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\begin{document}

\title{Effect of structuring psyllium (Plantago ovata) husk emulsion gels by
ultrasound for the application in dysphasia food}



\author[1]{Minfang Luo}%
\author[2]{B. Dave Oomah}%
\author[1]{Farah Hosseinian}%
\affil[1]{Carleton University}%
\affil[2]{Agriculture and Agri-Food Canada Pacific Regional}%


\vspace{-1em}



  
  \date{May 21, 2024}


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\selectlanguage{english}
\begin{abstract}
The aim of this paper was to investigate effects of inulin and
ultrasonic homogenization on particle size distribution and
microstructure of oil-in-water emulsion gels stabilized by psyllium husk
were investigated. The emulsion gel was assessed their utility in meat
puree prepared for people with dysphagia. The results showed that
increasing inulin percentage resulted in reduced particle size and
improved emulsion stability with the optimum at 20\% w/w inclusion.
Ultrasonic homogenization further enhanced the emulsion stability by
reducing the size of emulsion droplet and improving encapsulation of
emulsion droplet. Increasing inulin concentrations in the emulsion gels
added into purees also corresponded with decreasing total expressible
fluid (TEF). The stability of puree against the action of
carbohydrate-hydrolyzing enzymes (\selectlanguage{greek}α-\selectlanguage{english}amylase and \selectlanguage{greek}α-\selectlanguage{english}glucosidase) was
improved with the addition of emulsion gels. Therefore, these developed
emulsion gels could be beneficial in formulating modified-texture food
prepare for people with dysphagia.%
\end{abstract}%



\sloppy


\textbf{1. INTRODUCTION}

Dysphagia is characterized as difficulty swallowing (an oral disorder),
which may range from total lack of swallowing ability to safely ingest
food, fluids, or saliva (Sasegbon \& Hamdy, 2017). In Canada, dysphagia
affects about 35\% of the elder population. Among hospitalized elders,
approximately 50\% have dysphagia which not only impacts their nutrition
and hydration status but also medication intake and overall
quality-of-life (Werstuck \& Steel, 2021). Dysphagia can be caused by
weak tongue, cheek, or throat muscles, hindering food movement in the
mouth for chewing and transferring meals to the stomach (Sasegbon \&
Hamdy, 2017). Aspiration, aspiration pneumonia, dehydration,
malnutrition, morbidity, and death are among risks associated with
dysphagia (Tagliaferri et al., 2019).

Dysphagia is clinically managed through the provision of thickened
liquids and texture-modified foods. These modified foods and liquids
reduce the risk of aspiration and increase hydration and nutrition.
(Seshadri et al., 2018). Texture modified foods include pureed foods
that are naturally or mechanically altered so that the original food
becomes moist, smooth and homogeneous requiring minimal oral preparation
(Keller et al., 2012). In the preparation of pureed foods, thickeners
are an integral ingredient which improve consistency and cohesiveness
and decrease syneresis (e.g., released liquid) of food products
(Nishinari et al., 2019; Alvarez et al., 2012). Thickened fluids delay
flow than liquids (e.g., water), providing an appropriate reflex
reaction time when swallowing (Hadde et al., 2021).

Food ingredients used as thickening agents in purees are typically
hydrocolloids. Hydrocolloids are a heterogeneous group of long chain
polymers (such as polysaccharides and proteins) that form viscous
dispersions and/or gels in water (Saha \& Bhattacharya, 2010). Starch is
the most commonly used thickener in texture modified foods because it is
relatively cheap and abundant, and does not impart any foreign taste
(Saha \& Bhattacharya, 2010). Therefore, starch-based thickeners are
traditionally used in the management of dysphagia (Newman et al., 2016).
However, starch-thickened liquid decreases viscosity by 90\% in 10
seconds of oral processing (Hanson et al., 2011). This sudden viscosity
reduction in starch-thickened food during oral processing is due to the
action of \selectlanguage{greek}α-\selectlanguage{english}amylase, an enzyme present in saliva. Amylase catalyzes the
hydrolysis of \selectlanguage{greek}α-\selectlanguage{english}1,4 glycosidic linkages between glucose units in starch,
resulting in amylose and amylopectin breakdown. (Sukkar et al., 2018;
Souza, 2010). Hence, the stability of thickener to
carbohydrate-hydrolyzing enzymes should be taken into consideration in
food preparation for dysphagia patients (Sukkar et al., 2018).

The main carbohydrate-hydrolyzing enzymes are \selectlanguage{greek}α-\selectlanguage{english}amylase and
\selectlanguage{greek}α-\selectlanguage{english}glucosidases. Alpha-amylases are hydrolytic enzymes that act upon the
\selectlanguage{greek}α-\selectlanguage{english}(1,4)- and/or \selectlanguage{greek}α-\selectlanguage{english}(1,6)-linkages of starch polymers (Goesaert et al.,
2009). When food is ingested, \selectlanguage{greek}α-\selectlanguage{english}amylase in saliva randomly hydrolyses
\selectlanguage{greek}α-\selectlanguage{english}(1--4) glycosidic bonds of starch components to produce
oligosaccharides of various lengths and a different \selectlanguage{greek}α-\selectlanguage{english}limit dextrins
with \selectlanguage{greek}α-\selectlanguage{english}(1--6) bonds. As a result, the digestion process also breaks down
the mechanical food structure, which is created by starch granules. It
can also lower the viscosity of fluids that are thickened by
starch-based thickeners (Hanson et al., 2011). The oligosaccharides and
dextrins released from amylase action on starch can be further
hydrolyzed into monosaccharides by \selectlanguage{greek}α-\selectlanguage{english}glucosidases which catalyze the
hydrolysis of \selectlanguage{greek}α-\selectlanguage{english}1,4 and \selectlanguage{greek}α-\selectlanguage{english}(1,6) bonds (Tomasik \& Horton, 2012).

\emph{Plantago ovata} (Psyllium) husk polysaccharides are obtained after
milling psyllium seeds and is well-known for its strong hydrophilic and
gelling properties, enabling its use as stabilizers and thickeners in
food industry (Zhou et al., 2022; Franco et al., 2020). Psyllium husk is
an excellent source of both soluble and insoluble fiber, and about 80\%
of the fiber in the husk is soluble and classified as a mucilaginous
fiber due to its powerful ability to form a gel in water (Raymundo et
al., 2014). In addition, psyllium husk can bind with glucose, and
thereby inhibit amylase activity (Ahmed \& Urooj, 2010). Moreover,
psyllium husk can absorb water more than 50 times its initial weight,
expanding and creating a smooth bulky gel (Masood \& Miraftab, 2010).
However, due to its extremely strong gel-forming ability and
water-absorption property, psyllium husk rapidly forms a solid gel when
it binds with water, impeding its incorporation into food homogeneously
and limiting its food product application (Yu et. al., 2003).

These limitations can be overcome by developing psyllium husk emulsion
gel for use in modified-texture foods to enhance consistency and
cohesiveness, and to reduce syneresis. Emulsion gels are formed by
gelling the continuous phase of emulsions or by aggregating the emulsion
droplets through the addition of hydrophilic polymers (Fig. 1). With the
gelling of the continuous phase, the resulting medium is a soft solid
that can entrap emulsified lipid droplets inside the gel matrix. As a
result, functional compounds incorporated into emulsion gels often have
better storage stability compared to those incorporated into emulsion
(Cofrades et al., 2017).

(Place for figure 1)

Fig. 1. The formation of an emulsion gel (O/W), modified from Lu et.al.
(2019).

The formation of emulsions requires energy to agitate the two immiscible
phases together. Ultrasonic homogenization is a high-energy,
cost-effective, energy-efficient, easy, and environmentally friendly
emulsification process to split aggregates and generate tiny droplets
with a narrow size distribution (Leong et al., 2017). Smaller droplet
size can improve emulsion stability by avoiding gravity separation;
hence, ultrasound-treated emulsion has higher stability than untreated
emulsion. However, the effect of ultrasound on emulsion gels needs to be
further explored and assessed.

In this study, we first developed and optimized food-grade psyllium husk
emulsion gel. Then, the stability of ultrasonic-treated and untreated
emulsion gels was investigated by polarized light microscopic,
cryo-scanning electron microscopic observations and particle size
analysis. We also studied the total expressible fluid and the inhibitory
effects of psyllium husk emulsion gel on alpha-amylase and
alpha-glucosidase activities in puree samples.

\textbf{2. MATERIALS AND METHODS}

\textbf{2.1. Materials}

Sunflower oil was from Saporito foods (Montreal, Quebec, Canada). Inulin
was extracted from Jerusalem artichoke by Nutia Food Ingredients
(Kentwood, Michigan, USA). Sodium alginate (Landor Trading Company) was
purchased from Amazon. Psyllium husk was from a local grocery store
(Bulkbarn.ca). Sodium carbonate was from VWR International Co.
(Mississauga, ON, CA). Tween 80 (polyoxyethylene-20-sorbitan monooleate)
was from Fisher Scientific (CA). Alpha-glucosidase, \selectlanguage{greek}α--\selectlanguage{english}amylase, P-NPG
(p-Nitrophenyl-\selectlanguage{greek}α-\selectlanguage{english}D-glucopyranoside), 3,5-Dinitrosalicylic acid and
potassium sodium tartrate tetrahydrate were from Sigma-Aldrich (St
Louis, MO, USA). Salmon puree, chicken puree, chicken stew puree and
beef puree were kindly provided by Apetito HFS Ltd. (Orl\selectlanguage{ngerman}éans, ON, CA).

\textbf{2.2. Formulation and preparation of psyllium husk emulsion gels}

Psyllium husk (3\%) was dissolved completely at 78.4\% of water phase
(80 \selectlanguage{english}) then cooled to room temperature (23 \selectlanguage{english}). Emulsions were prepared
with 0\%, 5\%, 10\%, 15\% and 20\% (w/w) inulin to investigate suitable
inulin concentration. In preparation, inulin was dissolved in water
phase to replace the same amount of water in the formulation. Then 1\%
sodium alginate and 17.6\% sunflower oil were added to the water phase,
followed with mechanical stirring using a Tissuemiser (Fisher
Scientific, Ontario, CA).

\textbf{2.3. Ultrasound-treated emulsion gel}

Ultrasound was applied to prepare emulsion gel with above formulation
(section 2.2.) based on the method of Leong et al. (2017) with
modification. Husk (1.5 g) was first dissolved completely in 13.7g of
water (80 \selectlanguage{english}) then cooled to room temperature (23 \selectlanguage{english}). Inulin (0, 2.5, 5,
7.5 or 10 g) was mixed in the husk solution by ultrasound at 2 W
calorimetric power for \textasciitilde{}10-20 seconds. Sunflower oil
phase (8.8 g) was then mixed with the aqueous phase by ultrasound at 10
W calorimetric power for \textasciitilde{} 60-120 seconds. The mixture
was then remixed with 25 g of alginate solution (0.5 g sodium alginate
in 24.5 g water) at 10 W until the emulsion appeared homogenous. The
formulated emulsions were stored at 4 \selectlanguage{english} for further analysis.

\textbf{2.4. Droplet size measurement}

Droplet size of emulsion gels were determined by polarized light
microscope (Axioplan 2 imaging and Zeiss Axiophot 2 universal
microscope, Carl Zeiss Inc., Jena, Germany). The images were taken with
a Retiga 1300 camera linked to Northern eclipse software. The dispersed
droplet size from the images was analyzed via Image J software.

\textbf{2.5. Meat sample preparation}

Puree samples (salmon, chicken, chicken stew and beef) were stored at
least -20 oC until needed and thawed to room temperature for the
experiment. Different puree sample (5\% and 10\% w/w) were replaced with
ultrasonic-treated 3\% psyllium husk 0\%, 10\%, or 20\% inulin emulsion
gels. Each treatment was mixed homogeneously using a Tissuemiser (Fisher
Scientific, Ontario, CA). After each mixing, the resultant puree samples
were stored at -20 oC until analysed.

\par\null

\textbf{2.6. Total expressible fluid (TEF) determination}

The total expressible fluid (TEF) was determined according to the
procedures described by Ismail et al. (2021) and Colmenero et al. (1995)
with minor modification. Three replicates of puree (\textasciitilde{}10
g) at room temperature were centrifuged (1 min, 3250 g), heated in a
water bath (30 min, 70 degC) and immediately recentrifuged. In case of
microwave oven heating method, three replicates of puree
(\textasciitilde{}10 g) at room temperature were centrifuged (1 min,
3250 g), heated by the household microwave oven (Model DMW799BL, Danby,
ON, CA) for 1 min at 700W and immediately recentrifuged. The supernatant
was removed and the residue weighed. The total expressible fluid (TEF)
was calculated according to the following equation (Ismail et al.,
2021):

TEF(\%) =\(\frac{Weight\ of\ the\ sample\ before\ heating-\ Weight\ of\ the\ sample\ after\ heating}{\text{Weight\ of\ the\ sample\ before\ heating}}\)x 100 (1)

\textbf{2.7. Cryo-Scanning Electron microscopic observation of emulsion
gels and puree samples}

Emulsion gels and puree samples were observed under cryo-SEM
(cryo-scanning electron microscope, Nano Imaging Facility Laboratory of
Carleton University, Ottawa, ON). The method of Liu \& Lanier (2015) was
employed with slight modification. The internal portion of the fresh
emulsion gels and puree samples were cut into blocks of 0.5 cm, the
blocks were then frozen on a metal plate surrounded by liquid nitrogen
for 20 s. The block was placed on a copper specimen holding and observed
under a Cryo-SEM. The microscope was operated at 20 kV in low vacuum
mode (40 Pa), with the temperature at \textless{}\selectlanguage{english}-50 \selectlanguage{english}.

\textbf{2.8. Alpha-amylase inhibitory activity}

The \selectlanguage{greek}α-\selectlanguage{english}amylase inhibitory activity of emulsion gels and puree samples was
carried out according to the standard method with minor modification
(Telagari \& Hullatti, 2015; Bhutkar \& Bhise, 2012). In a 96-well
plate, reaction mixture containing 20 \selectlanguage{greek}μ\selectlanguage{english}l \selectlanguage{greek}α--\selectlanguage{english}amylase (1 U/ml) and 60 \selectlanguage{greek}μ\selectlanguage{english}l
of varying diluted sample solution was preincubated at room temperature
for 30 min. Then, 80 \selectlanguage{greek}μ\selectlanguage{english}l of 1\% soluble starch in buffer (20 mM phosphate
buffer pH 6.9) was added as a substrate and incubated further at 37 \selectlanguage{ngerman}°C
for 10 min; DNS color reagent (80 \selectlanguage{greek}μ\selectlanguage{english}l) was then added and boiled for 10
min. The absorbance of the resulting mixture was measured at 540 nm
using a Multiplate Reader (BioTek Cytation 5, Ottawa, Canada).

Psyllium husk (3\%) and inulin emulsion gels (0, 5, 10, 15, and 20\%)
were diluted in buffer to give a final concentration of 5 mg/ml. Diluted
emulsion samples were centrifuged (10,000 rpm, 2 min, room temperature),
and the clear supernatant was applied to the test. For meat puree
sample, a blank was prepared without sample and another without the
amylase enzyme, replaced by equal quantities of buffer (20 mM sodium
phosphate buffer, pH 6.9). Meat puree samples were diluted in buffer to
give a final concentration of 50 mg/ml and centrifuged (10,000 rpm, 2
min, room temperature). The clear supernatant was used for the test.
Puree sample (salmon, chicken, chicken stew or beef) without emulsion
incorporation was representative of the 100\% enzyme activity.

Each experiment was performed in triplicates. The results were expressed
as percentage inhibition, calculated using the formula:

Inhibitory activity (\%) = {[}(Abs\textsubscript{bank} -
Abs\textsubscript{sample})/ Abs\textsubscript{bank}{]}\selectlanguage{ngerman}×100 (2)

Where Abs\textsubscript{bank} is the absorbance of the bank and
Abs\textsubscript{sample} is the absorbance of the sample.

\textbf{2.9. Alpha -glucosidase inhibitory activity}

The \selectlanguage{greek}α-\selectlanguage{english}glucosidase inhibitory activity of emulsion gels and puree samples
was carried out according to the standard method with minor modification
(Telagari \& Hullatti, 2015; Picot et al., 2014). In a 96-well plate,
reaction mixture containing 50 \selectlanguage{greek}μ\selectlanguage{english}l phosphate buffer (0.1 mM, pH 6. 9), 10
\selectlanguage{greek}μ\selectlanguage{english}l alpha-glucosidase (1 U/ml), and 20 \selectlanguage{greek}μ\selectlanguage{english}l of varying diluted emulsion
gels was preincubated at 37 \selectlanguage{ngerman}°C for 15 min. Then, 20 \selectlanguage{greek}μ\selectlanguage{english}l P-NPG (1 mM) was
added as a substrate and incubated further at 37 \selectlanguage{ngerman}°C for 30 min. The
reaction was stopped by adding 50 \selectlanguage{greek}μ\selectlanguage{english}l
Na\textsubscript{2}CO\textsubscript{3}~(0.1 M). The absorbance of the
released p-nitrophenol was measured at 405 nm using Multiplate Reader
(BioTek Cytation 5, Ottawa, Canada). A blank was prepared without
diluted emulsion gels and another without the glucosidase enzyme,
replaced by equal quantities of buffer (0.1 mM phosphate buffer, pH
6.9). Psyllium husk (3\%) and inulin emulsion gels (0, 5, 10, 15, and
20\%) were diluted in buffer to give a final concentration of 5 mg/ml.
For meat sample, a blank was prepared without emulsion sample and
another without the glucosidase enzyme, replaced by equal quantities of
buffer (0.1 mM phosphate buffer, pH 6.9). Meat samples were diluted in
buffer to give a final concentration of 50 mg/ml and then were
centrifuged at 10,000 rpm for 2 mins at room temperature. After
centrifugation, the clear supernatant was applied to the test. Puree
sample (salmon, chicken, chicken stew or beef) without emulsion
incorporation was representative of the 100\% enzyme activity. A blank
was prepared without sample and another without the glucosidase enzyme,
replaced by equal quantities of buffer (0.1 mM phosphate buffer, pH
6.9).

Each experiment was performed in triplicates. The results were expressed
as percentage inhibition, calculated using the formula:

Inhibitory activity (\%) = {[}(Abs\textsubscript{bank} -
Abs\textsubscript{sample})/ Abs\textsubscript{bank}{]}\selectlanguage{ngerman}×100 (3)

Where Abs\textsubscript{bank} is the absorbance of the bank and
Abs\textsubscript{sample} is the absorbance of the sample.

\textbf{2.10. Statistical analysis}

Statistical analyses were performed with SAS Software (SAS Institute
Inc, Cary, NC). One-way analysis of variance (ANOVA) by Duncan's
Multiple Range test was used to compare the mean values (\selectlanguage{greek}α\selectlanguage{english}=0.05).
Differences were significant at p \textless{} 0.05.

\textbf{3. RESULTS AND DISCUSSION}

\textbf{3.1. Emulsion gel characterization}

3.1.1. Microscopy

Microscopic images showed that inulin concentration significantly
influenced morphologies of emulsion gels prepared with 3\% psyllium husk
(Fig. 2).

(Place for figure 2)

Fig.2. microscopic observation (500X) of ultrasonic-treated and
untreated 3\% psyllium husk emulsion gel with different concentration of
inulin. Dark arrow indicates length of 20 \selectlanguage{greek}μ\selectlanguage{english}m.

At 0\% inulin concentration, emulsion droplets in close proximity to
each other were large and polydispersed, which increased the
flocculation rate. High flocculation of emulsion droplets indicates low
emulsion stability (Yvonne and Victoria, 2018). The oil droplets in the
emulsion gels became smaller and uniform with increased inulin
concentration suggesting that the husk-emulsions were stable at higher
inulin concentration. A similar result was reported previously (Xu et
al., 2020), where the particle size of oil-in-water emulsion decreased
with increasing inulin concentration. The droplet decrease may be due to
high inulin concentration that forms a secondary interfacial layer
enhancing surface coating of oil droplets to prevent against droplet
aggregation and coalescence; and this result in smaller oil droplets and
highly stable emulsion (Sarkar et al., 2018). These results were further
confirmed by the particle analysis and SEM image.

The ultrasonic-treated emulsions showed higher stability with smaller
particle size compared to untreated emulsion. Reduction of droplet size
by ultrasound can be attributed to shear force generated by the
cavitation of the ultrasonic wave breaking droplets into smaller sizes
(Guo et al., 2014).

3.1.2. Particle size distribution

Fig.3. shows the droplet size distribution of ultrasonic-treaded husk
emulsion gel with different inulin concentration.

(Place for figure 3)

Fig. 3. Particle size analysis of ultrasonic-treated 3\% psyllium husk
emulsion gel with different concentration of inulin.

The particle size analysis of the emulsion gel system indicated one
sharp peak that shifted progressively to the left towards smaller
droplet size with increase in inulin concentration (Fig. 3). The result
revealed that emulsion droplets were more uniformly distributed, and the
number of smaller droplets kept increasing in the emulsion gels.
Reduction of droplet size may be due to increased polysaccharide
concentration resulting in stronger and more compact gel-network, which
entrapped emulsion oil droplets and reduced droplet aggregation (Xu et
al., 2020). In addition, inulin was available to wrap the oil droplet
surface which limited the movement of emulsion droplets and prevented
their aggregation, resulting in smaller oil droplets and more stable
emulsion (Sarkar et al., 2018; Hu et al., 2020). These results were
further confirmed by PLM and SEM image.

3.1.3. Cryo-Scanning Electron microscopic observation

(Place for figure 4)

Fig. 4. SEM observation of ultrasonic-treated and untreated 3\% psyllium
husk emulsion gel with different concentration of inulin. Dark arrow
indicates length of 50 \selectlanguage{greek}μ\selectlanguage{english}m.

The SEM images (Fig. 4) revealed that inulin addition and ultrasonic
treatment affected the morphology of the husk emulsion gel system. The
microstructure of the emulsion gel without inulin was heterogeneous and
porous. Droplets surface changed with increased inulin concentration
from irregular to smooth and less cavities, suggesting that inulin was
in a packed arrangement at the droplets interface, and could also form
an interfacial layer coating the surface of oil droplets. Similar result
was observed for an emulsion developed with zein/corn fiber gum complex
(Zhu et al., 2019). Their study reported that the polysaccharide complex
was adsorbed at the oil-water interface, and that complex also created a
mechanical barrier to prevent interfacial film rupture. Polymers
adsorption at the interface can enhance mechanical properties of the
interfacial films, which can inhibit coalescence, therefore, bigger size
droplets have weaker interfacial films (Mao \& Miao, 2015),

Compared to the untreated emulsion, the droplets surface in
ultrasonic-treated emulsions showed higher integrity of the coating
layer. At 20\% inulin, the dark area in the untreated emulsion gel (Fig.
4) showed that droplets were not completely covered by the inulin layer.
On the other hand, the surface of the ultrasonic treated emulsion was
very smooth, without gap, suggesting that the droplet is completely
covered by the inulin layer at that concentration. Similarly, Xiong et
al. (2019) reported that more emulsifier molecules were adsorbed on the
surface of the oil droplets in the ultrasonic-treated xanthan gum
emulsion compared to untreated emulsion. The increased particle
adsorption on the surface of emulsion droplet by ultrasound apparently
occurs from momentum transfer from the fluid to the particles and
droplets caused by random cavitation events. The momentum transfer can
overcome the stabilizing energy barriers that normally prohibit
nanoparticles from spontaneously adhering to the oil-water interface
(Lee et al., 2019).

\textbf{3.2. Effect of emulsion gel addition in meat puree}

3.2.1. Total expressible fluid (TEF)

Figures 5A and B represent the results of TEF of different purees by
water bath, and microwave oven heating, respectively.

(Place for figure 5)

Fig.5. Effect of incorporation of 10\% psyllium husk (PH) emulsion gel
with 0\%, 10\% and 20\% inulin in puree samples (A) at 70 water bath
heating for 30 min, and (B) at microwave oven heating with power 700W
for 2 min and then centrifugation at 3750 g for 3 min. Different letters
represent significant different at p\textless{}0.05.

TEF of water bath-heated or microwave-heated pure puree (chicken,
salmon, chicken stew and beef without emulsion gel incorporation) was
significantly higher than that of puree with 10\% w/w husk-0\% inulin
emulsion gel incorporation. Water bath and microwave oven heating
methods were selected in this study because they are common household
heating methods. Increased inulin concentration in emulsion gel (from
0\% to 20\%) incorporation in the purees further reduced their TEF. So,
the puree with husk-20\% inulin emulsion gel had the lowest TEF among
the same puree group. For example, within the chicken puree group
(Figure 3.7), the pure puree (no emulsion gel incorporation) had the
highest TEF (31.77\% mean value), while the puree with 10\% w/w replaced
by husk-20\% inulin emulsion gel had the lowest TEF (17.22\% mean
value). Microwave-heating method (Figure 3.8) produced similar result;
the puree with husk-20\% inulin emulsion gel incorporation still had the
lowest TEF within the same puree group. TEF reduction with the inclusion
of husk emulsion gel may be due to ingredients in the emulsion gel
crosslinking with the polar groups of protein matrix. The cross-linking
can strengthen the puree three-dimensional network structure, leading to
stronger binding properties and smaller fluid release during heating
(Colmenero et al., 2005; Kumar, 2021). Previous study (Kumar, 2021) has
shown that inulin has water and fat retention capacity, which also help
TEF reduction.

In comparison to water bath heated-meat puree, the microwave-heated meat
puree had higher TEF, which agrees with Colmenero et al., (2005). This
may be due to the internal microwave heating creating higher center
temperature of the puree, and the high steam pressure driving more water
from within the sample to the surface (Wang et al., 2020).

3.2.2. Cryo-Scanning Electron microscope

(Place for figure 6)

Fig. 6. SEM observation of meat puree samples before and after
incorporation with 10\% w/w husk-20\% inulin emulsion gel

In SEM images, all pure puree samples exhibited the formation of
different size cavities creating structures with a rough and porous
appearance. The high proportion of cavities can be interpreted as water,
fat, and air expansion in the protein network (Paglarini et al. 2022).
The 10\% emulsion gel incorporated puree, had less cavities and more
compact structure compared to pure puree because the emulsion gel
contained high amount of inulin, (Felisberto et al., 2015). The
structural change was likely due to inulin's long chain length and
degree of polymerization, producing firmer and more viscous puree.
Hence, inulin was suggested for use to enhance food texture (Felisberto
et al., 2015).

According to Colmenero et al. (1995), meat matrices with homogeneous and
more compact (less and smaller cavities) structures, similar to the
structure of puree sample with 10\% emulsion gel (Fig. 6), can be
classified as strong meat gels with good water and fat binding
properties. On the other hand, meat matrix with irregular and less
compact (more and larger cavities), and aggregate structures, similar to
those of pure puree samples (Fig. 6), can be classified as poor meat
gels with weak binding properties.

3.2.3. Alpha-amylase inhibition

Figure 7A shows the \selectlanguage{greek}α-\selectlanguage{english}amylase inhibitory effect of 3\% husk emulsion
with 0, 5, 10, 15 and 20\% w/w inulin addition at 5 mg/ml. Inhibitory
activity increased with increasing inulin concentration from 0\% to
15\%. The \selectlanguage{greek}α-\selectlanguage{english}amylase inhibitory activity of the emulsion gel at 20\%
inulin was not significantly different (p\textgreater{}0.05) from that
of 15\% inulin concentration. The inhibitory activity of 3\% husk
emulsion gel with 20\% inulin at 5 mg/ml on \selectlanguage{greek}α-\selectlanguage{english}amylase was 16.06 \selectlanguage{ngerman}±
3.03\%.

(Place for figure 7)

Fig. 7 Inhibitory potency of (A) 3\% psyllium husk emulsion in the
presence of different concentration of inulin at 200X dilution, and (B)
puree samples with incorporated 5\% or 10\% husk-20\% inulin emulsion
gel against \selectlanguage{greek}α-\selectlanguage{english}amylase (1 U/mL) activity at 1\% starch concentration.
Different letters represent significant different at p\textless{}0.05.

The \selectlanguage{greek}α-\selectlanguage{english}amylase inhibitory activity of puree samples (salmon, chicken,
chicken stew or beef) with 5\% w/w and 10\% w/w husk-20\% inulin
emulsion gel (Fig. 7B), showed that all puree samples can delay
\selectlanguage{greek}α-\selectlanguage{english}amylase activity. The inhibitory activity of puree samples with 10\%
w/w replacement by the emulsion gel was higher than that of puree with
5\% w/w replacement. Amongst the purees with 10\% w/w replacement by
husk-20\% inulin emulsion gel, the chicken stew had the highest amylase
inhibition (21.14\%), followed by salmon and chicken (14.12 and 12.68\%
inhibition, respectively). The beef had the lowest amylase inhibition of
7.93\%. Guo et al. (2020) reported that the hydroxyl (-OH) and carboxyl
groups (-COOH) on the polysaccharides branched chain can interact with
the amino acid residues of digestive enzymes (\selectlanguage{greek}α-\selectlanguage{english}amylase and
\selectlanguage{greek}α-\selectlanguage{english}glucosidase), thus inhibiting their activity. In addition, Ahmed \&
Urooj (2010) concluded that dietary fiber, such as wheat bran and
psyllium husk, can bind glucose, and thereby inhibit amylase activity.
Previous \selectlanguage{greek}α-\selectlanguage{english}amylase inhibitory activity indicated that soluble fibers can
capsulate \selectlanguage{greek}α-\selectlanguage{english}amylase and starch, thereby reducing starch accessibility to
the enzyme (Ou et al., 2001).

Our result indicates that incorporation of husk-20\% inulin emulsion gel
will be beneficial to delay dietary starch breakdown in food product and
thereby maintain their consistency with addition of starch-based
thickener during oral digestion.

3.2.4. Alpha-glucosidase inhibition

Figure 8A illustrates \selectlanguage{greek}α- \selectlanguage{english}glucosidase inhibitory effects of 3\%
husk-emulsion with inulin addition (0, 5, 10, 15 and 20\% w/w) at 5
mg/ml. All emulsion gel samples delayed \selectlanguage{greek}α-\selectlanguage{english}glucosidase activity, however
inhibitory activity decreased slightly with increasing inulin
concentration from 0\% to 20\%. The husk-emulsion gel without inulin had
the highest \selectlanguage{greek}α-\selectlanguage{english}glucosidase inhibition (12.93 \selectlanguage{ngerman}± 0.19\%), while the
husk-emulsion gel with 20\% w/w inulin addition had the lowest
glucosidase inhibition of (10.6 ± 0.91\%).

(Place for figure 7)

Fig. 8. Inhibitory potency of (A) 3\% psyllium husk emulsion in the
presence of different concentration of inulin at 200X dilution, and (B)
puree samples with incorporated 5\% or 10\% husk-20\% inulin emulsion
gel against \selectlanguage{greek}α-\selectlanguage{english}glucosidase (1 U/mL) activity at 1mM PNPG concentration.
Different letters represent significant different at p\textless{}0.05.

All puree samples delayed \selectlanguage{greek}α-\selectlanguage{english}glucosidase activity (Fig. 8B). The
inhibitory activity of puree samples with 10\% w/w replacement of the
emulsion gel was higher than that with 5\% w/w replacement. The results
suggest that emulsion addition improved \selectlanguage{greek}α- \selectlanguage{english}glucosidase inhibitory
activity of the puree samples. Among the purees with 10\% w/w
replacement with husk-20\% inulin emulsion gel, salmon had the highest
glucosidase inhibition (4.54\%), followed by beef and chicken (4.08 and
3.87\%, respectively). The chicken stew had the lowest glucosidase
inhibition of 2.13\%. Previous study also suggested psyllium mucilage
could delay \selectlanguage{greek}α-\selectlanguage{english}glucosidase activity and entrap glucose \emph{in vitro}and
\emph{in vivo} (Palanuvej, 2009; Gibb et al., 2015), but this mechanism
has not been explored. Overall, it can be concluded that husk-20\%
inulin emulsion gel incorporation in food product will beneficially
delay \selectlanguage{greek}α- \selectlanguage{english}glucosidase activity.

\textbf{4. Conclusion}

In this study an innovative allergy-free psyllium husk-inulin (up to
20\%) emulsion gel was developed, in which the inulin molecule formed a
protective layer on emulsion droplets. Ultrasonic homogenization further
enhanced the emulsion stability by reducing emulsion droplet size and
improving the formation of inulin layer to encapsulate emulsion droplet.
The inclusion of the husk-inulin emulsion gel in meat puree reduced the
fluid loss during water bath and microwave oven heating and can delay
the action of carbohydrate-hydrolyzing enzymes (\selectlanguage{greek}α-\selectlanguage{english}glucosidase and
\selectlanguage{greek}α-\selectlanguage{english}amylase). It enables the use in food preparation for people with
dysphagia. This study demonstrates the gelling properties of psyllium
husk used in forming emulsion gels with positive impact on meat product.
As such, the results present another ingredient that can be explored in
emulsion-based foods.

\textbf{Acknowledgements~}

Authors acknowledge the financial support from the Natural Sciences and
Engineering Research Council of Canada (NSERC), grant: ALLRP-2020-555211
and Apetito HFS Ltd. (Orl\selectlanguage{ngerman}éans, ON, CA) for providing puree samples.

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