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- 저자 : Aphichart Karnchanatat (검색결과 4 건)
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Pariyaphon Petnual,Polkit Sangvanich,Aphichart Karnchanatat 한국식품과학회 2010 Food Science and Biotechnology Vol.19 No.4
A Curcuma longa L. lectin was purified by aqueous extraction, 80% ammonium sulfate precipitation and ConA Sepharose affinity chromatography. Its specific activity was of 64,566 HU/mg protein for a yield of 41.2%total protein. The molecular weight is of 17.3 kDa. It has hemagglutinating activity against human blood group B,rabbit, mouse, rat, guinea pig, geese, and sheep erythrocytes. The optimum pH is between 6-7, and stable up to 40℃. Activity was stimulated by Ca2+ and Mn2+. The internal sequence indicated similarity with legume lectin family. Moreover, at concentration of 47 and 94 mg/0.3 ㎠ disc showed antifungal activity against Exserohilum turicicum,Fusarium oxysporum, and Colectrotrichum cassiicola. The minimal inhibitory concentration were 0.002, 0.005, 0.011,0.09, and 0.046 mg/mL Pseudomonas aeruginosa, Staphylococcus aureus, Bacillus subtilis, Escheriehia coli, and Candida albicans, respectively. Additionally, it contains a high α-glucosidase inhibitory activity with an IC50 of 8 mg/mL.
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Expression and characterization of Apis dorsata α-glucosidase III
Manlika Kilaso,Chanpen Chanchao,Jirattikarn Kaewmuangmoon,Aphichart Karnchanatat,Polkit Sangvanich 한국응용곤충학회 2011 Journal of Asia-Pacific Entomology Vol.14 No.4
α-Glucosidase III plays a major role in producing the monosaccharides in honey, mainly glucose and fructose,from sucrose in plant nectar. The honey from Apis dorsata is different and somewhat acidic compared to that of A. mellifera. The transcript expression level of the α-glucosidase III gene was evaluated by RT-PCR on total RNA extractions from eggs, larvae, pupae, and foraging imagoes. The highest expression level was found in foragers, which concurs with its biological function in honey bees as only foragers make honey. Using primers designed from the sequence of the A. mellifera α-glucosidase III gene, the full length ORF of the cDNA (1704 bp including the stop codon and 567 predicted amino acids) was obtained by RT-PCR of a total RNA preparation from foragers, and direct sequenced. BLASTn analysis revealed that the cDNA sequence showed the highest sequence similarity to the A. mellifera α-glucosidase III gene (96%). Enrichment of the native α-glucosidase III protein from forager bees was performed by ammonium sulfate precipitation at 95% saturation followed by diethylaminoethyl-cellulose ion exchange column chromatography of the unprecipitated fraction (yield and specific activity of 3.95 U/mg and 118.5%) followed by Superdex 75 ion exchange column chromatography to give a main protein and sole α-glycosidase activity band of ~63 kDa, with a yield of 5.57 U/mg and a specific activity of 19.5%. This enriched fraction had optimal pH, temperature, and substrate concentration for α-glucosidase activity of 4.5, 35 °C and 55 °C, and 50 mM maltose, respectively.
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Puttaporn Pongkai,Tanatorn Saisavoey,Papassara Sangtanoo,Polkit Sangvanich,Aphichart Karnchanatat 한국식품과학회 2017 Food Science and Biotechnology Vol.26 No.5
Tyrosinase is a copper-containing enzyme that controls mammalian melanogenesis. Tyrosinase inhibitors are important for their potential application in cosmetic products. Chicken feather meal is a rich source of amino acids, which have been linked with tyrosinase inhibition activity. This study investigated the tyrosinase inhibitory properties of protein hydrolysates prepared from chicken feather meal. Protein hydrolysates prepared by pepsinpancreatin with MW \3 kDa exhibited strong tyrosinase inhibition activity for both monophenolase (IC50 5.780 ± 0.188 lg/mL) and diphenolase activities (IC50 0.040 ± 0.024 lg/mL) in a cell-free mushroom tyrosinase system. These samples were uncompetitive inhibitors with Ki values of 18.149 and 27.189 lg/mL in monophenolase and diphenolase activities, respectively. A cell culture model showed that this hydrolysate had the strongest inhibition on the viability of B16F10 cells (IC50 1.124 ± 0.288 lg/mL) and 0.210 lg/mL of the sample exhibited inhibition of tyrosinase activity by 50.493% and melanin synthesis by 14.680% compared to the control.
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Tanatorn Saisavoey,Tanapat Palaga,Suchinda Malaivijitnond,Sukanya Jaroenporn,Nuttha Thongchul,Polkit Sangvanich,Aphichart Karnchanatat 한국식품과학회 2014 Food Science and Biotechnology Vol.23 No.4
The flavonoid contents of intact tubers and cellculture media were determined and physiological activitiesof Pueraria mirifica extracts were investigated. The totalflavonoid contents from cell culture media (PMC) werehigher than from tubers (PMT). Results from in vivoestrogenic activity assays indicated that PMT had a strongestrogenic activity in ovariectomized rats. The same amountof PMC exhibited a weak activity. In vitro osteoclastsuppression investigations indicated that both PMT andPMC extracts exhibited anti-osteoclastogenic activities withlow toxicities in a standard test cell line. Determination ofthe antioxidant potential using the DPPH assay revealedthat the IC50 value for PMT was lower than for PMC. P. mirifica cell cultures produce more flavonoids and exhibita mild estrogenic and more antioxidant activities than tubers.
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