying properties and can
be used as a functional protein ingredient in several products (Lanier, 1986).
Surimi is stabilized myofibrillar proteins concentrated through heading,
gutting, mincing, washing, and dewatering (Lee, 1984; Park & Lin, 2005b).
The concentrated myofibrillar protein is then mixed with cryoprotectants, such
as sugar, sorbitol, and polyphosphates, which serve to stabilize the surimi
during frozen storage (Park et al., 1987;
Park et al., 1988).

There are several steps of surimi
manufacturing process, (Lee, 1984).  For
surimi-type products, fish should be processed soon after the onset of rigor
mortis (Sonu, 1986).  First, the fish is
headed, gutted and cleaned in a washing tank. The fish are then run through a
mechanical deboner which separates the fish flesh from the bone and skin. The
main difference between surirni and ordinary minced fish is that it is
repeatedly washed with water to remove various undesirable components, such as
fat, blood, pigments, and odorous compounds, but more importantly, water
soluble proteins. Washing also increases the concentration of myofibrillar
protein which improves gel strength and elasticity. After washing, water is
removed and the remaining fish flesh is run through a strainer to remove any
residual skin, bone, and scale. 
Cryoprotectants, such as sugar, sorbitol, and polyphosphate are added at
this stage to protect the fish  proteins from
the  denaturing effect of cold  temperatures.

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In
general, lean fish species used in India for production of surimi are mainly
threadfin bream (Nemipterus spp), bigeye
snapper (Priacanthus spp.), croaker (Pennahia and Johnius spp.) and lizardfish (Saurida
spp.). However, the main problem facing the surimi industry is the supply
of raw materials, due to over exploitation of the lean fish. The use of small
pelagic fish species, such as sardine could be better alternative for the lean
fish, but their use for surimi production is limited mainly due to the large
quantity of lipids and myoglobin in the muscle tissue. This results in the
difficulties in making high quality surimi as evidenced by poor gel forming
ability of those species (Chaijan, et
al., 2004).

The
limited fish resources, especially lean fish, dark muscle fish have been paid
more attention as a potential alternative raw material, especially for surimi
production (Wu, et al., 2000; Chaijan
et al., 2004). So far, sardine and
mackerel have been used for surimi production (Ochiai, et al., 2001). The pelagic and shoal fishes such as Sardinella longiceps and Sardinella fimbriata have bumper
landings in Ratnagiri (CMFRI, 2013). Dark-muscle fish species, which currently
make up 40-50% of the total fish catch The normally lower “L value” (which is a
measure of lightness) for dark muscle (Jiang et al.,1998, Wang et al., 2002)
is associated with a high concentration of haem proteins (Lanier, 2000) in
blood (as haemoglobin) and red muscle (as myoglobin) compared with that present
in white fish muscle. According to Lanier (2000), “removal of the coloured
heme-containing moiety from the muscle during refining depends on maintaining
the haem proteins in a nearly native or undenatured state.” If the heme
component of a protein is denatured, the colour of surimi will be darkened due
to binding between heme and myofibril proteins. Lanier (2000) noted that, as myoglobin
is located within the muscle cells, it is more difficult to leach than
haemoglobin.

Gel
forming ability and viscoelastic property are important for meat and meat
products (Lanier, 1992). Quality of gel product depends on the intrinsic and extrinsic
factors such as species, season, harvesting etc. Gelation of fish proteins is
the most important step in forming desired textures in many seafood products,
particularly those from surimi. Various physical conditions and chemical additives
can affect surimi gelling property. Freshness of fish is considered as the
crucial factor determining the surimi quality (Benjakul et
al., 2002; MacDonald et al., 1990)
Fresh or ice-stored fish are commonly used for surimi production worldwide. Due
to over exploitation and the lack of raw material, fish fleet has to go
farther, leading to the poorer quality of raw material. This is mainly caused
by degradation mediated by endogenous proteinase or microorganism.

The quality of surimi during frozen storage depends upon storage temperature.
storage period.  the level of remaining
moisture, and the cryoprotectants used (Lee, 1984). Sucrose was the first cryoprotectants
used after it was found to prevent muscle protein.  particularly the actomyosin. From
denaturation during froze storage (Matsumoto, 1978).  Adding polyphosphates also extends the frozen
shelf-life by enhancing the effects of sucrose. During frozen storage there are
changes in fish muscle quality. Rapid texture deterioration occur during frozen
storage and these changes are connected to protein changes, especially of the
myofibrillar proteins, myosin and actin, which are responsible for the two-step
process of gel formation (Madsen, 1984).

The utilization of surimi increased drastically in recent times because
of its unique texture, high protein and low fat content. Because of this
increased demand, substantial efforts are being made in many countries to study
the suitability of other species for surimi production (Gopakumar et al., 1992; Kim et. al., 1996). Surimi is usually prepared from low fatty white
meat with good gel forming ability to have an elastic texture and desirable characteristics
like bland flavour and functional properties like emulsification properties,
gel strength and elasticity. Though, generally most of the fishes are suitable
for the preparation of surimi, fish with low fat content is often preferred
because of its storage characteristics. Besides this, actomyosin, the principal
component responsible for the above said functional properties, decides the
suitability of a particular species of fish for preparation of myofibrillar
protein concentrate. An elaborate processing schedule is necessary to get the
desired quality washed mince and the washing process depends on the quality of
mince from a particular fish. The gel forming ability of surimi decreases with an
increase in water content (Lee, 1984). High water content is associated with
lower myofibrillar protein content and decreases in the cross-link density.
Since surimi preparation process is species specific establishing the exact
correlation between separating methods and test data becomes the task of each
experiment.

Myofibrillar proteins represent between 70 to 79% of total proteins in
fish with myosin comprising 55 to 60% of the total myofibrillar proteins (Lanier
et al., 2005).  Myosin is the main protein responsible for
the gelation properties of fish, with the gelation properties of the myosin
being species specific (Chan et al.,1993; Park et al., 2008; Yongsawatdigul & Park, 1999). Myosin is a large
asymmetric molecule that has a long ?-helical coiled-coil tail and two globular
heads with an approximate weight of 500 kDa (Hodge & Cope, 2000).  The basic body plan of myosin consists of an
N -terminal head or motor domain, a light chain-binding neck domain, and a
class conserved, C -terminal tail domain and have been categorized into over
twenty different classes (Mooseker & Foth, 2008).

Myofibrillar proteins play a major role in the gelling properties of
muscle foods (Nakayama & Sato, 1971a; Nakayama & Sato, 1971b) and
myosin is the most abundant protein found in myofibrillar proteins (Lanier et al., 2005). Myofibrillar proteins are
the major component of surimi.  Surimi is
produced through heading, gutting, mincing, washing, dewatering and
concentrating the fish myofibrillar proteins (Lee, 1984; Park et al., 2005a).  The concentrated myofibrillar protein is
mixed with cryoprotectants, such as sugar, sorbitol, and polyphosphates which
serve to stabilize the fish myofibrillar protein during frozen storage (Park et al., 1987; Park et al., 1988).  This
concentrated and stabilized myofibrillar protein is used for surimi seafood products
because of its excellent gelling ability.

Increasingly, consumer are demanding more natural,
minimally proceed products. To satisfy these requirements, one of the major
challenges in the food industry consists of reducing conventional chemical
additives in food formulation. In these sense, the alternative use of natural,
plant product have been receiving more and more attention mainly because many of
these product have additional fictional properties. Many naturally occurring
compound found in plant herb and species. Naturally derived plant phenolic
compounds, especially in the oxidized form, have been shown to be the potential
protein cross-linker (Rawel et al., 2002a).
Delcour et al., (1984) found the
formation of a have in beer due to protein-phenolic compound interactions.
Interactions of different phenolic acids and flavonoids with soy proteins were
reported by Rawel et al., (2002b).   the gel strength of bigeye snapper surimi
was found when oxidised phenolic compounds were added (Balange and Benjakul,
2009). phenolic compounds are rich in hydroxyl groups,  surimi 
gel  can  be 
strengthened  via hydrogen  bond 
and  other  interactions 
(Ali  2002).  Polyphenols are the natural compounds, which
are abundant in plants (Shahidi and Naczk, 2004).  The interactions between phenolic compounds
and proteins play an essential role in the processing of certain food products.
Tannin can be used as a food additive with the range of 10 to 400 mg/l,
depending on the type of food to which it is added (Chen and Chung, 2000).

The textural properties developed during gelation are
normally expressed in terms of gel strength, which is the basic parameter for
determining the quality and price of surimi (Benjakul, et al., 2004a). To increase the gel strength of surimi, various
food grade ingredients have been used. However, the addition of these
ingredients poses adverse effect on the surimi gel, particularly on off-flavour
or off-colour development (Rawdkuen and Benjakul, 2008). Addition of the bovine
plasma protein has been prohibited due to the mad cow disease, while egg white
is associated with allergy problems. Hence, the need of natural additives with
an ability of protein cross-linking has been paid increasing attention for the
surimi industry.

Tannins, also referred to as tannic acid (TA), belong
to the first group and have a structure consisting of a central carbohydrate
(glucose) and 10 galloyl groups (Lopes et
al., 1999). Red wine, coffee, chocolate, tea, sorghum, spinach and fruits
(Bananas and grapes) are the different kinds of foods containing tannins
(Lopes, et al., 1999). Tannins can be
used as a food additive with the range of 10 to 400 mg/l, depending on the type
of food to which it is added (Chen and Chung, 2000).

Seaweed
contains phenol level up to 20 % of their dry weight (Connan and Stengel,
2007). Tannin substances with phenolic character occur in marine algae in the
physodes of Phaeophyta, such as Sargassum
species (Vimalabai et al., 2004).
Seaweeds have been identified as a rich source of bioactive compounds and also
exhibiting antimicrobial potential against the pathogenic microbes of medical,
agricultural and environmental importance.

Mango
(Mangifera indica) is one of the most
important tropical plants. Most studies on the exploitation of mango have
been  dealing  with 
mango  peels,  juices 
and  stem  bark, 
however  a  little 
attention  has  been 
given  to mango  leaves. Mango (Mangifera indica) leave have potential for use as therapeutic for
disease such as cancer. (Joona et al., 2013).
The mango leaves contain high amounts of total phenolics and flavonoids that
assesses the possibility to utilize mango leaves as natural source for phenolic
compound in food and industry (Elzaawely and Tawata, 2010).

The
interactions between phenolic compounds and proteins play a very important role
in the processing of certain food products. A better understanding of phenolic
compound-protein interactions would help to control the functional properties
of proteins in food products and the production of protein ingredients. Additionally,
the use of phenolic compound in the appropriate form at a proper concentration
would be a possible means to improve the surimi gel property, especially from
low quality fish like lesser sardine. Therefore, the novel natural additive for
surimi gel improvement can be used as the processing aid in surimi industry.
The outcome of this research will be of great benefit for the surimi and surimi
based products industry.  Thus the aim of
the present work has to study the effect of natural phenolic compound extract
on surimi gel prepared from lesser sardine with the following objective.

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