• Archives of Pharmacal Research
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• v.9 no.1
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• pp.39-43
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• 1986

Bovine serum albumin microspheres containing cytarabine were prepared using cross-linking agent, formaldehyde. The shape and the size distribution of them were observed. The shape of them was spherical and the susrface was compact and smooth. The size distribution of them was affected by dispersion forces during emulsfication. The release of cytarabine from albumin microspheres was dependent upon cross-linking time, amount of cross-linking agent and drug/albumin ratio. However, the difference of drug release by the dispersion forces was not great. After release test, the shape of albumin microspheres was nonspherical and the albumin matrix seemed to be a little relaxed. The degradation tests of albumin microspheres by the proteolytic enzyme showed that albumin microspheres were progressively digested according to the cross-linking degree.

• Preventive Nutrition and Food Science
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• v.3 no.4
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• pp.303-308
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• 1998

Influence of amylose content on formation and characteristics of enzyme-resistant starch (RS) was investigated by scanning electron microscopy, X-ray diffractometry and differential scanning calorimetry. RS yield increased up to 36.1 % as the amylose content of corn starch increased. Starch granules of Amyulomaize V and Ⅶ were more rounded and smaller than those of regular corn ; some were elongated and had appendages. After autoclaving -cooling cycles, the granular structure disappeared and a continous spongy-like porous network was visible in regular corn starch ; the granular structure was stillevident in parts in Amylomaize V and Ⅶ starches. In all isolated RS residues , the porous structures were no longer visible and more compact formations predominated. While regular corn starch showed an A-type X-ray profile, Amylomaize V and Ⅶ starches exhibited a combination of B- and V-types. Regular corn starch lost most of its crystallinity during autoclaving , but the crystallinity was still left in Amylomaize starches as diffuse or poor B-types. All RS residues showed the presence of poor B-type regardless of amylose contents. Transition temperatures and enthalypy of native starches were a little higher in Amylomaize V and Ⅶ starches than those of regular corn starch . Regardless of amylose contents, all RS residues exhibited an endothermic transition over a similar temperature range (135 $^{\circ}C$~169$^{\circ}C$), with a mean peak temperature of ~154$^{\circ}C$, which is generally foud for retrograded amylose crystallities. Higher transition temperature, enthalypy, and RS yield of AMylomaize V and Ⅶ starches were related granular stability shown by the microscopic and crystallographic studies.

• Food Science of Animal Resources
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• v.37 no.5
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• pp.635-645
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• 2017

In this study, effect of transglutaminase (TGase) addition on physical, water barrier, optical and mechanical properties of mechanically deboned chicken meat protein (MDCM-P) films was investigated. When TGase was added to the films, the thickness increased, but the solubility decreased. Films treated with TGase exhibited higher water vapor permeability than control film (p<0.05). When TGase concentration increased, the $L^*$ values of films decreased, but $a^*$ and $b^*$ values increased. All films showed very good barrier properties against UV light. The highest tensile strength was obtained in MDCM-P films containing 3% TGase (p<0.05). The elongation at break values increased with the TGase concentration increasing from 1 to 3%, but decreased at higher enzyme concentration (p<0.05). The addition of TGase altered molecular organization and intermolecular interaction in the film matrix. TGase treated films showed smoother and ordered surface structure and homogeneous and compact microstructure. The results indicated that TGase use can be an effective approach in improving the solubility and mechanical properties of MDCM-P films.

• Journal of Microbiology and Biotechnology
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• v.25 no.9
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• pp.1433-1441
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• 2015

Pollution resulting from the discharge of textile dyes into water systems has become a major global concern. Because peroxidases are known for their ability to decolorize and detoxify textile dyes, the peroxidase activity of Vitreoscilla hemoglobin (VHb) has recently been studied. It is found that VHb and variants of this enzyme show great promise for enzymatic decolorization of dyes and may play a role in achieving their successful removal from industrial wastewater. The level of VHb peroxidase activity correlates with two amino acid residues present within the conserved distal pocket, at positions 53 and 54. In this work, sitedirected mutagenesis of these residues was performed and resulted in improved VHb peroxidase activity. The double mutant, Q53H/P54C, shows the highest dye decolorization and removal efficiency, with 70% removal efficiency within 5 min. UV spectral studies of Q53H/P54C reveals a more compact structure and an altered porphyrin environment (λ_Soret = 413 nm) relative to that of wild-type VHb (λ_Soret = 406), and differential scanning calorimetry data indicate that the VHb variant protein structure is more stable. In addition, circular dichroism spectroscopic studies indicate that this variant's increased protein structural stability is due to an increase in helical structure, as deduced from the melting temperature, which is higher than 90℃. Therefore, the VHb variant Q53H/P54C shows promise as an excellent peroxidase, with excellent dye decolorization activity and a more stable structure than wild-type VHb under high-temperature conditions.

• Journal of Life Science
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• v.18 no.1
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• pp.103-108
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• 2008

An agar-degrading marine bacterium, strain AS-1 was isolated from the seawater. The strain AS-1 was identified as Sphingomonas paucimobilis (90% probability) by VITEK. The optimum medium for agarase activity of the isolated strain was determined to be marine medium, marine broth 2216 containing 0.1% agar as carbon source. An extracellular agarase was purified 104-fold from the culture supernatant by ammonium sulfate precipitation, ion exchange chromatography and gel filtration methods. The molecular weight of the purified enzyme was estimated to be 80 kDa by SDS-PAGE. The optimum pH and temperature for activity were 7.0 and $40^{\circ}C$, respectively. Antioxidative activity of the strain AS- was 72% in the supernatant cultured for 12 h. The culture supernatant of the strain AS-1 showed antibacterial activity against bacteria causing putrefaction and food poisoning such as Escherichia coli, Staphylococcus aureus and Proteus vulgaris. However, the cell growth of the lactic aicd forming strain, Lactobacillus plantarium was promoted by the treatment of 10% culture supernatant of an agar-degrading strain.