• Journal of Plant Biology
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• v.35 no.4
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• pp.333-338
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• 1992

Ginkgo (Ginkgo biloba L.) seeds were analyzed to determine the level of soluble sugars and insoluble starch during germination. Also the activities of the hydrolytic enzymes such as amylase, invertase and phosphatase were compared. As amylase activity was sharply increased, significant decline of starch was observed in the female gametophyte and increase of soluble sugars occurred concurrently. Invertase activity was gradually increased in cotyledon and radicle, while it was very low in dry seeds. In addition, phosphatase activity was variable only in radicle, and acid phosphatase showed higher activity than alkaline phosphatase.hatase.

• Journal of Korea Technical Association of The Pulp and Paper Industry
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• v.42 no.5
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• pp.1-14
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• 2010

Bio-ethanol is a promising alternative energy source for reducing both consumption of crude oil and environmental pollution from renewable resources like lignocellulosic biomass such as wood, forest residuals, agricultural leftovers and urban wastes. Based on current technologies, the cost of ethanol production from lignocellulosic materials is relatively high, and the main challenges are the low yield and high cost of the hydrolysis process. Development of more efficient pretreatment technology (physical, chemical, physico-chemical, and biological pretreatment), integration of several microbiological conversions into fewer reactors, and increasing ethanol production capacity may decrease specific investment for ethanol producing plants. The purpose of pretreatment of lignocellulosic material is to improve the accessible surface area of cellulose for hydrolytic enzymes and enhance the conversion of cellulose to glucose and finally high yield ethanol production which is economic and environmental friendly.

• The Korean Journal of Mycology
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• v.21 no.4
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• pp.316-322
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• 1993

Examination by scanning electron microscopy and potato-dextrose agar medium showed that the dry seeds of R. raetam were externally free of fungi. When planted in sandy loam soil, the seeds become colonized with eleven soilborne fungal species. The fungi were isolated on cellulose agar, pectin agar and lignin agar media. Aspergillus flavus, A. niger, Penicillium capsulatum and Fusarium oxysporum had broad occurrence and recovered on the three media. The production of hydrolytic enzymes by the isolated fungi depends on the substrate and species. P. capsulatum, P. spinulosum and A. niger had wide enzymatic amplitude and they were able to produce cellulolytic, pectolytic and lignolytic activities on corresponding substrates as well as on seed coat containing media. The lignolytic activities of the isolated species except Chaetomium bostrychods and Trichoderma viride were enhanced on applying the seed coat materials as C-source rather than using lignin. Soaking R. raetam seeds in culture filtrates of the most fungi grown on seed coat supplemented media induced pronounced and distinct stimulating effect on seed germination. The most effective filtrates were those of P. capsulatum, P. spinulosum and Sporotrichum pulverulentum.

• KSBB Journal
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• v.24 no.6
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• pp.579-583
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• 2009

The effects of cell lytic enzyme treatment on total phenolic content, antioxidant and antityrosinase activities of lotus leaf were investigated. The dried lotus leaves were hydroyzed by cell lytic enzymes such as Promozyme, Ceremix, Pectinex, Ultraflo, Celluclast, Pentopan, Tunicase, Viscozyme at their optimum pHs (pH 5-8) at $50^{\circ}C$ for 4 hrs. Depending on the enzymes used, total phenolic compounds content was measured as $1,079-1,476{\mu}g$/mL, and antioxidant activities and whitening activities were increased by 5~10% and 20%, respectively Among the tested hydrolytic enzymes, Promozyme (pullulanase) was selected as the most suitable enzyme for the extraction of total polyphenol from lotus leaf. The optimal dosage of Promozyme were found to be 1-2% (w/w). By Promozyme treatment, total phenolic compounds content of the lotus extract significantly increased compared to the extraction without enzyme treatment.

• Journal of Microbiology and Biotechnology
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• v.23 no.10
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• pp.1403-1412
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• 2013

Ethanol fuel production from lignocellulosic biomass is emerging as one of the most important technologies for sustainable development. To use this biomass, it is necessary to circumvent the physical and chemical barriers presented by the cohesive combination of the main biomass components, which hinders the hydrolysis of cellulose and hemicellulose into fermentable sugars. This study evaluated the hydrolytic capacity of enzymes produced by yeasts, isolated from the soils of the Brazilian Cerrado biome (savannah) and the Amazon region, on sugarcane bagasse pre-treated with $H_2SO_4$. Among the 103 and 214 yeast isolates from the Minas Gerais Cerrado and the Amazon regions, 18 (17.47%) and 11 (5.14%) isolates, respectively, were cellulase-producing. Cryptococcus laurentii was prevalent and produced significant ${\beta}$-glucosidase levels, which were higher than the endo- and exoglucanase activities. In natura sugarcane bagasse was pre-treated with 2% $H_2SO_4$ for 30 min at $150^{\circ}C$. Subsequently, the obtained fibrous residue was subjected to hydrolysis using the Cryptococcus laurentii yeast enzyme extract for 72 h. This enzyme extract promoted the conversion of approximately 32% of the cellulose, of which 2.4% was glucose, after the enzymatic hydrolysis reaction, suggesting that C. laurentii is a good ${\beta}$-glucosidase producer. The results presented in this study highlight the importance of isolating microbial strains that produce enzymes of biotechnological interest, given their extensive application in biofuel production.

• Korean Chemical Engineering Research
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• v.51 no.6
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• pp.716-726
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• 2013

Enzymatic acylations catalyzed by hydrolytic enzymes, along with enzymatic hydrolysis, are established reactions in the synthesis of fine chemicals such as chiral intermediates and polymerizations in the industry. Those reactions have been carried out mostly in organic media due to the thermodynamic limitations. Recently, there have been reports on enzymatic acylations in aqueous media. They have dealt with the elucidation of reaction mechanisms of hydrolases and acyl transferases based on their X-ray structures, homology comparison of the two kinds of enzymes, substrate engineering of acyl donors and computational design of acyl transferases for enzymatic acylations in aqueous media. Enzymatic acylations play an important role in the combinatorial synthesis of natural products such as polyketides and nonribosomal peptides. In this review, the historic developments of enzymatic acylations and industrial examples are described briefly. In addition, recent developments of enzymatic acylations in the modification of natural products and their prospects will be discussed.

• Journal of Microbiology and Biotechnology
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• v.19 no.11
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• pp.1306-1318
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• 2009

The filamentous ascomycete Sclerotinia sclerotiorum is well known for its ability to produce a large variety of hydrolytic enzymes. Two $\alpha$-amylases ScAmy54 and ScAmy43 predicted to play an important role in starch degradation were showed to produce specific oligosaccharides essentially maltotriose that have a considerable commercial interest. Primary structure of the two enzymes was established by N-terminal sequencing, MALDI-TOF masse spectrometry and cDNA cloning. The two proteins have the same N-terminal catalytic domain and ScAmy43 derived from ScAmy54 by truncation of 96 amino acids at the carboxyl-terminal region. Data of genomic analysis suggested that the two enzymes originated from the same $\alpha$-amylase gene and that truncation of ScAmy54 to ScAmy43 occurred probably during S. sclerotiorum cultivation. The structural gene of Scamy54 consisted of 9 exons and 8 introns, containing a single 1,500-bp open reading frame encoding 499 amino acids including a signal peptide of 21 residues. ScAmy54 exhibited high amino acid homology with other liquefying fungal $\alpha$-amylases essentially in the four conserved regions and in the putative catalytic triad. A 3D structure model of ScAmy54 and ScAmy43 was built using the 3-D structure of 2guy from A. niger as template. ScAmy54 is composed by three domains A, B, and C, including the well-known $(\beta/\alpha)_8$ barrel motif in domain A, have a typical structure of $\alpha$-amylase family, whereas ScAmy43 contained only tow domains A and B is the first fungal $\alpha$-amylase described until now with the smallest catalytic domain.

• Journal of Microbiology and Biotechnology
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• v.10 no.2
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• pp.258-263
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• 2000

2-Hydroxy-6-oxo-6phenylhexa-2,4-dienoate (HOPDA) hydrolase catalyzes the hydrolytic cleavage of HOPDA to bemzpate and 2-hydroxypenta-2, 4-dienoate (HPD) during microbial catabolism of biphenyl and polychlorinated biphenyls. A HOPDA hydrolase gene (pcbD) was isolated from the genomic library of Pseudomonas sp. P20 and designated as pCNUO1201; a 7.5-kb XbaI DNA fragment from Pseudomonas sp. P20 was inserted into the pBluescript SK(+) XbaI site. E. coli HB101 harboring pCNU1201 exhibited HOPDA hydrolase activity. The open reading frame (ORF) corresponding to the pcbD gene consisted of 855 base pairs with an ATG initiation codon and a TGA termination codon. The ORF was preceded by a rebosome-binding sequence of 5'-TGGAGC-3' and its G+C content was 55 mol%. The pcbD gene of Pseudomonas sp. P20 was located immedeately downstream of the pcbC gene encoding 2,3- dihydroxybiphenyl 1,2-dioxygenase, and approximately 4-kb upstream of the pcbE gene encoding HPD hydratase. The pcbK gene was able to encode a polypeptide with a molecular weight of 31,732 containing 284 amino acid residues. The deduced amino acid sequence of the HOPDA hydrolase of Pseudomonas sp. P20 exhibited high identity (62%) with those of the HOPDA hydrolases of P. putida KF715, P. pseudoalcaligenes KF707, and Burkholderia cepacia LB400, and also significant homology with those of other hydrolytic enzymes including esterase, transferase, and peptidase.

• Fisheries and Aquatic Sciences
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• v.5 no.4
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• pp.263-270
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• 2002

The Pacific oysters, Crassostrea gigas, were stressed with different concentrations of benzo(a) pyrene and depurated to determine the hemocyte lysosomal membrane stability and hydrolytic enzymatic activity as a biomarker candidate to the chemical, using NRR (neutral red retention) and API ZYM System, respectively. The membrane damage measured as NRR decrease was significant with the increase of chemical concentration and exposure time (P<0.05), providing a possible tool for biomarker. Interestingly, the control showed intrinsic stress probably due to captive life in the laboratory, and a recovering trend was also found during the depuration. The benzo(a)pyrene-exposed oysters showed increased enzyme activities in alkaline phosphatase, esterase (C4), acid phosphatase, naphthol-AS-BI-phospho­hydrolase, $\beta$-galactosidase, $\beta$-glucuronidase, and N-acetyl- $\beta$-glucosaminidase. Of them, only two enzymes, acid phosphatase and alkaline phosphatase, showed some potential available for the generation of enzymatic biomarker in the oyster. The results are suggestive of the potential availability of the cellular and enzymatic properties as a biomarker. However, considering that a robust biomarker should be insensitive to natural stress coming from normal physiological variation, but sensitive to pollutants, a concept of intrinsic stress the animal possesses should be taken into consideration. This reflects the necessity of further research on the intrinsic stress affecting the cellular and enzymatic properties of the chemical­stressed oysters prior to using the data as a biomarker.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.32 no.4
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• pp.488-494
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• 1999

Hydrolytic peptides of salted and fermented anchovy sauce, and anchovy actomyosin for the development of a rapid fermentation method with conventional tastes and flavors were studied. The optimal temperatures of crude enzymes isolated from anchor, liver and viscera of squid were 55, 40$\~$45 and $45\~60^{\circ}C$, respectively. Crude enzyme isolated from anchovy was more effective on hydrolysis of anchovy actomyosin than that from squid liver and viscera. But the crude enzyme from squid liver was less effective on NaCl than that from anchovy. Three peptides occurred in anchovy actomyosin hydrolyzed with crude enzymes from anchovy and squid liver for 30 min. Their molecular weight were determined by Superdex 200 gel chromatography as 10,800, 5,800 and 2,600 dalton. When anchovy sauce was hydrolyzed with crude enzymes of anchovy, squid liver and viscera, and Protamex during 70 days, ranges of their low molecular weight of hydrolyzed peptides were 300$\~$1,000dalton detected by Sephadex G-50 and their major amino acid compositions were glutamic acid, glycine and alanine, which was related with conventional tastes. Those amino acid compositions were similar to those of anchovy sauce hydrolyzed with squid liver, In the case of Protamex treatment, hydrolyzed peptides had high levels of isoleucine and leucine, being associated with the bitter, but a low level of glutamic acid.