• 한국생물공학회:학술대회논문집
• /
• 2003.04a
• /
• pp.209-212
• /
• 2003

This study was to investigate the effects of media components on carbohydrolase complex production in liquid culture of Lentinus edodes. Glucose and yeast extract, and $MgSO_4\;.\;7H_2O$ were selected as carbon, nitrogen, and mineral sources, respectively. The production level of ${\beta}-glucosidase$, one of carbohydrolase complex, was high. On the other hand, ${\beta}-glucuronidase$ and ${\beta}-galactosidase$ production levels were very low, which remain to be improved.

• Biotechnology and Bioprocess Engineering:BBE
• /
• v.8 no.2
• /
• pp.106-111
• /
• 2003

A novel carbohydrolase, which is a DXAMase, containing both dextranase and amylase equivalent activities, was purified from Lipomyces starkeyi KSM22. The purified DXAMase was also found to hydrolyze cellobiose, gentiobiose, trehalose and melezitose, while disproportionation reactions were exhibited with various di- and tri-saccharides, such as maltose, isomaltose, gentiobiose, kojibiose, sophorose, panose, maltotriose, and isomaltotriose with various kinds of oligosaccharides produced as acceptor reaction products. Furthermore, the purified DXAMase hydrolyzed raw waxy rice Starch and produced maltodextrin to the extent of 50% as a glucose equivalent.

• 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.

• 한국생물공학회:학술대회논문집
• /
• 2003.10a
• /
• pp.278-281
• /
• 2003

This study was concentrated on investigating the optimum compositions of medium for the production of carbohydrolases complex. In order to maximize the activities of the carbohydrolases complex, cellulose and yeast extract were chosen as the best C and N sources, respectively. The concentrations of cellulose and yeast extract as well as minerals and amino acids were also studied. On the other hand, ${\beta}-glucosidase$ and ${\beta}-glucuronidase$ showed the maximal activities at $60^{\circ}C$ and pH 4, while ${\beta}-galactosidase$ showed the maximal activity at $50^{\circ}C$ and pH 3.

• Korean Journal of Food Science and Technology
• /
• v.31 no.5
• /
• pp.1211-1215
• /
• 1999

The solid yields and color changes of garlic aqueous extracts were determined to study the effects of enzymatic hydrolysis, pH treatment, and addition of organic acids and some organic or inorganic salts. Hydrolysis with commercial polysaccharases resulted in an $15{\sim}20%$ increase in the solid yields, with a greenish color change in the garlic extracts. pH treatment gave it similar effect at the pH range of $4.4{\sim}5.0$. Among the salts and acidulants used, $CaCl_2$, sodium oxalate, tartaric and phosphoric acids were effective for increase in the yield and $K_{4}P_{2}O_{7}$ was effective for both yield increase and control of greening.

• KSBB Journal
• /
• v.17 no.6
• /
• pp.586-589
• /
• 2002

Lipomyces starkeyi KSM 22 produces dextranase and amylase (DXAMase). The addition of 0.02％ (w/v) 2-deoxy-D-glucose or 0.5% (w/v) glycerol into a 1% (w/v) starch medium increased the final activity of DXAMase produced 2.5 fold or 2.4 fold, respectively, compared to that of a 1% (w/v) starch medium. This activity was similar to that produced with 1% (w/v) dextran. The stability of purified OXAMase at 40$\^{C}$ for 3 weeks was tested using the various enzyme stabilizers. With the addition of 25% (v/v) glycerol, 90.9% of initial activity was left after 3 weeks. For practical use, the addition of 1% (v/v) glycerol with 50 mM of CaCl$_2$ or KH$_2$PO$_4$was adequate and maintained 73.4% of the initial activity under the test conditions used.