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 14

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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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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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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.
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Impact of divalent salts and bovine gelatin on gel properties of phosphorylated gelatin from the skin of unicorn leatherjacket
(2014-01-01)
Kaewruang, Phanngam
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Benjakul, Soottawat
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Prodpran, Thummanoon
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Encarnacion, Angel B.
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Nalinanon, Sittipong
The impact of zinc chloride (ZnCl<inf>2</inf>) and calcium chloride (CaCl<inf>2</inf>) as well as bovine gelatin (BG) on the gel strength of phosphorylated fish gelatin (PFG) from the skin of unicorn leatherjacket was investigated. The gel strength of PFG increased with increasing concentrations of ZnCl<inf>2</inf> and CaCl<inf>2</inf> (2.5-40μmol L-1). A higher gel strength was observed with CaCl<inf>2</inf>, compared with ZnCl<inf>2</inf>. The gel strength of PFG with 20μmolL-1 CaCl<inf>2</inf> increased by 15.7%, compared to the control gel. Nevertheless, at higher concentration (40μmolL-1) of both salts, gel strength of PFG decreased. Hardness of gels decreased with increasing PFG content (P<0.05). Nevertheless, no differences in hardness were found amongst gels with BG/PFG ratios of 4:0 and 3:1 (P≥0.05). Thus, PFG could be used in combination with CaCl<inf>2</inf> to substitute for BG at a level of 25%. © 2013 Elsevier Ltd.
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Characteristics, Functional Properties, and Antioxidant Activities of Water-Soluble Proteins Extracted from Grasshoppers, Patanga succincta and Chondracris roseapbrunner
(2018-01-01)
Chatsuwan, Niphattha
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Nalinanon, Sitthipong
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Puechkamut, Yuporn
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Lamsal, Buddhi P.
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Pinsirodom, Praphan
Water-soluble proteins extracted from two species of grasshoppers, Patanga succincta (WSPP) and Chondracris roseapbrunner (WSPC), were characterized as well as their functional properties and antioxidant activities were investigated. The extraction yield, on a wet weight basis, was 7.35% and 7.46% for WSPP and WSPC, respectively. The most abundant amino acid in both proteins was glutamic acid, followed by aspartic, alanine, and leucine, in that order. The electrophoretic study revealed that proteins with MW of 29, 42, 50, 69, and 146 kDa were the major protein components in WSPP and WSPC. FTIR analysis showed that those proteins remained their structural integrity. The surface hydrophobicity at pH 7 of WSPC was higher than WSPP, but the sulfhydryl group content did not show significant difference between the proteins from two species. Both grasshopper proteins were mostly soluble in strong acidic and alkaline aqueous solutions with a minimum value at pH 4. Those proteins exhibited poor emulsifying properties and foaming capacity, but they had greater foaming stability compared with bovine serum albumin (BSA) (p<0.05). WSPC showed greater DPPH• and ABTS•+ scavenging activities and ferric-reducing antioxidant power (FRAP) than did WSPP (p<0.05). Therefore, based on characteristics and functional properties, water-soluble proteins from both edible grasshoppers can be used as an ingredient in food applications.
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Effects of Ya-nang leaves (Tiliacora triandra) powder on properties and oxidative stability of tilapia emulsion sausage during storage
(2015-01-01)
Sriket, P.
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Sriket, C.
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Nalinanon, S.
Effect of Ya-nang leaves (Tiliacora triandra) powder (YLP) (0.5-2.0%) on qualities and lipid oxidation of tilapia emulsion sausages during 21 days of refrigerated storage was investigated. Control sample had lower fiber content than samples added with YLP (p<0.05) at day 0 of storage. YLP treated samples (1.0-2.0%) revealed lower L* value but higher b* and ΔE* values, compared to the control samples (p<0.05). With the addition of YLP, peroxide value (PV) and thiobarbituric acid-reactive substances (TBARS) value in the sausages were retarded effectively, compared to control sample (p<0.05), especially when the YLP at high contents were used. Addition of YLP were also effective in retarding the formation of fishy odor in the samples, compared to control sample (p<0.05). Samples treated with YLP had higher hardness and springiness, compared with control sample during storage (p<0.05). YLP had no detrimental effect on the sensory attributes of sausages. This study pointed out that YLP can be utilized in sausages to enhance quality.
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Production of collagen hydrolysate with antioxidant activity from pharaoh cuttlefish skin
(2016-05-01)
Bousopha, Sophawan
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Nalinanon, Sitthipong
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Sriket, Chodsana
The aim of this study was to produce collagen hydrolysate with antioxidant activity. Pepsin soluble collagen (PSC) isolated from the skin of Pharaoh cuttlefish (Sepia pharaonis) was used as a substrate for hydrolysis at 25°C and pH 7.5 by using collagenase from Clostridium histolyticum. The result showed that rapid hydrolysis was observed within the first 90 min with a degree of hydrolysis (DH) approaching 35%. Thereafter, a slower rate of hydrolysis was generally observed. An increase in DH was generally observed with increasing enzyme concentration. When log10 (collagenase concentration) versus DH (%) was plotted, a linear relationship was found with a coefficient of determination (R2) of 0.9863. Electrophoretic study of collagen hydrolysates with 10% DH, 20% DH, and 30% DH revealed that their major peptides had molecular weights (Mr) ranging from 6.5 to 10.3 kDa; and 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,2-diphenyl-1-picryl hydrazyl (DPPH) radical scavenging activities. The ferric reducing activity power (FRAP) of collagen hydrolysates with 20% DH and 30% DH were similar (p > 0.05). Chelating activity of collagen hydrolysates with 20% DH was negligible and for 10% DH and 30% DH it was not detectable. Given these findings, Pharaoh cuttlefish skin, a byproduct of cuttlefish processing, is a promising source material for production of collagen hydrolysate with antioxidant activities.
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Changes in lipids and fishy odour development in skin from Nile tilapia (Oreochromis niloticus) stored in ice
(2013-01-01)
Sae-Leaw, Thanasak
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Benjakul, Soottawat
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Gokoglu, Nalan
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Nalinanon, Sitthipong
Changes in lipids, lipoxygenase activity and fishy odour development in the skin of Nile tilapia (Oreochromis niloticus) during iced storage of 18 days were monitored. Triacylglycerol content of skin decreased with coincidental increases in free fatty acid, monoacylglycerol, diacylglycerol and phospholipid contents during storage (p < 0.05). During iced storage, peroxide value increased at day 9 and subsequently decreased up to 18 days (p < 0.05). Thiobarbituric acid reactive substances values and lipoxygenase activity increased throughout 18 days of iced storage (p < 0.05). With increasing storage time, a progressive formation of hydroperoxide was found as evidenced by the increase in amplitude of peak at 3600- 3200 cm-1 in Fourier transform infrared spectra. Those changes indicated that lipid oxidation took place during iced storage. The increase in fishy odour of skin was observed as the storage time increased. The development of fishy odour in Nile tilapia skin during iced storage was mostly governed by lipid oxidation via autoxidation or induced by lipoxygenase. Thus, the extended storage time of whole fish resulted in the pronounced changes in lipids and the increased fishy odour in the skin. © 2013 Elsevier Ltd.

Nalinanon, Sitthipong

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