• Applied Biological Chemistry
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• v.12
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• pp.7-11
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• 1969

Mucor-rennin, the crystalline milk-clotting enzyme, isolated from Mucor pusillus var. Lindt, has an acid protease activity. The optimum pH for the digestion of k-casein is 4.5, while that for hemoglobin digestion is 4.0. The skim milk solution was easily clotted acidic solution than alkalin solution, and the milk clotting activated by Ca ion. The enzyme was heat stable against heat from pH 4.0 to 6.0 but was more stable at pH 5.0. The activity of the enzyme at pH 5.0 did not decrease at 30 C for 15 days and the activity was not effected by sodium propionate and salicilic acid. Therefore, the enzyme of liguid type could store for a long time and could be transported from Erzyme production Co. to Manufacture of cheese Co. by adding the antiesptic and by adjusting pH to 5.0.

• Journal of Applied Biological Chemistry
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• v.55 no.1
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• pp.13-17
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• 2012

In order to enzymatically produce chitooligosaccharide using the crude enzyme preparation from Bacillus cereus D-11, we first studied the optimal reaction conditions. It was found that the optimal temperature for hydrolysis of chitosan was $55^{\circ}C$. The ratio of enzyme/substrate should not be lower than 0.13 U/mg in the reaction mixture. The enzyme activity was stable below $50^{\circ}C$. The products of enzymatic reaction were analyzed by both thin layer chromatography and high performance liquid chromatography. Under the appropriate condition, chitosan was hydrolyzed using the enzyme preparation. The resulting chitooligosaccharides were purified and separated by Dowex ($H^+$) ion exchange chromatography. From 4 g soluble chitosan, 0.95 g $(GlcN)_2$, 1.43 g $(GlcN)_3$, and 1.18 g $(GlcN)_4$ were recovered.

• Journal of Microbiology and Biotechnology
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• v.19 no.12
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• pp.1596-1602
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• 2009

A lipase-catalyzed esterification reaction of (S)-naproxen ethyl ester by CALB (Candida antarctica lipase B) enzyme was performed in supercritical carbon dioxide. Experiments were performed in a high-pressure cell for 10 h at a stirring rate of 150 rpm over a temperature range of 313.15 to 333.15 K and a pressure range of 50 to 175 bar. The productivity of (S)-naproxen ethyl ester was compared with the result in ambient condition. The total reaction time and conversion yields of the catalyzed reaction in supercritical carbon dioxide were compared with those at ambient temperature and pressure. The experimental results show that the conversion and reaction rate were significantly improved at critical condition. The maximum conversion yield was 9.9% (216 h) at ambient condition and 68.9% (3 h) in supercritical state. The effects of varying amounts of enzyme and water were also examined and the optimum condition was found (7 g of enzyme and 2% water content).

• BMB Reports
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• v.29 no.2
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• pp.111-115
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• 1996

A novel glutathione S-transferase from Pseudomonas sp. DJ77 was expressed in E. coli and purified by glutathione-affinity chromatography. The enzyme was composed of two identical subunits. The molecular size of the enzyme was 42 kDa by sephadex G-150 gel permeation chromatography and Mr of each subunit was 23 kDa by sodium dodecylsulfate-polyacrylamide gel electrophoresis. pI value of the enzyme was approximately 5.8 by isoelectric focusing. This enzyme showed the highest activity toward 1-chloro-2,4-dinitrobenzene as the electrophilic substrate. The relative activities toward p-nitrobenzyl chloride and 1,2-dichloro-4-nitrobenzene were 3.8% and 1.3% of the activity toward 1-chloro-2,4-dinitrobenzene, respectively. $K_m$ and $V_{max}$ values for 1-chloro-2,4-dinitrobenzene calculated by Lineweaver-Burk plot were 0.76 mM and $14.81\;{\mu}mol/min/mg$, respectively, and those for glutathione were 6.23 mM and $64.93\;{\mu}mol/min/mg$, respectively. The enzyme showed highest glutathione S-transferase activity at pH 8.0 and was stable between pH 6.0 and 9.0. The enzyme retained its activity up to $35^{\circ}C$ for 90 min but was unstable above $45^{\circ}C$.

• Journal of Photoscience
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• v.10 no.1
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• pp.37-48
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• 2003

A review of the background and development of the p-hydroxyphenacyl group (pHP) as a photoprotecting group for biological substrates is chronicled. The pHP group has promise as an efficient, rapid phototrigger for the study of very fast biological processes. Applications include the release of neurotransmittors and second messengers, enzyme switches and nucleotides.

• Applied Biological Chemistry
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• v.51 no.3
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• pp.247-249
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• 2008

• Applied Biological Chemistry
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• v.44 no.4
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• pp.273-275
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• 2001

• Journal of Microbiology and Biotechnology
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• v.20 no.3
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• pp.574-578
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• 2010

Archaebacteria Sulfolobus acidocaldarius contains the highly thermophilic cytochrome P450 enzyme (CYP119). CYP119 possesses stable enzymatic activity at up to $85^{\circ}C$. However, this enzyme is still considered as an orphan P450 without known physiological function with endogenous or xenobiotic substrates. We characterized the regioselectivity of lauric acid by CYP119 using the auxiliary redox partner proteins putidaredoxin (Pd) and putidaredoxin reductase (PdR). Purified CYP119 protein showed a tight binding affinity to lauric acid ($K_d=1.1{\pm}0.1{\mu}M$) and dominantly hydroxylated (${\omega}-1$) position of lauric acid. We determined the steady-state kinetic parameters; $k_{cat}$ was 10.8 $min^{-1}$ and $K_m$, was 12 ${\mu}M$. The increased ratio to $\omega$-hydroxylated production of lauric acid catalyzed by CYP119 was observed with increase in the reaction temperature. These studies suggested that the regioselectivity of CYP119 provide the critical clue for the physiological enzyme function in this thermophilic archaebacteria. In addition, regioselectivity control of CYP119 without altering its thermostability can lead to the development of novel CYP119-based catalysts through protein engineering.

• Journal of Life Science
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• v.11 no.1
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• pp.27-29
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• 2001

Vibrio vulnificus endotoxin was extracted, analyzed the chemical composition, tested its biological activity, and compared to those of Escherichia coli and Salmonella typhimurium. The major fatty acid of three endotoxins were different each other; V. vulnificus endotoxins were different each other; V. vulnificus endotoxin was myristric acid (C14:0), E. coli was lauric acid (C12:0), S. typhimurium was capric acid (C10:0). The biological activities of V. vulnificus endotoxin were similar to those of E. coli and S. typhimurium in terms of the gelation activity of the Limulus amebocyte lysate and the lethal toxicity. But the result of enzyme (AST, ALT, and LDH) analysis showed that the enzyme activity of V. vulnificus endotoxin was similar to that of E. coli, but smaller than that of S. typimurium.

• Mycobiology
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• v.42 no.2
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• pp.109-113
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• 2014

During a survey of marine fungi from the waters surrounding Jeju Island, Korea, several Penicillium strains were isolated from seawater and marine sponges. Based on morphological characteristics and phylogenetic analyses of the internal transcribed spacer and RNA polymerase subunit II, four strains were identified as Penicillium antarcticum, a fungus that, to the best of our knowledge, had not been previously reported in Korea. Here, we provide detailed descriptions of the morphological characteristics and extracellular enzyme activities of the four strains.