Thermostable α-amylase from germinating Sword bean ( (Jacq.) DC.) seeds has been successfully immobilized on DEAE-cellulose (ICgAmy1) and chitosan bead (ICgAmy2) support materials.
View Article and Find Full Text PDFThe plasma and serum of Crocodylus siamensis have previously been reported to exhibit potent antimicrobial, antioxidant, and anti-inflammatory activities. During wound healing, these biological properties play a crucial role for supporting the formation of new tissue around the injured skin in the recovery process. Thus, this study aimed to evaluate the wound healing properties of C.
View Article and Find Full Text PDFBiochem Genet
December 2014
Heteroscorpine-1 (HS-1) was identified as a member of the scorpine family. HS-1 shows insecticidal activities, exhibiting a low median lethal dose (LD50) in mealworm (Tenebrio molitor L.) and inhibitory activities against Bacillus subtilis, Klebsiella pneumoniae, and Pseudomonas aeruginosa.
View Article and Find Full Text PDFCrocodylus siamensis hemoglobin was purified by a size exclusion chromatography, Sephacryl S-100 with buffer containing dithiothreitol. The purified Hb was dissociated to be two forms (α chain and β chain) which observed by SDS-PAGE, indicated that the C. siamensis Hb was an unpolymerized form.
View Article and Find Full Text PDFBackground: The Siamese crocodile (Crocodylus siamensis) is a critically endangered species of freshwater crocodiles. Crocodilians live with opportunistic bacterial infection but normally suffer no adverse effects. They are not totally immune to microbial infection, but their resistance thereto is remarkably effective.
View Article and Find Full Text PDFAn antibacterial compound from crocodile blood was partially purified and functionally characterised. The freshwater crocodile (Crocodylus siamensis) plasma with antibacterial activity was partially purified by using a centrifugal concentrator and reverse phase high powered liquid chromatography, and designated as crocosin. Crocosin exhibits antibacterial activity toward Salmonella typhi and Staphylococcus aureus.
View Article and Find Full Text PDFComp Biochem Physiol C Toxicol Pharmacol
January 2010
Peptide fragments possessing antimicrobial activity were obtained by protease digestion of goose egg white lysozyme. Digested peptide purified from RP-HPLC which showed no lysozyme activity exhibited bactericidal activity toward Gram-negative and Gram-positive bacteria. LC/MS-MS and automated Edman degradation revealed the amino acid sequence to be Thr-Ala-Lys-Pro-Glu-Gly-Leu-Ser-Tyr.
View Article and Find Full Text PDFComp Biochem Physiol B Biochem Mol Biol
June 2007
Two lysozymes were purified from quail egg white by cation exchange column chromatography and analyzed for amino acid sequence. The enzymes showed the same pH optimum profile for lytic activity with broad pH optima (pH 5.0-8.
View Article and Find Full Text PDFComp Biochem Physiol C Toxicol Pharmacol
June 2006
Cation exchange column chromatography and gel filtration chromatography were used to purify four reptile lysozymes from egg white: SSTL A and SSTL B from soft shelled turtle (Trionyx sinensis), ASTL from Asiatic soft shelled turtle (Amyda cartilagenea) and GSTL from green sea turtle (Chelonia mydas). The molecular masses of the purified reptile lysozymes were estimated to be 14 kDa by SDS-PAGE. Enzyme activity of the four lysozymes could be confirmed by gel zymograms and showed charge differences on native-PAGE.
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