• Title, Summary, Keyword: Enzymatic degradation

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Biodegradability of Polylactic Acid Fabrics by Enzyme Hydrolysis and Soil Degradation

  • Lee, So Hee
    • Textile Coloration and Finishing
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    • v.29 no.4
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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.

Control of Enzymatic Degradability of Microbial Polyester by Surface Modification (표면 개질을 통한 미생물합성 폴리에스테르의 효소분해속도 조절)

  • 이원기
    • Journal of Environmental Science International
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    • v.11 no.12
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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.

Mechanism of Enzymatic Degradation of Poly(butylene succinate)

  • Lee, Chan-Woo;Kimura, Yoshiharu;Chung, Jin-Do
    • Macromolecular research
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    • v.16 no.7
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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.

Enzymatic Degradation and Stabilization of Thyrotropin Releasing Hormone in Various Rabbit Mucosa Extracts (점막 추출액중 치로트로핀 유리호르몬의 효소적 분해 및 안정화)

  • Chun, In-Koo;Shin, Dong-Won
    • Journal of Pharmaceutical Investigation
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    • v.27 no.2
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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.

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Surface Modification and Enzymatic Degradation of Microbial Polyesters by Plasma Treatments (플라즈마를 이용한 미생물합성 폴리에스테르의 표면개질과 효소분해성)

  • Kim, Jun;Lee, Won-Ki;Ryou, Jin-Ho;Ha, Chang-Sik
    • Journal of Adhesion and Interface
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    • v.7 no.2
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    • pp.19-25
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    • 2006
  • Since the enzymatic degradation of microbial poly(hydroxylalkanoate)s (PHAs), such as poly[(R)-3-hydroxybutyrate] and poly[(R)-3-hydroxybutyrate-co-3-hydroxyvalerate] initially occurs by a surface erosion process, their degradation behaviors can be controlled by the change of surface property. In order to control the rate of enzymatic degradation, plasma modification technique was applied to change the surface property of microbial PHAs. The surface hydrophobic and hydrophilic properties of PHA films were introduced by $CF_3H$ and $O_2$ plasma exposures, respectively. 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. The results showed that the significant retardation of initial enzymatic erosion of $CF_3H$ plasma-treated PHAs was observed due to the hydrophobicity and the enzyme inactivity of the fluorinated surface layers while the erosion rate of $O_2$ plasma-treated PHAs was not accelerated.

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Control of Enzymatic Degradability of Biodegradable Polylactide by Blending with Non-degradable Polymers (비 분해성고분자와 블렌드를 이용한 생분해성 폴리유산의 효소분해속도 조절)

  • Jang, Seong-Ho;Park, Sang-Bo;Lee, Won-Ki
    • Journal of Environmental Science International
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    • v.19 no.9
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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.

Enzymatic Characteristics of Biosynthesis and Degradation of Poly-$\beta$-hydroxybutyrate of Alcaligenes latus

  • Kim, Tae-Woo;Park, Jin-Seo;Lee, Yong-Hyun
    • Journal of Microbiology and Biotechnology
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    • v.6 no.6
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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.

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Enzymatic Degradation of Leucine Enkephalin and $[D-Ala^2]$-Leucine Enkephalinamide in Various Rabbit Mucosa Extracts (토끼의 수종 점막 추출액중 로이신엔케팔린 및 [D-알라$^2]$-로이신엔케팔린아미드의 효소적 분해 특성)

  • Chun, In-Koo;Park, In-Sook
    • YAKHAK HOEJI
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    • v.38 no.5
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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.

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Chain orientation and Degradation Behavior of Poly[(R)-3-hydroxybutyrate] Lamellar Crystals

  • Lee, Won Gi;Jo, Nam Ju;Ha, Chang Sik
    • Bulletin of the Korean Chemical Society
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    • v.22 no.8
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    • pp.872-876
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    • 2001
  • Topological changes caused by the alkaline and enzymatic attacks of solution-grown, chain-folded lamellar crystals (SGCs) of poly[(R)-3-hydroxybutyrate] P(3HB) have been studied in order to investigate the chain-folding structure in P(3HB) crystal regions. NaOH and an extracellular PHB depolymerase purified from Alcaligenes faecalis T1 were used for alkaline and enzymatic hydrolysis, respectively. The measurements were performed on crystals attached to a substrate which is inactive to degradation mediums. Both alkaline and enzymatic attacks lead to a breakup of the lamellar crystals along the crystallographic b-axis during initial erosion. Since hydrolysis preferentially occurs in amorphous regions, this morphological result reflects relatively loosely packed chains in core parts of lamellar crystals. Additionally, it was supported by the ridge formation along the b-axis in the lamellar crystals after thermal treatment at a low temperature because of the thermally sensitive nature of the loosely packed chains in lamellar crystals. However, the alkaline hydrolysis accompanied the chain erosions or scissions in quasi-regular folded lamellar surfaces due to smaller size of alkaline ions in comparison to the enzyme, resulting in the decrease of molecular weight.

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Degradation Behavior of Poly[(R)-3-hydroxybutyrate] by Using Single Crystals and Monolayers as Model Systems (단결정과 단분자막을 모델 시스템으로 한 Poly[(R)-3-hydroxybutyrate]의 분해거동)

  • Kim, Seong-Soo;Lee, Won-Ki;Ahn, Yong-Sik
    • Polymer Korea
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    • v.29 no.1
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    • pp.54-58
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    • 2005
  • The hydrolytic behavior of microbial poly[(R)-3-hydroxybutyrate]](P(3HB)) has been studied by using two model systems, Langmuir monolayer and solution-grown single crystals (SCs), for elucidating the mechanism for both alkaline and enzymatic degradations. An initial degradation of SCs of P(3HB) leads to breakup lamellae parallel to their short axis (b-axis). Similarly, ridge formation on the lamellar surface appears along the b-axis at lower quenching temperature than melting temperature. Both results support that the lamellar crystals contain less-ordered and more thermally sensitive regions along the b-axis. Although the enzymatic hydrolysis of P(3HB) monolayers was similar to its alkaline one, the enzymatic degradation of P(3HB) monolayers occurred at higher constant surface pressure than the alkaline degradation. This behavior might be attributed to the size of enzymes which is much larger than that of alkaline ions; that is, the enzymes need larger contact area with monolayers to be activated.