Faculty Profiles - IMAMURA Koreyoshi

Cleaning of a stainless steel surface fouled with protein using a UV-H2O2 technique

K Imamura, Y Tada, H Tanaka, T Sakiyama, A Tanaka, Y Yamada, K Nakanishi

JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 34 ( 7 ) 869 - 877 2001.7

Language：English Publisher：SOC CHEMICAL ENG JAPAN

The UV-H2O2 technique, which is commonly known as a method of decomposing organic substances from wastewater, was applied into cleaning of a stainless steel surface fouled with protein. On a stainless steel surface fouled with bovine beta -lactoglobulin (beta -Lg), H2O2 Solution was made to now, and UV rays were irradiated over the flowing liquid. The amounts of beta -Lg adsorbed before and during the UV-H2O2 cleaning were measured by a reflection absorption technique using Fourier transform infrared spectroscopy (RA-IR). The adsorbed amount approximately decreased linearly with time during the UV-H2O2 cleaning. There was an optimum H2O2 concentration for the removal rate. The H2O2 concentration dependency of the removal rate could be explained by considering the formation and disappearance rates of hydroxyl radicals (. OH), the decay of UV illuminance along the depth of the flow, and the rate of reaction between adsorbed beta -Lg and -OH.

DOI： 10.1252/jcej.34.869

Increase in the stability of serine acetyltransferase from Escherichia coli against cold inactivation and proteolysis by forming a bienzyme complex

K Mino, K Imamura, T Sakiyama, N Eisaki, A Matsuyama, K Nakanishi

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 65 ( 4 ) 865 - 874 2001.4

Language：English Publisher：TAYLOR & FRANCIS LTD

Cysteine synthetase from Escherichia coli is a bienzyme complex composed of serine acetyltransferase (SAT) and O-acetylserine sulfhydrylase-A, (OASS), The effects of the complex formation on the stability of SAT against cold inactivation and proteolysis were investigated. SAT was reversibly inactivated on cooling to 0 degreesC. Ultracentrifugal analysis showed that SET (a hexamer) was dissociated mostly into two trimers on cooling to 0 degreesC in the absence of OASS, while in the presence of BASS one trimer of the SAT subunits formed a complex with one dimer of BASS subunits. In the presence of BASS, trot only the cold inactivation rate was reduced but also the reactivation rate was increased. Furthermore, SAT became stable against proteolytic attack bg alpha -chymotrypsin and V8 protease by forming the complex with OASS, On the other hand, SAT was degraded by trypsin in the same manner both in the presence and in the absence of OASS. The different tendency in the stability against proteolysis with the different proteases was discussed with respect to the substrate specificity of the proteases and amino acid sequence of the C-terminal region of SAT that interacts with OASS.

DOI： 10.1271/bbb.65.865

On the adsorption of proteins on solid surfaces, a common but very complicated phenomenon

K Nakanishi, T Sakiyama, K Imamura

JOURNAL OF BIOSCIENCE AND BIOENGINEERING 91 ( 3 ) 233 - 244 2001.3

Language：English Publishing type：Book review, literature introduction, etc. Publisher：SOC BIOSCIENCE BIOENGINEERING JAPAN

Adsorption of proteins on solid surfaces and their interaction are major concerns in a number of fields such as biology, medicine, biotechnology and food processing, and play an important role from various points of view. Based on practical viewpoints, information on the conformation of the adsorbed protein as well as adsorption characteristics is essential for a system's performance. Although there are still many problems to be solved, extensive studies in recent years, owing to the development in instrumentation and instrumental techniques, reveal the adsorption behavior of proteins in detail. Here, we stress the importance and interesting aspect of protein adsorption on solid surfaces by reviewing findings that have been obtained in recent years.

Enzymatic modification of β-lactoglobulin with N-fatty-acyl-dipeptides by transglutaminase from Streptomyces mobaraense.

凍結乾燥によって得られた糖類アモリファスマトリクスにおけるタンパク質の水和状態の評価

Journal of Pharmacentical Sciences 91(12), 1955-1964 2001

UV/H₂O₂処理を利用したステンレス表面に付着したタンパク質の洗浄

34 ( 7 ) 869 - 877 2001

Wada Eiko, Masuda Haruki, Imamura Koreyoshi, Sakiyama Takaharu, Adachi Shuji, Matsuno Ryuichi, Nakanishi Kazuhiro

13 158 - 158 2001

Purification of capsaicin-hydrolyzing enzyme from Streptomyces sp.

Koreishi Mayuko, Zhang Demin, Imamura Koreyoshi, Sakiyama Takaharu, Adachi Syuji, Matsuno Ryuichi, Nakanishi Kazuhiro

13 159 - 159 2001

pH-Responsive swelling of chitosan/chondroitin sulfate complex gels and its application.

Sakiyama Takaharu, Ikuta Yuji, Imamura Koreyoshi, Nakanishi Kazuhiro

13 282 - 282 2001

Cleaning of a stainless steel surface fouled with protein by H_2O_2-electrolysis technique

Imamura Koreyoshi, Tada Yoichiro, Tanaka Hirofumi, Sakiyama Takaharu, Nakanishi Kazuhiro, Tanaka Atsumi, Yamada Yosuke

13 282 - 282 2001

Cultivation characteristics of rerecombinant Aspergillus oryzae for production of enzyme

Shimamura Hiroko, Morita Masakazu, Yonashiro Ryota, Imammura Koreyoshi, Sakiyama Takaharu, Ninetoki Toshitaka, Nakanishi Kazuhiro

13 199 - 199 2001

バイオ・食品製造プロセスにおける汚れの付着と洗浄 (特集最近の生物工学の展望)

中西一弘, 崎山高明, 今村維克

ケミカルエンジニヤリング 45 ( 11 ) 854 - 861 2000.11

Adsorption behavior of amino acids on a stainless steel surface

K Imamura, T Mimura, M Okamoto, T Sakiyama, K Nakanishi

JOURNAL OF COLLOID AND INTERFACE SCIENCE 229 ( 1 ) 237 - 246 2000.9

Language：English Publisher：ACADEMIC PRESS INC

The adsorption behavior of various amino acids on a stainless steel surface was investigated at 30 degrees C and over a pH range of 3-10. Acidic and basic amino acids except histidine adsorbed remarkably at pH 3-4 and 7-10, respectively, and showed Langmuir-type adsorption isotherms. The effects of pH and ionic strength on the adsorption isotherms were investigated to analyze the interactions between amino acids and adsorption sites on the stainless steel. Hydrophobic amino acids and glycine showed only small adsorbed amounts at all pHs tested. For the acidic and basic amino acids, reversibility of the absorption and the influence of the ionic strength on the adsorption behavior were examined. The adsorption isotherms of the derivatives of aspartic acid were also measured in order to examine the contribution of the carboxylic groups of acidic amino acids to the adsorption. Furthermore, a Fourier-transform infrared spectroscopic analysis and semiempirical molecular orbital calculation were carried out to analyze the ionization states and the configuration of the amino acids adsorbed on a stainless steel surface. These investigations suggest that the acidic and basic amino acids adsorb through two electrostatic interactions of two ionized groups in the amino acid with a stainless steel surface, (C) 2000 Academic Press.

DOI： 10.1006/jcis.2000.7016

Characteristics of serine acetyltransferase from Escherichia coli deleting different lengths of amino acid residues from the C-terminus

K Mino, K Hiraoka, K Imamura, T Sakiyama, N Eisaki, A Matsuyama, K Nakanishi

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY 64 ( 9 ) 1874 - 1880 2000.9

Language：English Publisher：TAYLOR & FRANCIS LTD

Some properties of serine acetyltransferases (SATs) from Escherichia coli, deleting 10-25 amino acid residues from the C-terminus (SAT Delta C10-Delta C25) were investigated. The specific activity depended only slightly on the length of the C-terminal region deleted. Although the sensitivity of SAT Delta C10 to inhibition by L-cysteine was similar to that for the wild-type SAT, it became less with further increases in the length of the amino acid residues deleted. SAT Delta C10 was inactivated on cooling to 0 degrees C and dissociated into dimers or trimers in the same manner as the wild-type SAT, but Met-256-Ile mutant SAT as web as SAT Delta C14, SAT Delta C20, and SAT Delta C25 were stable. Since SAT Delta C10, SAT Delta C14, and SAT Delta C25 did not form a complex with O-acetyl-serine sulfhydrylase-A (OASS-A) in a way similar to SAT Delta C20. it was indicated that 10 amino acid residues or fewer from the C-terminus of the wild-type SAT are responsible for the complex formation with OASS-A. The C-terminal peptide of the 10 amino acid residues interacted competitively with OASS-A with respect to OAS although its affinity was much lower than that for the wild-type SAT.

DOI： 10.1271/bbb.64.1874

Adsorption behavior of amino acids on a stainless steel surface

K Imamura, T Mimura, M Okamoto, T Sakiyama, K Nakanishi

JOURNAL OF COLLOID AND INTERFACE SCIENCE 229 ( 1 ) 237 - 246 2000.9

Language：English Publisher：ACADEMIC PRESS INC

DOI： 10.1006/jcis.2000.7016

PubMed

Water sorption and glass transition of amorphous sugars containing BSA

K Imamura, T Suzuki, T Tatsumichi, S Kirii, M Okazaki

JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 33 ( 4 ) 657 - 660 2000.8

Language：English Publisher：SOC CHEMICAL ENG JAPAN

Water sorption and glass transition of four amorphous sugars (lactose, maltose, sucrose, and trehalose) containing bovine serum albumin (BSA) are investigated. Freeze-dried sugar-BSA samples equilibrated at several water activities ranging from 0 to 0.43 were prepared. Moisture content and glass transition temperature (T-g) were measured. For the all sugars, it is found that BSA lowers T-g at low water activity, and raises it at high water activity. It Is also found that the difference between T-g of the sugar-BSA samples and that of the corresponding amorphous sugar samples (T-go) depends mainly on T-go.

DOI： 10.1252/jcej.33.657