• Microbiology and Biotechnology Letters
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• v.24 no.3
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• pp.376-379
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• 1996

Cane molasses, the most widely used carbon source for the industrial fermentation of L-lysine, usually contains a high concentration of calcium ions which tend to cause scaling problem in the recovery process. To remove the calcium ions, cane molasses was pretrea ted with sulfuric acid by adjusting the pH to 2.5-3.5. When the pretreated solution was directly heat-sterilized and used in the fermentation, a significant reduction in L-lysine production was observed. In this paper, we proved that sucrose is a superior substrate for L-lysine fermentation to that of glucose or fructose and that the above-mentioned decrease of L-lysine production was caused by the hydrolysis of sucrose in the molasses when the molasses was heat-sterilized at a low pH. The problem was overcome by adjusting the pH of molasses to neutral before sterilization.

• Journal of Microbiology and Biotechnology
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• v.9 no.6
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• pp.704-708
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• 1999

In addition to catalyzing the synthesis of glucan from sucrose as a primary reaction, glucansucrase also catalyzes the transfer of glucose from sucrose to other carbohydrates that are present or are added to the reaction digest. Using dextransucrase and altemansucrase, prepared from Leuconostoc mesenteroides B-742CBM and B-1355C, respectively, we modified the bacterial cellulose in Acetobacter xylinum ATCC10821 culture, and then produced a characteristic cellulose that is soluble and has a new structure. There were also some partially modified insoluble cellulose and oligosaccharides in the modification culture. After methylation and following acid hydrolysis of both the soluble and insoluble glucans, there were ($1{\rightarrow}4$) as well as ($1{\rightarrow}6$) and ($1{\rightarrow}3$) glycosidic linkages in the soluble glucan.

• Applied Biological Chemistry
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• v.13 no.3
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• pp.181-186
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• 1970

1) Conditions for the hydrolysis of starch by bacterial liquefying amylase (BLA), saccharifying amylase (BSA) and isoamylase were investigated. Out of four syrups prepared by different combinations of these enzymes, those made by BLA followed by BSA and/or isoamylase were comparable to sucrose syrup in canning of orange segments. 2) Two branched maltooligosaccharides were isolated from the hydrolyzate of starch by BLA and BSA, and their structures were tentatively identified as pentaose and hexaose having an ${\alpha}-1$, 6-linkage at the branching point.

• Biomolecules & Therapeutics
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• v.6 no.3
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• pp.242-246
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• 1998

The inhibitory activities of Amberlite active fraction, which was obtained from methanol soluble fraction of freeze dried slikworm urine, on the rat intestinal glycosidase-catalyzed enzymatic reaction were examined in in viro and in vivo experiments. Amberlite active fraction showed significant inhibitory effects on the hydrolysis of o-glycosidic bond, especially $\alpha$-1,4 bond. On the other hand, the inhibition on the hydrolysis of $\beta$-glycosidic bond was very weak. Oral administration of Amberlite active fraction resulted in a dose-dependent decrease in the blood glucose after an oral maltose load, and postprandial hyperglycemia in carbohydrate-loaded mice was suppressed by Amberlite active fraction at 60 mgHg in decreasing order of maltose, starch, sucrose and lactose. 60 mg/kg of Amberlite active fraction lowered the blood glucose level markedly after 18, 35, and 60 min after an oral maltose load and the antihyperglycemic activity was maintained upto 90 min. In alloxan-induced hyperglycemic mice, Amberlite active fraction at a dose of 100 mg/kg also significantly lowered blood glucose after an oral maltose load, and its efficacy was almost equivalent to that of acarbowe.

• Microbiology and Biotechnology Letters
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• v.26 no.4
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• pp.309-315
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• 1998

An extracellular levansucrase, which catalyzes the formation of levan from sucrose, from the culture broth of Zymomonas mobilis ZM1 was purified by conventional column purification methods. The final purification yield was 18.3 fold of the crude enzyme from Z. mobilis, with 16.5 % of the enzyme recovered in the preparation step. The molecular weight of the enzyme was estimated to be 91,000 by Superose 12 gel filtration, and 45,000 by SDS-PAGE, indicating that levansucrase is a dimer. The optimum pH for the enzyme activity was around pH 4.0 for sucrose hydrolysis, and was around pH 5.0 for levan formation. The enzyme was inhibited by some metal ions, such as Hg$\^$2+/ and Cu2$\^$2+/, and 50% of inhibition was observed with 5mM EDTA. The enzyme activity was enhanced by the presence of detergent Triton X-100, but inhibited by SDS completely The enzyme catalyzes the liberation of reducing sugars, oligosacccharides and the formation of fructose polymer(levan). The enzyme also catalyzes the transfructosylation reaction of fructose moiety from sucrose to various sugar acceptor molecules, including sugar alcohols.

• The Korean Journal of Food And Nutrition
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• v.14 no.1
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• pp.46-51
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• 2001

No glucide-added Dongchimi, and 1% starch-added Dongchimi, and 1% sucrose-added one, each using 30% mashed radish as ingredients, were fermented at 4$^{\circ}C$ for 30 days. HPLC and TLC analyses showed that the no starch-added Dongchimi had glucose. fructose and sucrose. The starch-added Dongchimi produced maltose, maltotriose and maltotetraose by the hydrolysis reaction of amalyse. The sucrose added Dongchimi showed glucose. fructose and sucrose. And the sugar contents were reduced in the process of fermentation. The sugar-added Dongchimi showed 53 ${\mu}$g/ml of reducing sugar, 0.012 unit/ml of amylase activity, 3.84 of pH. 1.8 of acidity, after 30 days\` fermentation. One percent starch-added Dongchimi showed 173 ${\mu}$g/ml of reducing sugar, 0.019unit/m1 of amylase activity, 3.87 of pH, 2.1 of acidity, One percent sucrose-added Dongchimi showed 211 ${\mu}$g/ml of reducing sugar, 0.015 unit/ml of amylase activity, 3.36 of pH, 2.4 of acidity.

• The Journal of the Convergence on Culture Technology
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• v.9 no.4
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• pp.587-592
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• 2023

Plant growth is regulated by a variety of factors, including organic matter availability. Organic nutrients are carbohydrate molecules from photosynthetic products produced by tissues associated with carbon and energy fixation called "sources". These compounds flow through plant vascular bundles into non-photosynthetic or growing tissues called "sinks". Among these possible compounds, the disaccharide fructosyl glucose, sucrose, is the most representative. During the transport of sucrose, the pathway from the source to the sinks can include hydrolysis of sucrose into glucose and fructose derivatives or direct transfer of sucrose. Among the enzymes involved in this, β-D-fructofuranosidase is the most important. Soluble neutral β-D-fructofuranosidase, one of several isoenzymes, is located in intracellular protoplasts and helps plant cells metabolize sucrose to produce energy. In order to track the activity of this enzyme during the course of plant growth, histological methods were used for the most effective immunolocalization. As a result, the activity was higher in the phloem and epidermis than in the mesophyll tissue in the leaf. In the growing stem, activity was high in the phloem, epidermis, and cortex. The activity of the root, which is a sink tissue, was high in all parts, but especially the highest in the root tip part. It is thought that this is because it helps unloading of sucrose in sink tissues that require sucrose degradation and plays a role in hydrolysising sucrose.

• Journal of Microbiology and Biotechnology
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• v.22 no.9
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• pp.1253-1257
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• 2012

A gene (acas) designated as ${\alpha}$-amylase was cloned from Arthrobacter chlorophenolicus A6. The multiple amino acid sequence analysis and functional expression of acas revealed that this gene really encoded an amylosucrase (ASase) instead of ${\alpha}$-amylase. In fact, the recombinant enzyme exhibited typical ASase activity by showing both sucrose hydrolysis and glucosyltransferase activities. The purified enzyme has a molecular mass of 72 kDa and exhibits optimal hydrolysis activity at $45^{\circ}C$ and a pH of 8.0. The analysis of the oligomeric state of ACAS with gel permeation chromatography revealed that the ACAS existed as a monomer.

• Journal of Plant Biology
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• v.34 no.2
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• pp.113-119
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• 1991

The contents of reducing sugar, sucrose, starch and fructose-2,6-bisphosphate (F-Z,$6-P_2$) in relation to the activities of amylase, invertase and fructose-1,6-bisphosphatase (FBPase) were investigated from the leaves of rice (Oryza sativa L. cv. Samjin) seedlings grown at $4^{\circ}C$ for 3 days_ In the seedlings, the contents of reducing sugar and sucrose were increased, but soluble and insoluble starch were declined. Under this condition, amylase activity was increased. but acid invertase activity was declined and alkaline invertase activity was not changed. Cytosolic and stromal FBPase activities were increased. But F-2,$6-P_2$ content was declined. It seemed that the increase of reducing sugar content might be due to the increased activity of amylase and the increase of sucrose content might be related to the increased activity of cytosolic FBPase, reduced content of F-Z,$6-P_2$ and reduced rate of hydrolysis of sucrose during the cold treatment. These results suggested that the changes in carbohydrate rnetabolim of rice seedlings under low temperature reflect one of the protection mechanism to the low temperature during the cold treatment.atment.

• Journal of Microbiology and Biotechnology
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• v.25 no.6
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• pp.837-844
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• 2015

Carob waste is a useful raw material for the second-generation ethanol because 50% of its dry weight is sucrose, glucose, and fructose. To optimize the process, we have studied the influence of the initial concentration of sugars on the fermentation performance of Saccharomyces cerevisiae. With initial sugar concentrations (S₀ ) of 20 g/l, the yeasts were derepressed and the ethanol produced during the exponential phase was consumed in a diauxic phase. The rate of ethanol consumption decreased with increasing S₀ and disappeared at 250 g/l when the Crabtree effect was complete and almost all the sugar consumed was transformed into ethanol with a yield factor of 0.42 g/g. Sucrose hydrolysis was delayed at high S₀ because of glucose repression of invertase synthesis, which was triggered at concentrations above 40 g/l. At S₀ higher than 250 g/l, even when glucose had been exhausted, sucrose was hydrolyzed very slowly, probably due to an inhibition at this low water activity. Although with lower metabolic rates and longer times of fermentation, 250 g/l is considered the optimal initial concentration because it avoids the diauxic consumption of ethanol and maintains enough invertase activity to consume all the sucrose, and also avoids the inhibitions due to lower water activities at higher S₀ .