Nalinanon, Sitthipong

Preferred name

Alternative Name

Nalinanon, S.

Nalinanon, Sittipong

Main Affiliation

School of Food Industry

sitthipong.na@kmitl.ac.th

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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
;
Kishimura, Hideki
;
Yamamoto, Jun
;
Ando, Seiichi
;
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 Ca<sup>2+</sup> 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 Ca<sup>2+</sup>-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
;
Benjakul, Soottawat
;
Kishimura, Hideki
;
Karnjanapratum, Supatra
;
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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Characteristics of pepsin-solubilised collagen from the skin of splendid squid (Loligo formosana)
(2015-01-01)
Kittiphattanabawon, Phanat
;
Nalinanon, Sitthipong
;
Benjakul, Soottawat
;
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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Elucidating the physicochemical and structural properties of Ganoderma lucidum spores: Comparative analysis of various disruption techniques
(2024-04-15)
Sriket, Chodsana
;
Kuimalee, Surasak
;
Yarnpakdee, Suthasinee
;
Benjakul, Soottawat
;
Sriket, Pornpimol
This study evaluated Ganoderma lucidum G2 spores (GLS) using various processing techniques: vibrating milling, ball milling, and autoclaving. Broken GLS via vibrating and ball milling showed higher lipid content (22.89% and 22.50%) but lower L*, a*, and b* values compared to intact GLS. Vibrating milling achieved the highest sporoderm-broken rate (98.27%). Ball milling resulted in the highest lipid oxidation. Vibrating milling yielded the highest bioactive compounds, and both methods increased DPPH-RSA values. Differential scanning calorimetry indicated varying T<inf>max</inf> values: non-broken GLS (106.56 °C), vibrating milling (92.77 °C), ball milling (97.58 °C), and autoclaving (109.35 °C). FT-IR spectra showed triterpenes, polysaccharides, and fatty acids. X-ray diffraction and Fourier transform infrared spectroscopy revealed increased crystallinity with vibrating milling (37.12% to 47.99%). Both milling methods altered GLS structure to a disintegrated, pancake-like form. Scanning electron microscopy with energy-dispersive X-ray spectroscopy indicated significant carbon and oxygen concentrations. This study provided crucial insights for utilizing GLS.
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Characterization of acid soluble collagen from the skin of snakeskin gourami (Trichogaster Pectoralis)
(2020-01-01)
Sukkon, Piyaporn
;
Ali, Ali Muhammed Moula
;
Nalinanon, Sitthipong
;
Kishimura, Hideki
;
Takeungwongtrakul, Sirima
The present study was aimed to isolate and characterized acid soluble collagen (ASC) from the skin of snakeskin gourami (Trichogaster pectoralis). ASC from gourami skin had a yield of 9.43% and 34.65%, based on wet and dry weight basis, respectively. The purity of ASC was superior with a distinct absorption peak at wavelength (WL) of 230.7 nm. Based on the electrophoretic pattern, gourami skin ASC was classified as type I collagen, as it comprised α1 and α2 as major components and higher molecular weight (MW) components γ, β were distinctly observed. ASC exhibited high Tmax value of 33.43°C, which could correspond to its imino acids content of 188 residues/1000 residues. Fourier transform infrared (FTIR) spectrum and circular dichroism (CD) revealed that ASC extracted from gourami skin had greater structural integrity in its triple-helical form. Solubility of ASC was high at the pH range of 2-4 in which zeta potential exhibited highly positive charge. The highest solubility of ASC in the presence of NaCl was observed at 2% (w/v). Therefore, with all the characteristic features, ASC from snakeskin gourami skin can be a valueadded product in the fish processing industry.

Nalinanon, Sitthipong

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