Enzymatic Degradation of Poly(soybean oil-g-methyl methacrylate)

This study discusses grafting of methyl methacrylate units from thepolymeric soybean oil peroxide to produce poly(soybean oil-graft-methyl methacrylate) (PSO-g-PMMA). The degradation of this copolymer in solution was evaluated in the presence of different lipases, viz Candida rugosa (CR), Lipolase 100T (LP), Novozym 435 (N435) and Porcine pancreas (PP), at different temperatures The copolymer degraded by specific chain end scission and the mass fraction of the specific product evolved was determined The degradation was modeled using continuous distribution kinetics to determine the rate coefficients ofmenzymatic chain end scission and deactivation of the enzyme The enzymes, CR. LP and N435 exhibited maximum activity for the degradation of PSO-g-PMMA at 60 degrees C, while PP was most active at 50 degrees C. The thermal degradability of the copolymer, assessed by thermo-gravimetry, indicated that the activation energy of degradation of the copolymer was 154 kJ mol(-1), which was lesser than that of the PMMA homopolymer.

Non-enzymatic Degradation of (1→3)(1→4)-β-D-glucan in Aqueous Processing of Oats

Cereal water-soluble β-glucan [(1→3)(1→4)-β-D-glucan] has well-evidenced health benefits and it contributes to the texture properties of foods. These functions are characteristically dependent on the excellent viscosity forming ability of this cell wall polysaccharide. The viscosity is affected by the molar mass, solubility and conformation of β-glucan molecule, which are further known to be altered during food processing. This study focused on demonstrating the degradation of β-glucan in water solutions following the addition of ascorbic acid, during heat treatments or high pressure homogenisation. Furthermore, the motivation of this study was in the non-enzymatic degradation mechanisms, particularly in oxidative cleavage via hydroxyl radicals. The addition of ascorbic acid at food-related concentrations (2-50 mM), autoclaving (120°C) treatments, and high pressure homogenisation (300-1000 bar) considerably cleaved the β-glucan chains, determined as a steep decrease in the viscosity of β-glucan solutions and decrease in the molar mass of β-glucan. The cleavage was more intense in a solution of native β-glucan with co-extracted compounds than in a solution of highly purified β-glucan. Despite the clear and immediate process-related degradation, β-glucan was less sensitive to these treatments compared to other water-soluble polysaccharides previously reported in the literature. In particular, the highly purified β-glucan was relatively resistant to the autoclaving treatments without the addition of ferrous ions. The formation of highly oxidative free radicals was detected at the elevated temperatures, and the formation was considerably accelerated by added ferrous ions. Also ascorbic acid pronounced the formation of these oxidative radicals, and oxygen was simultaneously consumed by ascorbic acid addition and by heating the β-glucan solutions. These results demonstrated the occurrence of oxidative reactions, most likely the metal catalysed Fenton-like reactions, in the β-glucan solutions during these processes. Furthermore, oxidized functional groups (carbonyls) were formed along the β-glucan chain by the treatments, including high pressure homogenisation, evidencing the oxidation of β-glucan by these treatments. The degradative forces acting on the particles in the high pressure homogenisation are generally considered to be the mechanical shear, but as shown here, carbohydrates are also easily degraded during the process, and oxidation may have a role in the modification of polysaccharides by this technique. In the present study, oat β-glucan was demonstrated to be susceptible to degradation during aqueous processing by non-enzymatic degradation mechanisms. Oxidation was for the first time shown to be a highly relevant degradation mechanism of β-glucan in food processing.

Enzymatic degradation of polymers: a brief review

Recently, research on polymer has drawn much attention mainly due to the ever increasing application of these polymeric materials in several areas such as food packaging industry, agricultural industry and biomedical research. However, increasing industrial use of polymers has led to the environmentally critical issue of waste disposal. Further, the successful implication of polymeric materials in biomedical applications depends on the biodegradability of the concerned polymer. Various enzymes play an important role in the biodegradation of polymers. The present review describes the enzyme mediated biodegradation of various polymers including synthetic, natural and blends of these materials. Detailed examples of enzymatic degradation of polymers are illustrated from current scientific literature with the discussion on various factors that can influence the degradation. In addition, different techniques that are generally applied to assess the degradation process as well as degradation products have been described. Finally, a special emphasis is given to the investigation of the kinetics of polymer degradation by enzymes.

Lipase mediated enzymatic degradation of polydioxanone in solution

The enzymatic biodegradation of polydioxanone (PDO) in trifluoroethanol (TFE) at various temperatures (25-55 degrees C) was studied with two different types of lipases, namely immobilized enzyme Novozym 435 and free enzyme porcine pancreas lipase. The biodegradation process was monitored by gel permeation chromatography (GPC). Both enzymes showed the optimum activity at 37 degrees C and Novozym 435 exhibited better thermal stability over the experimental temperature range. A continuous distribution kinetic model was employed to describe the biodegradation process and the model was used to fit the experimental data satisfactorily and obtain kinetic parameters. (C) 2014 Elsevier Ltd. All rights reserved.

Enzymatic degradation of polycaprolactone-gelatin blend

Blends of polycaprolactone (PCL), a synthetic polymer and gelatin, natural polymer offer a optimal combination of strength, water wettability and cytocompatibility for use as a resorbable biomaterial. The enzymatic degradation of PCL, gelatin and PCL-gelatin blended films was studied in the presence of lipase (Novozym 435, immobilized) and lysozyme. Novozym 435 degraded the PCL films whereas lysozyme degraded the gelatin. Though Novozym 435 and lysozyme individually could degrade PCL-gelatin blended films, the combination of these enzymes showed the highest degradation of these blended films. Moreover, the enzymatic degradation was much faster when fresh enzymes were added at regular intervals. The changes in physico-chemical properties of polymer films due to degradation were studied by scanning electron microscopy, Fourier transform infrared spectroscopy and differential scanning calorimetry. These results have important implications for designing resorbable biomedical implants.

Enzymatic degradation of polycaprolactone-gelatin blend

Blends of polycaprolactone (PCL), a synthetic polymer and gelatin, natural polymer offer a optimal combination of strength, water wettability and cytocompatibility for use as a resorbable biomaterial. The enzymatic degradation of PCL, gelatin and PCL-gelatin blended films was studied in the presence of lipase (Novozym 435, immobilized) and lysozyme. Novozym 435 degraded the PCL films whereas lysozyme degraded the gelatin. Though Novozym 435 and lysozyme individually could degrade PCL-gelatin blended films, the combination of these enzymes showed the highest degradation of these blended films. Moreover, the enzymatic degradation was much faster when fresh enzymes were added at regular intervals. The changes in physico-chemical properties of polymer films due to degradation were studied by scanning electron microscopy, Fourier transform infrared spectroscopy and differential scanning calorimetry. These results have important implications for designing resorbable biomedical implants.

Enzymatic degradation of poly(L-lactide) and poly (epsilon-caprolactone) electrospun fibers

Poly(L-lactide) (PLLA) and poly(epsilon-caprolactone) (PCL) ultrafine fibers were prepared by electrospinning. The influence of cationic and anionic surfactants on their enzymatic degradation behavior was investigated by measuring weight loss, molecular weight, crystallinity, and melting temperature of the fibers as a function of degradation time. Under the catalysis of proteinase K, the PLLA fibers containing the anionic surfactant sodium docecyl sulfate (SDS) exhibited a faster degradation rate than those containing cationic surfactant triethylbenzylammonium chloride (TEBAC), indicating that surface electric charge on the fibers is a critical factor for an enzymatic degradation. Similarly, TEBAC-containing PCL fibers exhibited a 47% weight loss within 8.5 h whereas SDS-containing PCL fibers showed little degradation in the presence of lipase PS. By analyzing the charge status of proteinase K and lipase PS under the experimental conditions, the importance of the surface charges of the fibers and their interactions with the charges on the enzymes were revealed. Consequently, a "two-step" degradation mechanism was proposed: (1) the enzyme approaches the fiber surface; (2) the enzyme initiates hydrolysis of the polymer.

Enzymatic degradation of poly(epsilon-caprolactone)/poly(DL-lactide) blends in phosphate buffer solution

Blend films of poly(epsilon-caprolactone) (PCL) and poly(DL-lactide) (PDLLA) with 0.5 weight fraction of PCL were prepared by means of solution casting and their degradation behavior was studied in phosphate buffer solution containing Pseudomonas (PS) lipase. Enzymatic degradation of the blend films occurred continuously within the first 6 days and finally stopped when the film weight loss reached 50%, showing that only PCL in the blends degraded under the action of PS lipase in the buffer solution. These results indicate the selectivity of PS lipase on the promotion of degradation for PCL and PDLLA. The thermal properties and morphology of the blend films were investigated by differential scanning calorimetry, wide-angle X-ray diffraction and scanning electron microscopy (SEM). The morphology resulting from aggregate structures of PCL in the blends was destroyed in the enzymatic degradation process, as observed by SEM. These results confirm again the enzymatic degradation of PCL in the blends in the presence of PS lipase. (C) 1999 Published by Elsevier Science Ltd. All rights reserved.

Enzymatic degradation of poly(epsilon-caprolactone) film in phosphate buffer solution containing lipases

The enzymatic degradation of poly(epsilon-caprolactone) (PCL) films in phosphate buffer solution containing lipases has been studied by DSC, WAXD and SEM. Three lipases, pseudomonas lipase (PS), porcine pancreatic lipase (PP), and candida cylindracea lipase (AY), were used. The results showed that the degradation of PCL films in phosphate buffer solution containing PP or AY was very slow: no weight loss could be found within 1 week. However, PCL film could degrade rapidly and completely within 4 days in phosphate buffer solution containing PS lipase. (C) 1997 Elsevier Science Limited.

N-terminally modified glucagon-like peptide-1(7-36) amide exhibits resistance to enzymatic degradation while maintaining its antihyperglycaemic activity in vivo

Glucagon-like peptide-1 (7-36)amide (tGLP-1) is inactivated by dipeptidyl peptidase (DPP) IV by removal of the NH2-terminal dipeptide His(7)-Ala(8). We examined the degradation of NH2-terminally modified His(7)-glucitol tGLP-1 and its insulin-releasing and antihyperglycaemic activity in vivo, tGLP-1 was degraded by purified DPP IV after 4 h (43% intact) and after 12 hi 89% was converted to GLP-1(9-36)amide. In contrast > 99% of His(7)-glucitol tGLP-1 remained intact at 12 h. His(7)-glucitol tGLP-1 was similarly resistant to plasma degradation in vitro. His7-glucitol tGLP-1 showed greater resistance to degradation in vivo (92% intact) compared to tGLP-1 (27% intact) 10 min after i.p. administration to Wistar rats. Glucose homeostasis was examined following i.p. injection of both peptides (12 nmol/kg) together with glucose (18 mmol/kg). Plasma glucose concentrations were significantly reduced and insulin concentrations elevated following peptides administration compared with glucose alone. The area under the curve (AUC) for glucose for controls (AUC 691 +/- 35 mM/min) was significantly lower after administration of tGLP-1 and His7-glucitol tGLP-1 (36 and 49% less; AUC; 440 +/- 40 and 353 +/- 31 mM/min, respectively; P

Tuning self-assembled nanostructures through enzymatic degradation of a peptide amphiphile

The enzymatic cleavage of a peptide amphiphile (PA) is investigated. The self-assembly of the cleaved products is distinct from that of the PA substrate. The PA C16-KKFFVLK is cleaved by α-chymotrypsin at two sites leading to products C16-KKF with FVLK and C16-KKFF with VLK. The PA C16-KKFFVLK forms nanotubes and helical ribbons at room temperature. Both PAs C16-KKF and C16-KKFF corresponding to cleavage products instead self-assemble into 5-6 nm diameter spherical micelles, while peptides FVLK and VLK do not adopt well-defined aggregate structures. The secondary structures of the PAs and peptides are examined by FTIR and circular dichroism spectroscopy and X-ray diffraction. Only C16-KKFFVLK shows substantial β-sheet secondary structure, consistent with its self-assembly into extended aggregates, based on PA layers containing hydrogen-bonded peptide headgroups. This PA also exhibits a thermoreversible transition to twisted tapes on heating.

FACTORS THAT AFFECT THE ENZYMATIC DEGRADATION OF NATURAL STARCH GRANULES - EFFECT OF THE SIZE OF THE GRANULES

In this study the relationship between the enzymatic susceptibility and the size of the com and cassava starch granules was studied. The starch granules were separated by size and classified according to their average diameter in: a) larger than 16 mum; b) between 15 and 10 mum and c) smaller than 10 mum. The starch granules of various sizes were hydrolyzed by bacterial alpha-amylase and fungal amyloglucosidase. The results showed a relationship between the enzymatic susceptibility and the size of the starch granules; smaller size of the starch granules resulted in a higher percentage of hydrolysis. A basic difference in the mode of action of enzymes on small and large granules was observed. Enzymatic attack on the large granules was characterized by considerable surface corrosion, mainly at the radial axis. For small granules, the enzymatic action occurred on the surface of the granules and was characterized by an erosion with solubilization of the granules. Chemical and physical analysis of the starches suggested that hydrolysis should occur mainly at the amorphous areas of the granules.