Masaki K

References (8)

Title : Features and application potential of microbial urethanases - Masaki_2022_Appl.Microbiol.Biotechnol__
Author(s) : Masaki K
Ref : Applied Microbiology & Biotechnology , : , 2022
Abstract : Urethanase (EC 3.5.1.75) can reduce ethyl carbamate (EC), a group 2A carcinogen found in foods and liquor. However, it is not yet commercially available. Urethanase has been detected as an intracellular enzyme from yeast, filamentous fungi, and bacteria. Based on the most recent progress in the sequence analysis of this enzyme, it was observed that amidase-type enzyme can degrade EC. All five enzymes had highly conserved sequences of amidase signature family, and their molecular masses were in the range of 52-62 kDa. The enzymes of Candida parapsilosis and Aspergillus oryzae formed a homotetramer, and that of Rhodococcus equi strain TB-60 existed as a monomer. Most urethanases exhibited amidase activity, and those of C. parapsilosis and A. oryzae also demonstrated high activity against acrylamide, which is a group 2A carcinogen. It was recently reported that urease and esterase also exhibited urethanase activity. Although research on the enzymatic degradation of EC has been very limited, recently some sequences of EC-degrading enzyme have been elucidated, and it is anticipated that new enzymes would be developed and applied into practical use. KEY POINTS: Recently, some urethanase sequences have been elucidated The amino acid residues that formed the catalytic triad were conserved Urethanase shows amidase activity and can also degrade acrylamide.
ESTHER : Masaki_2022_Appl.Microbiol.Biotechnol__
PubMedSearch : Masaki_2022_Appl.Microbiol.Biotechnol__
PubMedID: 35536404

Title : Cutinase-like biodegradable plastic-degrading enzymes from phylloplane yeasts have cutinase activity - Ueda_2021_Biosci.Biotechnol.Biochem__
Author(s) : Ueda H , Tabata J , Seshime Y , Masaki K , Sameshima-Yamashita Y , Kitamoto H
Ref : Biosci Biotechnol Biochem , : , 2021
Abstract : Phylloplane yeast genera Pseudozyma and Cryptococcus secrete biodegradable plastic (BP)-degrading enzymes, termed cutinase-like enzymes (CLEs). Although, CLEs contain highly conserved catalytic sites, the whole protein exhibits >= 30% amino acid sequence homology with cutinase. In this study, we analyzed whether CLEs exhibit cutinase activity. Seventeen Cryptococcus magnus strains, which degrade BP at 15 degreesC, were isolated from leaves, and identified the DNA sequence of the CLE in one of the strains. Cutin was prepared from tomato leaves and treated with CLEs from three Cryptococcus species (C. magnus, Cryptococcus flavus, and Cryptococcus laurentii) and Pseudozyma antarctia (PaE). A typical cutin monomer, 10,16-dihydroxyhexadecanoic acid, was detected in extracts of the reaction solution via gas chromatography-mass spectrometry, showing that cutin was indeed degraded by CLEs. In addition to the aforementioned monomer, separation analysis via thin-layer chromatography detected high-molecular-weight products resulting from the breakdown of cutin by PaE, indicating that PaE acts as an endo-type enzyme.
ESTHER : Ueda_2021_Biosci.Biotechnol.Biochem__
PubMedSearch : Ueda_2021_Biosci.Biotechnol.Biochem__
PubMedID: 34160605

Title : Isolation and screening of biopolymer-degrading microorganisms from northern Thailand - Penkhrue_2015_World.J.Microbiol.Biotechnol_31_1431
Author(s) : Penkhrue W , Khanongnuch C , Masaki K , Pathom-Aree W , Punyodom W , Lumyong S
Ref : World J Microbiol Biotechnol , 31 :1431 , 2015
Abstract : Forty agricultural soils were collected from Chiang Mai and Lampang provinces in northern Thailand. Bacteria, actinomycetes and fungi were isolated and screened for their ability to degrade polylactic acid (PLA), polycaprolactone (PCL) and poly(butylene succinate) (PBS) by the agar diffusion method. Sixty-seven actinomycetes, seven bacteria and five fungal isolates were obtained. The majority of actinomycetes were Streptomyces based on morphological characteristic, chemotaxonomy and 16S rRNA gene data. Seventy-nine microorganisms were isolated from 40 soil samples. Twenty-six isolates showed PLA-degradation (32.9 %), 44 isolates showed PBS-degradation (55.7 %) and 58 isolates showed PCL-degradation (73.4 %). Interestingly, 16 isolates (20.2 %) could degrade all three types of bioplastics used in this study. The Amycolatopsis sp. strain SCM_MK2-4 showed the highest enzyme activity for both PLA and PCL, 0.046 and 0.023 U/mL, respectively. Moreover, this strain produced protease, esterase and lipase on agar plates. Approximately, 36.7 % of the PLA film was degraded by Amycolatopsis sp. SCM_MK2-4 after 7 days of cultivation at 30 degreesC in culture broth.
ESTHER : Penkhrue_2015_World.J.Microbiol.Biotechnol_31_1431
PubMedSearch : Penkhrue_2015_World.J.Microbiol.Biotechnol_31_1431
PubMedID: 26135516

Title : Heterologous production of horseradish peroxidase C1a by the basidiomycete yeast Cryptococcus sp. S-2 using codon and signal optimizations - Utashima_2014_Appl.Microbiol.Biotechnol_98_7893
Author(s) : Utashima Y , Matsumoto H , Masaki K , Iefuji H
Ref : Applied Microbiology & Biotechnology , 98 :7893 , 2014
Abstract : In the present study, we attempted to improve the production of recombinant horseradish peroxidase C1a (HRP-C1a; a heme-binding protein) by Cryptococcus sp. S-2. Both native and codon-optimized HRP-C1a genes were expressed under the control of a high-level expression promoter. When the HRP-C1a gene with native codons was expressed, poly(A) tails tended to be added within the coding region, producing truncated messenger RNAs (mRNAs) that lacked the 3' ends. Codon optimization prevented polyadenylation within the coding region and increased both the mRNA and protein levels of active HRP-C1a. To improve secretion of the recombinant protein, we tested five types of N-terminal signal peptide (NTP). These included the native HRP-C1a NTP (C1a-NTP), short and long xylanase secretion signals (X1-NTP and X2-NTP), cutinase signal (C-NTP), and amylase signal (A-NTP), with and without a C-terminal propeptide (CTP). X2-NTP without CTP resulted in the highest HRP-C1a secretion into the culture medium. HRP-C1a secretion was further increased by using xylose fed-batch fermentation. The production of HRP-C1a in this study was 2.7 and 15 times higher than the production reported in previous studies that used insect cell and Pichia expression systems, respectively.
ESTHER : Utashima_2014_Appl.Microbiol.Biotechnol_98_7893
PubMedSearch : Utashima_2014_Appl.Microbiol.Biotechnol_98_7893
PubMedID: 24928655

Title : Construction of a new recombinant protein expression system in the basidiomycetous yeast Cryptococcus sp. strain S-2 and enhancement of the production of a cutinase-like enzyme - Masaki_2012_Appl.Microbiol.Biotechnol_93_1627
Author(s) : Masaki K , Tsuchioka H , Hirano T , Kato M , Ikeda H , Iefuji H
Ref : Applied Microbiology & Biotechnology , 93 :1627 , 2012
Abstract : Yeast host-vector systems have been very successful in expressing recombinant proteins. However, because there are some proteins that cannot be expressed with existing systems, there is a need for new yeast expression systems. Here we describe a new host-vector system based on the basidiomycetous yeast Cryptococcus sp. strain S-2 (S-2). Two advantages of S-2 are that it naturally produces some very useful enzymes, so it would be a good system for expressing multiple copies of some of its genes, and that, it is a nonhazardous species. The orotate phosphoribosyltransferase (OPRTase, EC 2.4.2.10) gene (URA5) was selected as a selectable marker for transformation in the new host-vector system. URA5 was isolated and introduced into a uracil auxotroph of S-2 by electroporation. To demonstrate the S-2 system, we selected one of its unique enzymes, a plastic-degrading cutinase-like enzyme (CLE). We were able to insert multiple copies of the CLE gene (CLE1) into the chromosomes in a high fraction of the targeted cells. Under optimal conditions, one transformant exhibited 3.5 times higher CLE activity than the wild type. Expression vectors, including an inducible promoter (the promoter for the xylanase or alpha-amylase gene), were constructed for recombinant protein production, and green fluorescent protein was expressed under the control of these promoters. The xylanase promoter was more tightly controlled. Furthermore, putting CLE1 under the control of the xylanase promoter, which is induced by xylose, increased CLE activity of the culture medium to approximately 15 times greater than that of the wild type.
ESTHER : Masaki_2012_Appl.Microbiol.Biotechnol_93_1627
PubMedSearch : Masaki_2012_Appl.Microbiol.Biotechnol_93_1627
PubMedID: 22083278

Title : Different enantioselectivity of two types of poly(lactic acid) depolymerases toward poly(l-lactic acid) and poly(d-lactic acid) - Kawai_2011_Polym.Degrad.Stab_96_1342
Author(s) : Kawai F , Nakadai K , Nishioka E , Nakajima H , Ohara H , Masaki K , Iefuji H
Ref : Polymer Degradation and Stability , 96 :1342 , 2011
Abstract : Poly(lactic acid) (PLA) depolymerases are categorized into protease-type and lipase-type. Protease-types can hydrolyze poly(L-lactic acid) (PLLA) but not poly(D-lactic acid) (PDLA). Lipase-types, including cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2 preferentially hydrolyze PDLA. Both enzymes degraded not only PLA emulsion but also PLA film, in which amorphous region is preferentially attacked, but crystalline region can be also attacked. Stereocomplex PLA (sc-PLA) formed by 50:50 blending of PLLA and PDLA included no homo crystals, but a tiny homo crystallization peak appeared and crystallinity increased by 5% when attacked by CLE, although no significant change of molecular weight and crystalline size was found. Enantioselective degradation must occur in amorphous region of PLLA/PDLA film and preferentially hydrolyzed PDLA, resulting in a slightly excess amount of PLLA remained, which must be crystallized
ESTHER : Kawai_2011_Polym.Degrad.Stab_96_1342
PubMedSearch : Kawai_2011_Polym.Degrad.Stab_96_1342
PubMedID:
Gene_locus related to this paper: crysp-Q874E9

Title : Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2 - Kodama_2009_Proteins_77_710
Author(s) : Kodama Y , Masaki K , Kondo H , Suzuki M , Tsuda S , Nagura T , Shimba N , Suzuki E , Iefuji H
Ref : Proteins , 77 :710 , 2009
Abstract : The structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 A resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity.
ESTHER : Kodama_2009_Proteins_77_710
PubMedSearch : Kodama_2009_Proteins_77_710
PubMedID: 19544571
Gene_locus related to this paper: crysp-Q874E9

Title : Cutinase-like enzyme from the yeast Cryptococcus sp. strain S-2 hydrolyzes polylactic acid and other biodegradable plastics - Masaki_2005_Appl.Environ.Microbiol_71_7548
Author(s) : Masaki K , Kamini NR , Ikeda H , Iefuji H
Ref : Applied Environmental Microbiology , 71 :7548 , 2005
Abstract : A purified lipase from the yeast Cryptococcus sp. strain S-2 exhibited remote homology to proteins belonging to the cutinase family rather than to lipases. This enzyme could effectively degrade the high-molecular-weight compound polylactic acid, as well as other biodegradable plastics, including polybutylene succinate, poly (epsilon-caprolactone), and poly(3-hydroxybutyrate).
ESTHER : Masaki_2005_Appl.Environ.Microbiol_71_7548
PubMedSearch : Masaki_2005_Appl.Environ.Microbiol_71_7548
PubMedID: 16269800
Gene_locus related to this paper: crysp-Q874E9