• Journal of Microbiology and Biotechnology
• /
• v.1 no.1
• /
• pp.54-62
• /
• 1991

Cyclodextrin glucanotransferase(CGTase) derived from Bacillus macerans was immobilized by (1) covalent linkage on chitosan and chitin with glutaraldehyde, (2) adsorption on DEAE-cellulose and Amberite IRA 900 after succinylation, and (3) entrapment on alginate and polyacrylamide by cross linking. Adsorption on Amberite IRA 900 and covalent linking on chitosan were identified to be the most suitable immobilization methods considering the yield of activity and stability of immobilized CGTase. The enzymatic properties of immobilized CGTase were investigated and compared with those of the soluble CGTase. Thermal stability of CGTase immobilized on chitosan was increased from 50 to $55^{\circ}C$, and the optimum temperature of CGTase immobilized on Amberite IRA 900 was shifted from 55 to $50^{\circ}C$. The effect of molecular size of soluble starch (substrate) on immobilized CGTase investigated using partially liquefied substrates with different dextrose equivalent(DE). Cyclodextrin(CD) conversion yield augmented according to the increase of DE level for immobilized CGTase on Amberite IRA 900. CD conversion yield of partially cyclized starch with soluble CGTase was higher compared with liquefied one with ${\alpha}-amylase$.

• Korean Journal of Microbiology
• /
• v.38 no.1
• /
• pp.50-53
• /
• 2002

The optimum temperature and pH for mycelial growth of B. bassiana DGUM 34001 were $24^{\circ}C$ and pH 7.0, respectively. Among the complex media used, mushroom complex medium (MCM) was the most favorable for mycelial growth. When Czapek-Dox medium was used as a minimal medium, glucose was an excellent source for carbon and energy. Soytone and sodium phosphate were favorable constituent for culture medium as a source of organic nitrogen and phosphorus, respectively. When the fungus was grown in MCM broth, the specific activity of extracellular enzyme of ${\alpha}$-amylase, lipase, chitinase, CMCase and pretease were 297.0, 0.058, 0.33, 0.21 and 22.8 units/mg protein, respectively. When various sources of organic nitrogen and chitin were supplemented to determine the production of enzymes, casein and soluble chitosan enhanced the production of extracellular protease and chitinase.

• Journal of the Korean Applied Science and Technology
• /
• v.33 no.4
• /
• pp.706-716
• /
• 2016

In this study we applied the NAG obtained by the deacetylation of chitin extracted from the shells of crabs and shrimp as cosmetic ingredient. In order to compare NAG with GLC we identified the influence of cytotoxicity, anti-inflammatory, melanin biosynthesis formation inhibition on skin cell, and we measured the effects of the change of melanin and red spots. The results show that there was not any attentive cytotoxicity on the Raw 264.7 cell and B16F10 cell, and NO formation anti-inflammatory hindrance effect induced from Raw 264.7 by LPS was slight, and NAG suppressed the increase of melanin generation concentration-dependently after we induced the melanin generation with ${\alpha}$-MSH on B16F10 and measured the melanin biosynthesis inhibition. From this result, we identified the applicability of the cosmetics containing NAG as functional cosmetic for enhancing skin-lightening because when cream containing NAG was applied to skin the index of melanin red spots showed statistically meaningful changes.

• Korean Journal of Food Science and Technology
• /
• v.36 no.2
• /
• pp.321-328
• /
• 2004

Raw mulberry (Morus spp.) juice was prepared by minimal processing using several filter aids, fining agents, and clarifying enzymes, followed by filtration, centrifugation, and membrane filtration. Control of browning in minimally processed mulberry juices by anti-browning agents, sodium hydrosulfite, L-ascorbic acid, citric acid, and NaCl, was investigated using quantitative measurements of color changes during storage. Clarification of mulberry juice was improved by adding several filter aids, fining agents, and enzymes, followed by filtration and centrifugation. Several fining agents, including chitosan, chitin, PVPP, gelatin, and casein at a concentration of 1%, and combination of ultrafiltration and centrifugation at 8,000 rpm were not suitable for clarification of juice owing to strong adsorption of anthocyanin pigment. Combination of $0.01\;{\mu}m$ membrane filtration and centrifugation at 8,000 rpm was effective for clarification of mulberry juice. Browning of minimally processed mulberry juice was inhibited significantly by adding 200 ppm sodium hydrosulfite, and 0.1% L-ascorbic acid (L-AsA) and 0,1% citric acid (CA) also showed considerable browning inhibition. Combination of L-AsA and CA, which was moderately effective for browning inhibition of juice, may be useful as a sulfite alternative for mulberry juice. Optimum sugar ($^{\circ}Brix$)/acid ratio and commercial sterilization of minimally processed mulberry juice were approximately 40 and 10 min at $85-90^{\circ}C$, respectively.

• Journal of Microbiology and Biotechnology
• /
• v.19 no.3
• /
• pp.277-285
• /
• 2009

The nucleotide sequence of the Paenibacillus curdlanolyticus B-6 xyn10A gene, encoding a xylanase Xyn10A, consists of 3,828 nucleotides encoding a protein of 1,276 amino acids with a predicted molecular mass of 142,726 Da. Sequence analysis indicated that Xyn10A is a multidomain enzyme comprising nine domains in the following order: three family 22 carbohydrate-binding modules (CBMs), a family 10 catalytic domain of glycosyl hydrolases (xylanase), a family 9 CBM, a glycine-rich region, and three surface layer homology (SLH) domains. Xyn10A was purified from a recombinant Escherichia coli by a single step of affinity purification on cellulose. It could effectively hydrolyze agricultural wastes and pure insoluble xylans, especially low substituted insoluble xylan. The hydrolysis products were a series of short-chain xylooligosaccharides, indicating that the purified enzyme was an endo-$\beta$-1,4-xylanase. Xyn10A bound to various insoluble polysaccharides including Avicel, $\alpha$-cellulose, insoluble birchwood and oat spelt xylans, chitin, and starches, and the cell wall fragments of P. curdlanolyticus B-6, indicating that both the CBM and the SLH domains are fully functioning in the Xyn10A. Removal of the CBMs from Xyn10A strongly reduced the ability of plant cell wall hydrolysis. These results suggested that the CBMs of Xyn10A play an important role in the hydrolysis of plant cell walls.

• Journal of Periodontal and Implant Science
• /
• v.31 no.4
• /
• pp.823-832
• /
• 2001

Periodontal therapy has dealt primarily with attempts at arresting progression of disease, however, more recent techniques have focused on regenerating the periodontal ligament having the capacity to regenerate the periodontium. The effect of chitosan(poly-N-acetyl glucosaminoglycan), a carbohydrate biopolymer extracted from chitin, on periodontal ligament regeneration is of particular interest. The purpose of this study was to evaluate the effect of chitosan on the human periodontal ligament fibroblasts(hPDLFs) in vitro, with special focus on their proliferative properties by M'IT assay, the synthesis of type I collagen by reverse transcription-polymerase chain reaction(RT-PCR) and the activity of alkaline phosphatase(ALP). Fibroblast populations were obtained from individuals with a healthy periodontium and cultured with ${\alpha}MEM$ as the control group. The experimental groups were cultured with chitosan in concentration of 0.01,0.1, 1,2mg/ml. The results are as follows; 1. Chitosan-induced proliferative responses of hPDLFs reached a plateau at the concentration of O.lmg/ml(p<0.05). 2. When hPDLFs were stimulated with 0.lmg/ml chitosan, mRNA expression of type I collagen was up-regulated. 3. When hPDLFs were stimulated with 0.lmg/ml chitosan, ALP activity was significantly up-regulated(p<0.05). In summary, chitosan(0.lmg/ml) enhanced the type I collagen synthesis in the early stage, and afterwards, facilitated differentiation into osteogenic cells. The results of this in vitro experiment suggest that chitosan potentiates the differentiation of osteoprogenitor cells and may facilitate the formation of bone.