Nalinanon, Sitthipong

Preferred name

Alternative Name

Nalinanon, S.

Nalinanon, Sittipong

Main Affiliation

School of Food Industry

sitthipong.na@kmitl.ac.th

Now showing 1 - 10 of 44

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Pulsed electric field-assisted extraction of Djenkol (Archidendron pauciflorum) peel: Characterization, suppression of intracellular ROS generation and inflammatory cytokines in LPS-activated RAW264.7 macrophage cells
(2024-06-01)
Sinthusamran, Sirima
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Chotphrethipong, Lalita
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Benjakul, Soottawat
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Hutamekalin, Pilaiwanwadee
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Champoochana, Nidanut
Djenkol (Archidendron pauciflorum) peel is a source of phenolics with an antioxidative activity. Nevertheless, the high extraction efficacy of the target compounds is crucial for the isolation of such compounds. Pulsed electric field (PEF)-assisted extraction is the means that increase the efficacy of extraction via an electroporation mechanism. This research aimed to study the extraction of phenolics with antioxidative activities using the PEF and to investigate the anti-inflammation and antioxidative activities of the Djenkol peel extract (DPE) in RAW264.7 macrophage cells. The PEF at different electric field strengths (E) (4.5 and 6 kV/cm) and times (180, 360, and 540 ms) was implemented to extract the phenolic compounds. The PEF with the E level at 6 kV/cm for 540 ms provided the highest yield, the total phenolic content, and antioxidative activities, compared to other conditions (P < 0.05). The dominant compounds in the DPE were the gallic acid and catechin. When the RAW264.7 cells were treated with the DPE at different levels (0.125, 0.25, 0.5, 0.75 and 1 μg/mL), the DPE at 0.125 and 0.25 μg/mL had no cytotoxicity, compared to the control (P < 0.05). With adding lipopolysaccharide (LPS), the DPE-treated cells at 0.125 μg/mL showed the similar cell viability to that of the control (P < 0.05). Additionally, the use of the DPE, particularly at 0.125 and 0.25 μg/mL, could reduce the TNF-α and IL-6 levels and reactive oxygen species (ROS) generation in the LPS-activated cells. Thus, the DPE could be used as a functional ingredient in food.
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Ultrasonic-assisted preparation and characterization of sheepskin gelatin films modified with konjac glucomannan
(2026-12-01)
Hasdar, Muhamad
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Nalinanon, Sitthipong
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Kittiphattanabawon, Phanat
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Sriket, Chodsana
Gelatin derived from sheepskin (GSS) is a promising biomaterial for edible, biodegradable films, but exhibits poor water resistance, mechanical weakness, and brittleness. This study developed ultrasound-assisted composite films based on GSS and konjac glucomannan (KG; 0–75% w/w) to enhance their functionality. The ultrasonic treatment (40 kHz, 15 min) improved homogeneity and reduced structural defects. KG incorporation significantly increased film thickness from 0.031 mm to 0.038 mm and tensile strength from 0.5118 MPa to 0.9601 MPa, while reducing water vapor transmission from 2.6974 g m⁻² day⁻¹ to 1.7304 g m⁻² day⁻¹ and water activity from 0.4526 to 0.3084. Swelling decreased from 4.77% to 3.82%, whereas water resistance improved from 95.23% to 96.18%. The optimal formulation (25% KG) provided a balance between strength, flexibility, and hydrophobicity. FTIR confirmed intermolecular hydrogen bonding between GSS and KG, and ultrasound promoted uniform dispersion and denser microstructures. These findings highlight ultrasound-assisted GSS/KG films as sustainable, protein-polysaccharide-based materials with superior physicochemical and barrier properties for eco-friendly food packaging applications.
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Production of fiber hydrolysate from bamboo shoot with antioxidative properties by enzymatic hydrolysis
(2019-06-04)
Karnjanapratum, Supatra
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Kaewthong, Pensiri
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Takeungwongtrakul, Sirima
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Sae-Leaw, Thanasak
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Hong, Jeong Hwa
Bamboo shoots possess a rich source of dietary fiber for Asian countries as well as Thailand, which give various beneficial physiological effects for human beings. Dietary fibers in soluble form could provide better texture and would be easier to apply in food products. This study aimed to prepare fiber hydrolysate with high solubility and antioxidant activity from bamboo (Bambusa vulgaris) shoot. The fiber hydrolysate from bamboo shoot (FHBS) was prepared by stepwise enzymatic hydrolysis including amylase (1%, w/w), cellulase (1, 2, 3%, w/w) and papain (1%, w/w). The released fiber yield of FHBS increased with increasing cellulose levels in dose dependent manner (P≤0.05). It was found that the process with 1% (w/w) amylase for 1 h and 3% (w/w) cellulase for 3 h followed by 1% (w/w) papain for 1 h at 50 ºC, rendered the highest released fiber yield (92.10±1.10%). The resultant FHBS contained 5.76±0.21 % of total dietary fiber with total sugar and reducing sugar contents of 1431.22±46.01 and 918.91±10.57 mg/g solid, respectively. The FHBS exhibited antioxidant activities including ABTS radical scavenging activities (ABTS), DPPH radical scavenging activities (DPPH), ferric reducing antioxidant power (FRAP) and oxygen radical absorbance capacity (ORAC). Therefore, FHBS with antioxidant activities could be effectively prepared by using enzymatic hydrolysis and suitable to apply in the fiber fortified products.
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Evaluation of yellow mealworm (Tenebrio molitor) larvae protein extract as a cryoprotectant for frozen Pacific white shrimp
(2026-06-15)
Kittiphattanabawon, Phanat
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Sriket, Chodsana
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Nalinanon, Sitthipong
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Phaonakrop, Narumon
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Roytrakul, Sittiruk
This study evaluated the application of yellow mealworm ( Tenebrio molitor ) larvae protein extract (YMPE) as a clean-label cryoprotectant for frozen Pacific white shrimp ( Litopenaeus vannamei ), with emphasis on its underlying mechanism. Proteomic profiling identified 12 antifreeze protein-like peptides containing conserved ice-binding motifs (TCTxSxxCxxAx), supporting the cryoprotective potential of YMPE. During dose optimization, shrimp treated with 0.5% YMPE exhibited the highest weight gain (5.57%) and lowest freezable water content (59.67%) (P < 0.05). The cryoprotective efficacy of YMPE was further evaluated over five freeze–thaw cycles in comparison with distilled water and mixed phosphate. YMPE significantly mitigated quality deterioration by enhancing water retention, preserving protein functionality (higher Ca2+-ATPase activity), and reducing lysosomal enzyme leakage relative to the control (P < 0.05). Microstructural analysis revealed reduced muscle fiber disruption, characterized by fewer inter-fiber gaps. Mechanistically, YMPE may exert cryoprotective effects through a multimodal mechanism involving ice recrystallization inhibition and formation of a protective protein matrix. Although less effective than mixed phosphate, YMPE consistently improved all quality parameters compared with the control. These findings highlight the potential of insect-derived protein extracts as a novel, biologically based alternative to phosphate additives in seafood processing and provide a foundation for future industrial application.
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Development of djenkol peel extract-loaded liposome as functional food ingredients: Physicochemical characteristic, antioxidant activities, and cytotoxicity
(2025-06-01)
Chotphruethipong, Lalita
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Sinthusamran, Sirima
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Benjakul, Soottawat
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Senphan, Theeraphol
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Nalinanon, Sitthipong
Djenkol peel is an agricultural by-product containing valuable bioactive compounds. The direct use of its extract faces challenges related to stability and sensory acceptance. This study aimed to investigate the effect of djenkol peel extract (DPE) on the encapsulation efficiency (EE) using liposomes. The physicochemical properties, antioxidant activities, and cytotoxicity of the obtained liposomes were evaluated. DPE (0, 0.25, 0.50, 0.75, and 1.00 %, w/v) was encapsulated using phospholipid/cholesterol as the wall material. The highest EE (66.69 %) was observed in the liposomes loaded with 0.25 % (w/v) DPE (LE-0.25DPE) (P < 0.05). All DPE-loaded liposomes displayed nanometer-scale particle sizes (78.94–135.60 nm) and negative zeta potentials (−52.60 to −57.50 mV). Encapsulation of DPE in liposomes can mask its undesirable color. Fourier-transform infrared spectroscopy (FTIR), transmission electron microscopy (TEM), and differential scanning calorimetry (DSC) revealed changes in the physicochemical and thermal properties of LE-0.25DPE. Additionally, LE-0.25DPE showed increased DPPH radical-scavenging activity (DPPH-RSA) and ferric reducing antioxidant power (FRAP) in a dose-dependent manner (250–2000 μg/mL). In vitro Caco-2 cell viability test, LE-0.25DPE at 0.1–1 μg/mL exhibited no cytotoxicity compared to the control (P < 0.05). Thus, DPE-loaded liposomes demonstrate potential as a functional food ingredient with high bioactivity.
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Lipid oxidation and fishy odour development in protein hydrolysate from Nile tilapia (Oreochromis niloticus) muscle as affected by freshness and antioxidants
(2012-06-15)
Yarnpakdee, Suthasinee
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Benjakul, Soottawat
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Nalinanon, Sitthipong
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Kristinsson, Hordur G.
Lipid oxidation and fishy odour development in protein hydrolysate from fresh and ice-stored Nile tilapia (Oreochromis niloticus) were investigated. During iced storage of 18 days, heme iron content decreased with a concomitant increase in non-heme iron content (P < 0.05). Peroxide value (PV) and thiobarbituric acid reactive substances (TBARS) values increased. Phospholipid content decreased with a corresponding increase in free fatty acid content. The results suggested that lipid hydrolysis and oxidation took place during storage. When protein hydrolysates were produced from fresh and 18 days ice-stored Nile tilapia muscle, higher lipid oxidation and fishy odour/flavour along with higher amount volatile compounds were obtained in hydrolysate for unfresh sample (P < 0.05). However, the addition of mixed antioxidants during hydrolysis process markedly lowered lipid oxidation, b ·, ΔC ·, ΔE · values, fishy odour/flavour as well as the formation of volatile compounds in the resulting hydrolysates prepared from both fresh and unfresh samples. Therefore, hydrolysate from Nile tilapia muscle with reduced fishy odour and lighter colour could be prepared by using fresh fish and incorporation of mixed antioxidants during hydrolysis. © 2011 Elsevier Ltd. All rights reserved.
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Cold-adapted structural properties of trypsins from walleye pollock (Theragra chalcogramma) and Arctic cod (Boreogadus saida)
(2011-12-01)
Kanno, Gaku
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Kishimura, Hideki
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Yamamoto, Jun
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Ando, Seiichi
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Shimizu, Takeshi
Complementary DNA clones encoding trypsins were isolated from pyloric ceca of cold-adapted fish, walleye pollock (Theragra chalcogramma) (WP-T) and Arctic cod (Boreogadus saida) (AC-T). The isolated full-length cDNA clones of WP-T and AC-T were 852 and 860 bp, respectively, and both cDNAs were contained an open reading frame of 726 bp. WP-T and AC-T seemed to be synthesized as preproenzyme that contains a signal peptide, an activation peptide, and a mature trypsin. Although the amino acid sequence identities of WP-T and AC-T to that of bovine trypsin were 64 and 63%, respectively, they completely conserved the structural features for catalytic function of trypsin. On the other hand, WP-T and AC-T possessed the four Met residues (Met135, Met145, Met175 and Met242) in their molecules and the deletion of Tyr151 and substitution of Pro152 for Gly in their autolysis loops when aligned with the sequences of tropical-zone fish and bovine trypsins. In addition, the contents of charged amino acid residues at the N-terminal regions (positions 20-50) of WP-T and AC-T were extremely higher than those of other fish and bovine trypsins. Moreover, one amino acid (Asn72) and two amino acids (Asn72 and Val75) coordinating with Ca2+ in bovine trypsin were exchanged for another amino acids in WP-T (His) and AC-T (His and Glu), respectively, and the contents of negative charged amino acids at their Ca2+-binding regions were lower than those of tropical-zone fish and bovine trypsins. Therefore, it was considered that these structural characteristics of WP-T and AC-T are closely related to their lower thermostability. © 2011 Springer-Verlag.
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Impact of extraction condition on the yield and molecular characteristics of collagen from Asian bullfrog (Rana tigerina) skin
(2022-06-01)
Indriani, Sylvia
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Benjakul, Soottawat
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Kishimura, Hideki
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Karnjanapratum, Supatra
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Nalinanon, Sitthipong
The present study is the first report on collagen extraction as acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC), which could maximize the exploitation of Asian bullfrog (Rana tigerina) skin as an alternative collagen material in food and pharmaceutical fields. Extraction methods for ASC and PSC from Asian bullfrog skin were developed using different concentrations of acetic acid (0.50, 0.75, and 1.00 M) and pepsin (1.00, 2.00, and 3.00% [w/w]). PSCs exhibited a higher extraction yield (22.59%–28.30%) and recovery (22.48%–31.12%) than ASCs. An electrophoretic study revealed that collagens possessed type I collagen. ASC with 0.75 M acetic acid (ASC-0.75) and PSC with 3.00% (w/w) pepsin (PSC-3.00) were selected and analysed on their solubility, molecular characteristics, and amino acid composition. A better solubility with a higher isoelectric point was observed for PSC-3.00 than ASC-0.75. Fourier transform infrared- and circular dichroism-spectra revealed a high-interacted compact structure with a triple helical-structure of the collagen peptides, respectively. A similar amino acid profile with a high imino acid content was observed. Therefore, collagens from Asian bullfrog skin were successfully extracted, where the optimized conditions provided a high yield with less adverse effects on collagen properties and molecular characteristics.
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Autolysis of clown featherback (Chitala ornata) muscle
(2019-01-01)
Thiabmak, Chompunutch
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Sriket, Chodsana
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Yarnpakdee, Suthasinee
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Kim, Siriporn Riebroy
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Nalinanon, Sitthipong
Clown featherback (Chitala ornata) is a freshwater fish important in the cuisine of Thailand and other Southeast Asian countries. It has a short marketable life due mainly to poor gelling characteristic even when stored in ice. This deterioration has been associated with muscle autolysis. The research was aimed to investigate the autolysis of clown featherback muscle (CFM). To test autolysis, mince from CFM was incubated in a temperature controlled water bath for 60 min at 5, 10, 20, 30, 40, 50, 60, 65, 70, 75 or 80 °C at pH levels over the range of 2-11. The results showed that the highest autolytic activity was at 70 °C and it occurred at pH levels of 4 and 7, with pH 4 showing the highest autolysis. CFM was incubated with its crude enzyme counterpart at the physiological pH (6.73) at both 4 °C and 25 °C. Degradation of natural actomyosin showed that after incubation at either temperature myosin heavy chain was susceptible to hydrolysis indicating that autolysis of CFM took place even at low temperature as affected by its endogenous proteases. The effects of several protease inhibitors were tested and autolysis at the physiological pH (6.73) was strongly inhibited by 10 μM pepstatin A (20.3% inhibition), which had significantly higher inhibitory activity (P < 0.05) among the protease inhibitors tested. This suggests that aspartic protease was the major proteinase in CFM.
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Characteristics of pepsin-solubilised collagen from the skin of splendid squid (Loligo formosana)
(2015-01-01)
Kittiphattanabawon, Phanat
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Nalinanon, Sitthipong
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Benjakul, Soottawat
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Kishimura, Hideki
Pepsin-solubilised collagen from the skin of splendid squid (SC) was isolated, partially purified by salt precipitation and dialysis prior to characterisation. The yield of SC was 75.3% (dry weight basis). SC with high purity was obtained as shown by the distinct UV absorption peak at 232 nm and high hydroxyproline content. Total sugar content of SC was 4.70% (dry weight basis), which was higher than that of collagen from calf skin (CC) (1.45% dry weight basis) (P < 0.05). Based on SDS-PAGE and elution profile, SC might contain the mixed types of collagen (type SQ-I and type SQ-II), in which α- and β-chains were the major components. SC was rich in glycine and had high content of imino acids (189 residues/1000 residues). The degradation induced by chymotrypsin and lysyl endopeptidase was more pronounced in CC, compared with SC. The maximum transition temperature (T m a x) of SC was 34.1°C, which was about 7°C lower than that of CC. Fourier transform infrared spectra revealed that the triple-helical structure of SC was predominant with the copresence of carbohydrate moieties. Therefore, the skin of splendid squid, a byproduct from squid processing, can be an alternative source for collagen production.

Nalinanon, Sitthipong

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