• 한국염색가공학회지
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• 제29권4호
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• pp.181-194
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• 2017

The biodegradability of polylactic acid(PLA) fabrics was evaluated by two methods: enzyme and soil degradation. Three different enzymes were selected to evaluate. Degradation times were measured at optimal enzyme treatment conditions. Biodegradation by enzymatic hydrolysis was compared with soil degradation. As a result, biodegradation created cracks on the fiber surface, which led to fiber thickening and shortening. In addition, new peak was observed at $18.5^{\circ}$ by degradation. Moreover, cracks indicating biofragmentation were confirmed by enzyme and soil degradation. By enzyme and soil degradation, the weight loss of PLA fabrics was occurred, there through, the tensile strength decreased about 25% by enzyme hydrolysis when 21 days after, and 21.67% by soil degradation when 60 days after. Furthermore, the biodegradability of PLA fabrics by enzymatic and soil degradation was investigated and enzymatic degradation was found to be superior to soil degradation of PLA fabrics. Among the three enzymes evaluated for enzymatic degradation, alcalase was the most efficient enzymes. This study established the mechanism of biodegradation of PLA nonwovens, which might prove useful in the textile industry.

• 한국환경과학회지
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• 제11권12호
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• pp.1315-1320
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• 2002

Since the enzymatic degradation of microbial poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate] (P(3HB-co-3HV)) initially occurs by a surface erosion process, a degradation behavior could be controlled by the change of surface property. In order to control the rate of enzymatic degradation, plasma gas discharge and blending techniques were used to modify the surface of microbial P(3HB-co-3HV). The surface hydrophobic property of P(3HB-co-3HV) film was introduced by CF$_3$H plasma exposure. Also, the addition of small amount of polystyrene as a non-degradable polymer with lower surface energy to P(3HB-co-3HV) has been studied. The enzymatic degradation was carried out at 37 $^{\circ}C$ in 0.1 M potassium phosphate buffer (pH 7.4) in the presence of an extracellular PHB depolymerase purified from Alcaligenes facalis T1. Both results showed the significant retardation of enzymatic erosion due to the hydrophobicity and the enzyme inactivity of the fluorinated- and PS-enriched surface layers.

• Macromolecular Research
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• 제16권7호
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• pp.651-658
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• 2008

Poly(butylene succiate) (PBS), poly(butylene succinate-co-L-lactate) (PBSL), and poly(butylene succinate-co-6-hydroxycaproate) (PBSCL) polymers were degraded by lipase $PS^{(R)}$, and the enzymatic degradation mechanism of PBS was analyzed in detail. The enzymatic degradation of PBS gave 4-hydroxybutyl succinate (4HBS) as the main product. An exo-type hydrolysis mechanism was proposed based on this observation. The terminal chain of PBS had conformational similarity to ordinary tri- and diglycerides and could be incorporated as a substrate in the active site of this lipase. The surface adsorption of the lipase was much larger on PBS and its copolymer films than on the other polyester films because the lipase adhered quite strongly to the polymer terminal through a specific adsorption mechanism. Kinetic analysis showed that the total number of surface adsorption points per unit area of PBSL and PBSCL copolymers was larger than that of the PBS homopolymer.

• Journal of Pharmaceutical Investigation
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• 제27권2호
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• pp.99-108
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• 1997

To evaluate the feasibility of mucosal delivery of thyrotropin releasing hormone (TRH) through various mucosae, enzymatic degradation and stabilization of TRH in the nasal, rectal and duodenal extracts of rabbits were studied. TRH in the extracts was assayed by HPLC and its degradation was found to follow apparent first-order kinetics. The residual concentrations of TRH in the mucosal extracts of nasal, rectal and duodenal segments after 24 hr of incubation were found to be $65.1({\pm}1.1),\;19.7({\pm}2.7)$ and 0%, and in the serosal extracts, $65.6({\pm}5.5),\;75.2({\pm}1.1)$ and $68.7({\pm}1.4)%$, respectively. This result suggests that there is a significant difference in the activity of TRH-degrading enzymes among the sites of administration. The inhibition of TRH degradation in the mucosa extracts was kinetically investigated using various additives such as thimerosal, benzalkonium chloride, disodium edetate, ${\sigma}-phenanthroline$, dithiothreitol and dithioerythritol, and $IC_{50}$ values of inhibitors were calculated. The results obtained showed that thimerosal (0.5 mM) and benzalkonium chloride (0.141 mM) protected TRH from the enzymatic degradation in all the mucosa extracts more than 95% after 24 hr of incubation.

• 접착 및 계면
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• 제7권2호
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• pp.19-25
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• 2006

미생물 합성 고분자인 poly(hydroxylalkanoate)s (PHAs)의 초기효소분해는 표면침식의 메커니즘으로 진행하므로 이들의 분해거동은 표면특성을 개질로서 조절할 수 있다. 본 연구에서는 효소분해속도를 조절하기 위하여 플라즈마 기법을 PHAs 표면특성의 개질에 적용하였다. $CF_3H$와 $O_2$ 플라즈마를 사용하여 재료 표면에 각각 소수성 및 친수성을 부여하였다. 효소분해 실험은 pH 7.4의 0.1 M potassium phosphate 완충용액에서 Alcaligenes facalis T1에서 정제된 poly(hydroxybutyrate) 분해효소를 첨가하여 행하였다. $CF_3H$ 플라즈마 처리된 시편의 경우 표면 층의 불소화에 따른 소수성의 증가와 분해 효소에 대한 비활성으로 초기분해 속도가 상당히 지연됨을 관찰하였으나 $O_2$ 플라즈마 처리에 의한 표면 친수성은 분해속도의 촉진 등에 큰 영향을 미치지 않았다.

• 한국환경과학회지
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• 제19권9호
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• pp.1161-1167
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• 2010

The effects of addition of non degradable polymers, polystyrene (PS) and poly(methyl methacrylate) (PMMA) on the rate of enzymatic degradation of biodegradable poly(l-lactide) (PLLA) have been studied in term of surface structure. Since a component in multicomponent polymeric system has shown surface enrichment, PS and PMMA which have lower surface energy than PLLA were selected as a minor blend component (5 wt%). Enzymatic degradation was carried out at $37^{\circ}C$ and pH 8.5 in the aqueous solution of Proteinase K. Two blend systems, partially miscible (PS/PLLA) and immiscible (PMMA/PLLA), showed the surface enrichment of 4 and 2 times of PS and PMMA, respectively. From the weight loss profile data, the slow degradation rate of both blend films was observed. This indicates that PS or PMMA domains which exist at surface act as a retardant of enzymatic attack.

• Journal of Microbiology and Biotechnology
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• 제6권6호
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• pp.425-431
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• 1996

The enzymatic characteristics of Alcaligenes latus were investigated by measuring the variations of various enzyme activities related to biosynthesis and degradation of poly-${\beta}$-hydroxybutyrate (PHB) during cultivation. All PHB biosynthetic enzymes, ${\beta}$-ketothiolase, acetoacetyl-CoA reductase, and PHB synthase, were activated gradually at the PHB accumulation stage, and the PHB synthase showed the highest value among three enzymes. This indicates that the rate of PHB biosynthesis is mainly controlled by either ${\beta}$-ketothiolase or acetoacetyl-CoA reductase rather than PHB synthase. The enzymatic activities related to the degradation of PHB were also measured, and the degradation of PHB was controlled by the activity of PHB depolymerase. The effect of supplements of metabolic regulators, citrate and tyrosine, was also investigated, and the activity of glucose-6-phosphate dehydrogenase was increased by metabolic regulators, especially by tyrosine. The activities of ${\beta}$-ketothiolase and acetoacetyl-CoA reductase were also activated by citrate and tyrosine, while the activity of PHB depolymerase was depressed. The increased rate and yield of PHB biosynthesis by metabolic regulators may be due to the increment of acetyl-CoA concentration either by the repression of the TCA cycle by citrate through product inhibition or by the activation of sucrose metabolism by the supplemented tyrosine.

• 약학회지
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• 제38권5호
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• pp.530-543
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• 1994

To study the feasibility of transmucosal delivery of leucine enkephalin (Leu-Enk) and $[D-ala^2]$-leucine enkephalinamide (YAGFL), their degradation extents and pathways in various rabbit mucosa extracts were investigated by high performance liquid chromatography. The degradation of Leu-Enk and YAGFL was observed to follow the first-order kinetics. The degradation half-lives of Leu-Enk in the nasal, rectal and vaginal mucosal extracts were 1.62, 0.37 and 1.12 hrs and those of YAGFL were 30.55, 9.70 and 6.82 hrs, respectively, indicating Leu-Enk was degraded in a more extensive and rapid manner than YAGFL. But the mucosal and serosal extracts of the same mucosa showed the similar degradation rates for both pentapeptides. The degradation was most rapid in the neutral pH and increasing concentrations of substrates retarded the degradation rates. The maior hydrolytic fragments of Leu-Enk were Des-Tyr-Leu-Enk and tyrosine, indicating the enzymatic hydrolysis by aminopeptidases. However, the data also suggested endopeptidases such as dipeptidyl carboxypeptidase and dipeptidyl aminopeptidase could play some role in the degradation of Leu-Enk. On the other hand, the hydrolytic fragments of YAGFL in all the mucosa extracts were mainly Tyr-D-Ala-Gly and Phe-Leu-Amide, demonstrating the hydrolytic breakdown by endopeptidases. The degradation pathways were further explored by concomitantly determining the formation of smaller metabolites of primary hydrolytic fragments of Leu-Enk and YAGFL in the mucosa extracts.

• 폴리머
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• 제29권1호
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• pp.54-58
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• 2005

미생물 합성 poly[(R)3-hydroxybutyrate]](P(3HB))의 알칼리 및 효소 분해거동을 단결정과 Langmuir 단분자막을 모델시스템으로 하여 연구하였다. 단결정의 초기효소 및 알칼리 분해거동은 단결정의 장축에 대해 수직방향(b축)으로 분해가 일어났고 용융점 이하의 온도에서 열처리 또한 단결정의 b축을 따라 봉우리 형태의 형태학적 변화를 관찰하였다. 이러한 결과는 라멜라 단결정은 b축을 따라 불규칙한 영역을 가지고 있음을 의미하고 효소분해가 불규칙한 영역에서 선호적으로 일어난다고 설명할 수 있다. 한편, P(3HB), 단분자막의 효소 및 알칼리 분해경향은 분해매체와 표면압력에 크게 의존하였다. 알칼리 분해의 경우 낮은 표면압력에서도 분해를 나타내는 반면 효소 분해는 높은 표면 압력 하에서 분해거동을 나타내었다. 이러한 현상은 분자수준의 크기인 알칼리 분해매체는 P(3HB) 단분자막과 좁은 접촉면적(낮은 표면압력)에서도 활성을 보이는 반면 크기가 큰 분해효소는 보다 큰 활성 접촉면적(높은 표면압력)을 필요로 하는 것으로 판단된다.

• Journal of Pharmaceutical Investigation
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• 제26권3호
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• pp.175-185
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• 1996

To inhibit the enzymatic degradation of leucine enkephalin (Leu-Enk) and its synthetic analog. $[D-ala^2]$-leucine enkephalinamide (YAGFL), in the nasal, rectal and vaginal mucosal and serosal extracts of rabbits, effects of enzyme inhibitors such as amastatin (AM), puromycin (PM), thiorphan (TP), thimerosal (TM), EDTA, N-carboxymethyl-Phe-Leu (CPL), phenylethyl alcohol (PEA), phenylmercuric acetate (PMA), benzalkonium chloride (BC) and modified cyclodextrins, alone or in combination, were observed by assaying the pentapeptides staying intact during incubation. Mucosa extracts were prepared by exposing freshly-excised mucosal specimens mounted on Valia-Chien cells to isotonic phosphate buffer while stirring. The degradation of Leu-Enk and YAGFL followed the apparent first-order kinetics. The half-lives (mean) in the nasal, rectal and vaginal mucosal extracts were found to be 1.07, 0.33 and 1.14 hr for Leu-Enk, and 16.9, 6.2 and 6.8 hr for YAGFL, respectively. AM or PM, which is an aminopeptidase inhibitor, did not show a sufficient inhibition of Leu-Enk $(50\;{\mu}g/ml)$ degradation in all kinds of extracts. $Dimethyl-{\beta}-cyclodextrin\;(DM-{\beta}-CyD)$ decreased the degradation rate constants of Leu-Enk about 2 or 3 times, comparing with no additive. However, the use of mixed inhibitors of AM $(50\;{\mu}M)$/TM (0.25 mM)/EDTA (5 mM) resulted in a full stabilization of Leu-Enk by decreasing the degradation rate constants 67.3, 161.3 and 113.8 times far the nasal, rectal and vaginal mucosal extracts, respectively, comparing with no inhibitor. With mixed inhibitors, Leu-Enk remained intact more than 90% after 6 hr-incubation. In the stabilization of YAGFL, hM, TP or CPL alone showed little efffct, and some additives demonstrated a considerable inhibition of YAGFL degradation in the rank order of TM > BC > EDTA. However, the addition of mixed inhibitors such as TM (0.5 mM) and EDTA (5 mM) into the extracts protected YAGFL from the degradation by more than 85% even after 24 hr-incubation, suggesting almost complete inhibition of YAGFL degradation in the extract. On the other hand, $DM-{\beta}-CyD\;or\;hydroxypropyl-{\beta}-cyclodextrin$ (10%) were also found to retard enzymatic degradation rates of YAGFL markedly, and resulted in staying intact more than 80% of YAGFL in the nasal and vaginal mucosal extracts, and more than 60% in the rectal mucosal extract after 16 hr-incubation.