• KOREAN JOURNAL OF PACKAGING SCIENCE & TECHNOLOGY
• /
• v.28 no.2
• /
• pp.89-95
• /
• 2022

The goal of this study was to evaluate the effect of spent coffee grounds (SCG) biofiller on the morphological, thermal, mechanical and hydrolytic degradation characteristics of poly(lactic acid) (PLA) based biocomposites. The PLA-based biocomposite films were fabricated by using a high-viscosity kneading and hot-pressing machine. The PLA/SCG biocomposites were analyzed with SEM, DSC, TGA, UTM and hydrolytic degradation test. Aggregation in the PLA matrix is a result of increasing SCG concentrations. In the thermal properties, it was described that the cold crystallization temperature (T_cc) decreased as SCG was added to PLA. When SCG was incorporated to PLA, the degradation onset temperature (T_onset) revealed a diminish. The elastic modulus increased while tensile strength of PLA diminished as SCG was applied. Through hydrolysis analysis, the decomposition of PLA was accelerated with the addition of SCG. This research confirmed the possibility of devloping an eco-friendly packaging material with high degradability as SCG hasten the breakdown of PLA.

• Biotechnology and Bioprocess Engineering:BBE
• /
• v.5 no.6
• /
• pp.449-455
• /
• 2000

Pseudomonas sp. strain DJ-12 is a bacterial isolate capable of degrading 4-chlorobiphenyl (4CBP) as a carbon and energy source. The catabolic degradation of 4CBP by the strain DJ-12 was studied along with the genetic organization of the genes responsible for the crucial steps of the catabolic degradation. The catabolic pathway was characterized as being conducted by consecutive reactions of the meta-cleavage of 4CBP, hydrolytic dechlorination of 4-chlorobenzoate (4CBA), hydroxylation of 4-hydroxybenzoate, and meta-cleavage of protocatechuate. The pcbC gene responsible for the meta-cleavage of 4CBP only showed a 30 to 40% homology in its deduced amino acid sequence compared to those of the corresponding genes from other strains. The amino acid sequence of 4CBA-CoA dechlorinase showed an 86% homology with that of Pseudomonas sp. CBS3, yet only a 50% homology with that of Arthrobacter spp. However, the fcb genes for the hydrolytic dechlorination of 4CBA in Pseudomonas sp. DJ-12 showed an uniquely different organization from those of CBS3 and other reported strains. Accordingly, these results indicate that strain DJ-12 can degrade 4CBA completely via meta-cleavage and hydrolytic dechlorination using enzymes that are uniquely different in their amino acid sequences from those of other bacterial strains with the same degradation activities.

• Korean Journal of Pharmacognosy
• /
• v.31 no.1
• /
• pp.101-104
• /
• 2000

An inhibitory activity against ${\alpha}-glucosidase$ was identified in extract of an edible lichen, Umbilicaria esculenta. The inhibitor was very stable retaining above 95% of its original activity when treated with heat, acid and alkaline conditions, and some hydrolytic enzymes. Partially purified inhibitor showed strong inhibition against disaccharide hydrolytic enzymes of mammalian and mold origin, but weak or no inhibition against polysaccharide hydrolytic enzymes except glucoamylase. The inhibitor suppressed elevation of blood glucose level in rats after oral administration of soluble starch or sucrose.

• Microbiology and Biotechnology Letters
• /
• v.25 no.2
• /
• pp.115-120
• /
• 1997

Penicillium sp.-L4, a causative fungus of rot in citrus fruits, was isolated and its mode of hydrolytic enzyme production was investigated. Carboxymethylcellulase (CMCase), polygalacturonase(PGase), extra- & intra-cellular $\beta$-glucosidase and cellobiase were produced drastically by addition of substrates in minimal media. Production of the hydrolytic enzymes were induced efficiently by cellobiose and cellooligosaccharides which were the products of cellulose hydrolysis, but repressed by addition of mono-saccharide such as glucose, raffinose, galacturonic acid. The relative activity of p-nitrophenyl-$\beta$-D-glucopyranoside(PNPG) hydrolysis was higher than that of cellobiose hydrolysis in extracellular enzymes, and reverse is true in intracellular enzymes. Intact enzyme production of P. sp.-L4 on lemon peel lesion was sequential. $\beta$-Glucosidase and CMCase were produced first and followed by PGase. The enzyme productivities and pH in lesions were coincident with optimal pH of each enzyme activities.

• The Korean Journal of Food And Nutrition
• /
• v.13 no.2
• /
• pp.134-138
• /
• 2000

An inhibitory activity against ${\alpha}$-glucosidase was identified in extracts of medicinal lichens, Parmelia austrosinensis and P. praesorediosa. The extracts retained almost all of their original activities when treated with heat, acid and alkaline conditions, and some hydrolytic enzymes. Partially purified inhibitor showed strong inhibition against disaccharide hydrolytic enzymes of mammalian and mold origin, but weak or no inhibition against polysaccharide hydrolytic enzymes except glucoamylase. The inhibitors from the two Parmelia sp. showed almost same retention time in HPLC. The inhibitor suppressed elevation of blood glucose level in rats after oral administration of soluble starch or sucrose.

• YAKHAK HOEJI
• /
• v.38 no.5
• /
• pp.530-543
• /
• 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.

• Microbiology and Biotechnology Letters
• /
• v.47 no.1
• /
• pp.125-131
• /
• 2019

We have isolated and identified 72 bacterial strains from four bentonite samples collected at the mining areas located in Gyeongsangbuk-do, Republic of Korea, and measured their hydrolytic enzyme (${\alpha}$-amylase, protease, and cellulase) activities to identify the isolates with industrial-use potential. Most of the isolates belonged to the Bacillaceae, with minor portions being from the Paenibacillaceae, Micrococcaceae, and Bacillales Family XII at the family level. Of the strains isolated, 33 had extracellular ${\alpha}$-amylase activity, 30 strains produced cellulase, and 35 strains produced protease. Strain MBLB1268, having the highest ${\alpha}$-amylase activity, was identified as Bacillus siamensis ($0.38{\pm}0.06U/ml$). Bacillus tequilensis MBLB1223, isolated from Byi33-b, showed the highest cellulase activity ($0.26{\pm} 0.04U/ml$), whereas Bacillus wiedmannii MBLB1197, isolated from Zdb130-b, exhibited the highest protease activity ($54.99{\pm}0.78U/ml$). These findings show that diverse bacteria of the Bacillaceae family adhere to and exist in bentonite and are potential sources of industrially useful hydrolytic enzymes.

• Macromolecular Research
• /
• v.9 no.4
• /
• pp.210-219
• /
• 2001

Quenched and slow cooled as well as isothermally crystallized poly(tetramethylene succinate)(PTMS) films at two different temperatures were prepared. In the process of hydrolysis of the four specimens, structural changes such as the crystallinity, crystal size distribution, lattice parameter, lamellar thickness, long period and surface morphology were investigated by using wide and small angle X-ray scattering (WAXS and SAXS), differential scanning calorimetry (DSC) and scanning electron microscopy (SEM). The hydrolytic degradation of quenched film was faster than that of slow cooled and isothermally crystallized films. The film crystallized at 100$\^{C}$ exhibited extensive micro voids and thus showed faster degradation than that crystallized at 75$\^{C}$, demonstrating surface morphology is another important factor to govern degradation rate. The crystallinity of the specimen increased by 5-10% and long period decreased after hydrolysis for 20 days. At the initial stage of degradation, the lamellar thickness of quenched film rather increased, while that of slow cooled and isothermally crystallized films decreased. The hydrolytic degradation preferentially occurred in the amorphous region. The hydrolytic degradation in crystal lamellae are mainly at the crystal surfaces.

• Asian-Australasian Journal of Animal Sciences
• /
• v.19 no.5
• /
• pp.684-689
• /
• 2006

The present study examined the effects of Tween 80 on the attachment and hydrolytic activity of a cellulase enzyme against ball-milled cellulose (BMC), using the whole component (native CBH I) and the catalysis module (core CBH I) of carbohydrolase I purified from Trichoderma viride (Meicelase, Meiji Seika, Tokyo, Japan). The effects were evaluated as protein concentrations in the supernatant after mixing enzyme and substrate with Tween 80 at room temperature. Tween 80 decreased the adsorption of native CBH I and core CBH I onto BMC (p<0.001) and increased the amount of reducing sugars released from BMC by native CBH I (p<0.001). However, Tween 80 did not enhance the hydrolytic activity of core CBH I. Observations using SEM revealed that Tween 80 caused cellulose filter paper to swell and enhanced surface cracks and filaments caused by native CBH I but not by core CBH I. These results suggested that Tween 80 decreases enzyme adsorption to its substrate but enhances enzymatic activity.

• Journal of the Korean Wood Science and Technology
• /
• v.42 no.5
• /
• pp.605-614
• /
• 2014

This study investigated microstructural changes of cured urea-formaldehyde (UF) resins mixed with aqueous rubber latex emulsion after intentional acid etching. Transmission electron microscopy (TEM) was used in order to better understand a hydrolytic degradation process of cured UF resins responsible for the formaldehyde emission from wood-based composite panels. A liquid UF resin with a formaldehyde to urea (F/U) molar ratio 1.0 was mixed with a rubber latex emulsion at three different mixing mass ratios (UF resin to latex = 30:70, 50:50, and 70:30). The rate of curing of the liquid modified UF resins decreased with an increase of the rubber latex proportion as determined by differential scanning calorimetry (DSC) measurement. Ultrathin sections of modified and cured UF resin films were exposed to hydrochloric acid etching in order to mimic a certain hydrolytic degradation. TEM observation showed spherical particles and various cavities in the cured UF resins after the acid etching, indicating that the acid etching had hydrolytically degraded some part of the cured UF resin by acid hydrolysis, also showing spherical particles of cured UF resin dispersed in the latex matrix. These results suggested that spherical structures of cured UF resin might play an important role in hindering the hydrolysis degradation of cured UF resin.