Quan Tran Hong | Prince of Songkla University (original) (raw)

Papers by Quan Tran Hong

Colloids and Surfaces A, 2019

Duck albumen hydrolysates (DAH) conjugated with epigallocatechin gallate (EGCG) at various levels... more Duck albumen hydrolysates (DAH) conjugated with epigallocatechin gallate (EGCG) at various levels (2-5%, w/ w) were prepared and characterized. FTIR analysis showed that the conjugation between DAH and EGCG induced the change of secondary structure and modified functional groups of DAH. Furthermore, surface hydro-phobicity of DAH was increased, while total sulfhydryl group and total carbonyl contents were decreased when EGCG was conjugated, especially when EGCG at higher levels was used (P < 0.05). Antioxidant activities and emulsifying properties of DAH-EGCG conjugates were enhanced, particularly when DAH conjugated with 4% EGCG (P < 0.05). Storage stability of fish oil emulsion (FOE) stabilized by DAH or DAH-EGCG conjugate was also investigated up to 15 days at 26-28 °C. Emulsion stabilized by DAH-EGCG conjugate had higher magnitude of ζ-potential (negative charge), smaller oil droplets size (d 43), as well as lower flocculation and coalescence of oil droplets as compared to those of emulsion prepared using DAH throughout the storage. Moreover, oxidative stability of FOE was improved when DAH-EGCG conjugate was incorporated as evidenced by lowered thio-barbituric acid-reactive substances and peroxide value. Thus, the conjugate between DAH and 4% EGCG could serve as an antioxidant emulsifier for enhancement of physical and oxidative stability of FOE.

Trends in Food Science & Technology, 2019

Background: Proteins from different sources serve as primary food components, while polyphenols, ... more Background: Proteins from different sources serve as primary food components, while polyphenols, as secondary metabolites, are abundantly present in plant. Both components play an important role in functional properties and quality of food products. Interaction between proteins and polyphenols, yielding "protein-polyphenol conjugate", spontaneously occurs in most of food systems, and is known to have an impact on sensorial, functional , and nutraceutical properties of the food products. Scope and approach: Protein-polyphenol conjugate can be implemented for improvement of food quality. In this article, mechanism and factors affecting protein-polyphenol interactions as well as the functionalities of protein-polyphenol conjugates, especially solubility, thermal stability, emulsifying, gelling and antioxidant properties, are revisited. The information on potential applications of protein-polyphenol conjugates in emulsions, protein-based films, and protein gels, as well as conjugates-based delivery systems is also discussed and reviewed. Key findings and conclusions: The interaction of proteins and polyphenols mainly results from non-covalent (H-bonding, electrostatic interactions) or covalent bonds taking place mostly based on the oxidation of proteins or polyphenol by enzymatic or non-enzymatic pathways. Moreover, protein-polyphenol interaction greatly depends on environmental conditions such as temperature and pH as well as on the conformation or type of proteins and polyphenols. The protein-polyphenol conjugates with higher thermal stability, antioxidant activities, better emulsifying properties and enhanced gelling property can be used as novel food additives for improvement of functionalities and quality of food products.

International Journal of Food Science and Technology, 2019

Influences of different ultrasound treatments combined with heat pretreatment on enzymatic hydrol... more Influences of different ultrasound treatments combined with heat pretreatment on enzymatic hydrolysis, emulsifying properties and antioxidant activities of hydrolysates from duck egg albumen were studied. Heat pretreatment at 95 °C for 30 min inhibited both serine and cysteine protease inhibitors effectively. Ultrasonication of heated duck albumen at 60% amplitude for 10 min yielded the highest surface hydrophobicity. Coincidentally, aforementioned pretreatment rendered the hydrolysate with highest degree of hydrolysis (DH) than other pretreatments when Alcalase was used. The resulting hydrolysate showed the highest antioxidant activities including DPPH radical and ABTS radical cation scavenging activities and ferric reducing antioxidant power as well as emulsifying properties when hydrolysis time of 90 min was used. The hydrolysate possessed the peptides with molecular weight of 219-255 Da with the highest ABTS radical scavenging activity. Thus, heat pretreatment, followed by ultrasonication of duck albumen under appropriate condition could increase DH, antioxidant activities and emulsifying properties of duck albumen hydrolysate.

Journal of Texture Studies, 2019

The influences of salted duck egg albumen powder (SDEAP) as salt replacer at various levels (0.5-... more The influences of salted duck egg albumen powder (SDEAP) as salt replacer at various levels (0.5-2.5%) on autolysis and gelling properties of sardine surimi were investigated. SDEAP had high salt (33.67%) and protein contents (64.52%) with trypsin inhibitory activity of 5,975 kunits/g solid. SDEAP was white in color with L*-value of 96.72. It had low moisture content (3.98%) and water activity (0.38). Autolysis of sardine surimi was drastically inhibited when SDEAP was incorporated with increasing levels as indicated by the more retained myosin heavy chain and the reduced trichloroacetic acid-soluble peptide content. Breaking force and deformation of surimi gel increased, while expressible mois

Journal of Food Science and Technology, 2019

The demand for duck meat and eggs in Asian countries increases every year. Duck egg albumen has b... more The demand for duck meat and eggs in Asian countries increases every year. Duck egg albumen has become an important ingredient in the food industry alongside its hen counterpart, because of its excellent nutritive and functional properties. The major proteins in duck albumen are ovalbumin, ovomucoid, ovomucin, conalbumin, and lysozyme. Comparing with hen albumen, lower contents of ovalbumin, conalbumin, lysozyme and ovoflavoprotein are found in duck albumen. Nevertheless, duck albumen shows better gelling and foaming properties than hen albumen. During storage, duck albumen gel properties are enhanced, while foam volume and foam stability are decreased. Moreover, the changes in quality indices of duck egg including the thinning of the albumen, an increase in albumen pH, loss of water and carbon dioxide occur as storage time is increased. Some processes such as alkaline treatment also cause the loss in nutritive value of egg albumen. In this review, the composition and functional properties of duck albumen and how they are affected by processing conditions are also addressed, in comparison with hen albumen. A better understanding of duck egg albumen would be beneficial so that the food processing industry can exploit the potential of this avian protein.

Journal of Food Biochemistry, 2019

Egg albumen is a potential source of trypsin inhibitor (TI), which has been widely used to impro... more Egg albumen is a potential source of trypsin inhibitor (TI), which has been widely used
to improve textural property of surimi or surimi‐based food products. TI from duck
albumen was isolated and purified using ammonium sulfate precipitation at 20%–
40% saturation and affinity chromatography using trypsin‐CNBr‐activated Sepharose
4B column. TI was purified with purity and yield of 111.8‐fold and 0.6%, respectively.
The purity of inhibitor was confirmed using Native‐PAGE as indicated by the presence
of single band. Molecular weight of purified TI was 43 kDa based on SDS‐GAGE
and gel filtration. The purified TI remained unchanged at temperatures below 60°C
and the pH in the range of 7–9. The inhibitory activity of TI was decreased with the
addition of salt higher than 5%. Inhibition kinetic study revealed that purified TI from
duck albumen was uncompetitive inhibitor and the inhibition constant (Ki) was
508 nM. TI from duck egg albumen could serve as a food grade inhibitor for controlling
undesirable proteolysis.

Journal Texture Studies, 2018

The effects of desugarization using glucose oxidase/catalase and spray-drying conditions on gelli... more The effects of desugarization using glucose oxidase/catalase and spray-drying conditions on gelling properties of duck albumen powder were studied. Gelling temperatures increased as spray drying inlet temperatures (140–180C) were increased (p < .05). ΔE*, a*-, and b*- values of gel increased but L* and whiteness decreased when higher spray-drying temperatures were used (p < .05). However, whiteness and lightness of albumen gel were drastically increased after desugarization (p < .05). Texture profile analysis showed that hardness, springiness, gumminess, and chewiness of gel decreased with increasing spray-drying temperatures. Moreover, gel of freeze-dried desugarized albumen powder had higher hardness, springiness, gumminess, and chewiness than that of spray-dried nondesugarized counterpart (p < .05). Albumen gel prepared from desugarized albumen powder showed the compact network with more connectivity and
smaller voids than that from nondesugarized one as visualized by scanning electron microscopy, regardless of drying conditions. Prior desugarization could lower browning and increased gelling properties of duck albumen powder. Higher spray drying inlet temperature generally exhibited the adverse effect on properties of resulting albumen powder. Both desugarization and drying conditions had the profound influence on characteristics and textural property of duck egg albumen.

Drying Technology, 2018

Desugarization of duck albumen using glucose oxidase/catalase was optimized before drying. Optimu... more Desugarization of duck albumen using glucose oxidase/catalase was optimized before drying. Optimum condition for desugarization using response surface methodology was as follows: glucose oxidase 31.24 units and catalase 781 units/mL albumen and incubation time of 6.55 h at 30 C. Foaming capacity (FC) and foam stability (FS) were enhanced, while the solubility decreased after desugarization. This coincided with the increase in surface hydrophobicity (p<0.05). Higher trypsin inhibitory activity was found in freeze-dried albumen powder than spray-dried counterpart. Trypsin inhibitory activity was continuously decreased as the inlet temperature for spray-drying increased (p<0.05). Desugarization could increase FC and FS, but slightly decreased solubility of powders. No marked differences in protein patterns were observed in all the powders, regardless of desugarization and drying methods. L* of albumen powder decreased but DE, a*-, b*-values and browning index increased as spray-drying temperatures increased (p<0.05). Therefore, prior desugarization could lower browning and increased foaming property of duck albumen, particularly when spray-dried with inlet temperature of 160 C.

Korean Journal for Food Science of Animal Resources, 2018

Chemical compositions, trypsin inhibitory activity, and gelling properties of albumen from duck e... more Chemical compositions, trypsin inhibitory activity, and gelling properties of albumen from duck egg during salting of 30 days were studied. As the salting time increased, moisture content decreased, the salt content and surface hydrophobicity increased (p<0.05). Trypsin inhibitory activity and specific activity were continuously decreased throughout the salting time of 30 days (p<0.05). This coincided with the decrease in band intensity of inhibitor with molecular weight of 44 kDa as examined by inhibitory activity staining. Nevertheless, no differences in protein patterns were observed
in albumen during the salting of 30 days. Based on texture profile analysis, hardness,
springiness, gumminess, chewiness, and resilience of albumen gel decreased with
increasing salting time. Conversely, salted albumen gels exhibited higher cohesiveness
and adhesiveness, compared to those of fresh albumen. Scanning electron microscopic study revealed that gel of salted albumen showed the larger voids and less compactness. In general, salting lowered trypsin inhibitory activity and gelling property of albumen from duck egg to some extent. Nevertheless, the salted albumen with the remaining inhibitor could be an alternative additive for surimi or other meat products to prevent proteolysis.

International Journal of Food Properties, 2017

The effects of duck and hen albumens at different levels (1%–4%, w/w) on proteolysis and gel pro... more The effects of duck and hen albumens at different levels (1%–4%, w/w) on
proteolysis and gel properties of sardine (Sardinella albella) surimi were studied. The addition of both albumens into surimi resulted in the increases in breaking force and deformation, especially with increasing levels added (P < 0.05). Both albumens inhibited autolysis of surimi in a dose dependent manner as indicated by the lower TCA-peptide content and more retained myosin heavy chain and actin. Texture profile analysis showed that hardness, cohesiveness, springiness, gumminess and chewiness of surimi gel increased with increasing albumen levels. In general, breaking force, hardness, gumminess and chewiness of surimi gel added with duck albumen were higher than those added with hen albumen when the same level was used. Lightness and whiteness of gels added with albumen increased, particularly at higher amount of albumen. Surimi gel added with both albumens showed compact network with more connectivity and smaller voids than the control gel as visualized by scanning electron microscopy. Thus, duck albumen could be used to replace hen albumen for improvement of sardine surimi gel properties.

Journal of Food Science and Technology, 2018

Physicochemical properties, trypsin inhibitory activity, and gelling properties of albumen from d... more Physicochemical properties, trypsin inhibitory activity, and gelling properties of albumen from duck egg during 15 days of storage at 4 C and room temperature (28–30 C) were studied. As the storage time increased, Haugh unit and moisture content decreased, while the pH value increased (P<0.05). The rate of changes was lower at 4 C. Trypsin inhibitory activity in albumen from egg stored at 4 C was higher than that kept at room temperature throughout the storage time (P<0.05). Nevertheless, no differences in protein patterns were observed during the storage. Based on texture profile analysis, the highest hardness, gumminess, and chewiness were found at day 3 for room temperature and at day 6 for 4 C. Higher values were attained for eggs kept at 4 C. Conversely, albumen gels made from eggs stored at room temperature exhibited higher cohesiveness, adhesiveness, springiness, resilience than those kept at 4 C. The gels had the lowered whiteness when eggs were stored for a longer time, particularly at room temperature. Thus, storage condition directly affected the quality of albumen from duck egg.