Nakayama A

References (5)

Title : Microbial decomposition of biodegradable plastics on the deep-sea floor - Omura_2024_Nat.Commun_15_568
Author(s) : Omura T , Isobe N , Miura T , Ishii S , Mori M , Ishitani Y , Kimura S , Hidaka K , Komiyama K , Suzuki M , Kasuya KI , Nomaki H , Nakajima R , Tsuchiya M , Kawagucci S , Mori H , Nakayama A , Kunioka M , Kamino K , Iwata T
Ref : Nat Commun , 15 :568 , 2024
Abstract : Microbes can decompose biodegradable plastics on land, rivers and seashore. However, it is unclear whether deep-sea microbes can degrade biodegradable plastics in the extreme environmental conditions of the seafloor. Here, we report microbial decomposition of representative biodegradable plastics (polyhydroxyalkanoates, biodegradable polyesters, and polysaccharide esters) at diverse deep-sea floor locations ranging in depth from 757 to 5552 m. The degradation of samples was evaluated in terms of weight loss, reduction in material thickness, and surface morphological changes. Poly(L-lactic acid) did not degrade at either shore or deep-sea sites, while other biodegradable polyesters, polyhydroxyalkanoates, and polysaccharide esters were degraded. The rate of degradation slowed with water depth. We analysed the plastic-associated microbial communities by 16S rRNA gene amplicon sequencing and metagenomics. Several dominant microorganisms carried genes potentially encoding plastic-degrading enzymes such as polyhydroxyalkanoate depolymerases and cutinases/polyesterases. Analysis of available metagenomic datasets indicated that these microorganisms are present in other deep-sea locations. Our results confirm that biodegradable plastics can be degraded by the action of microorganisms on the deep-sea floor, although with much less efficiency than in coastal settings.
ESTHER : Omura_2024_Nat.Commun_15_568
PubMedSearch : Omura_2024_Nat.Commun_15_568
PubMedID: 38278791

Title : Synthesis, Properties, and Biodegradability of Thermoplastic Elastomers Made from 2-Methyl-1,3-propanediol, Glutaric Acid and Lactide - Zahir_2021_Life.(Basel)_11_
Author(s) : Zahir L , Kida T , Tanaka R , Nakayama Y , Shiono T , Kawasaki N , Yamano N , Nakayama A
Ref : Life (Basel) , 11 : , 2021
Abstract : An innovative type of biodegradable thermoplastic elastomers with improved mechanical properties from very common and potentially renewable sources, poly(L-lactide)-b-poly(2-methyl-1,3-propylene glutarate)-b-poly(L-lactide) (PLA-b-PMPG-b-PLA)s, has been developed for the first time. PLA-b-PMPG-b-PLAs were synthesized by polycondensation of 2-methyl-1,3-propanediol and glutaric acid and successive ring-opening polymerization of L-lactide, where PMPG is an amorphous central block with low glass transition temperature and PLA is hard semicrystalline terminal blocks. The copolymers showed glass transition temperature at lower than -40 degreesC and melting temperature at 130-152 degreesC. The tensile tests of these copolymers were also performed to evaluate their mechanical properties. The degradation of the copolymers and PMPG by enzymes proteinase K and lipase PS were investigated. Microbial biodegradation in seawater was also performed at 27 degreesC. The triblock copolymers and PMPG homopolymer were found to show 9-15% biodegradation within 28 days, representing their relatively high biodegradability in seawater. The macromolecular structure of the triblock copolymers of PLA and PMPG can be controlled to tune their mechanical and biodegradation properties, demonstrating their potential use in various applications.
ESTHER : Zahir_2021_Life.(Basel)_11_
PubMedSearch : Zahir_2021_Life.(Basel)_11_
PubMedID: 33445658

Title : Structural evidence that puromycin hydrolase is a new type of aminopeptidase with a prolyl oligopeptidase family fold -
Author(s) : Matoba Y , Nakayama A , Oda K , Noda M , Kumagai T , Nishimura M , Sugiyama M
Ref : Proteins , 79 :2999 , 2011
PubMedID: 21905123
Gene_locus related to this paper: strmo-q2hxd9

Title : The draft genome of Ciona intestinalis: insights into chordate and vertebrate origins - Dehal_2002_Science_298_2157
Author(s) : Dehal P , Satou Y , Campbell RK , Chapman J , Degnan B , De Tomaso A , Davidson B , Di Gregorio A , Gelpke M , Goodstein DM , Harafuji N , Hastings KE , Ho I , Hotta K , Huang W , Kawashima T , Lemaire P , Martinez D , Meinertzhagen IA , Necula S , Nonaka M , Putnam N , Rash S , Saiga H , Satake M , Terry A , Yamada L , Wang HG , Awazu S , Azumi K , Boore J , Branno M , Chin-Bow S , DeSantis R , Doyle S , Francino P , Keys DN , Haga S , Hayashi H , Hino K , Imai KS , Inaba K , Kano S , Kobayashi K , Kobayashi M , Lee BI , Makabe KW , Manohar C , Matassi G , Medina M , Mochizuki Y , Mount S , Morishita T , Miura S , Nakayama A , Nishizaka S , Nomoto H , Ohta F , Oishi K , Rigoutsos I , Sano M , Sasaki A , Sasakura Y , Shoguchi E , Shin-I T , Spagnuolo A , Stainier D , Suzuki MM , Tassy O , Takatori N , Tokuoka M , Yagi K , Yoshizaki F , Wada S , Zhang C , Hyatt PD , Larimer F , Detter C , Doggett N , Glavina T , Hawkins T , Richardson P , Lucas S , Kohara Y , Levine M , Satoh N , Rokhsar DS
Ref : Science , 298 :2157 , 2002
Abstract : The first chordates appear in the fossil record at the time of the Cambrian explosion, nearly 550 million years ago. The modern ascidian tadpole represents a plausible approximation to these ancestral chordates. To illuminate the origins of chordate and vertebrates, we generated a draft of the protein-coding portion of the genome of the most studied ascidian, Ciona intestinalis. The Ciona genome contains approximately 16,000 protein-coding genes, similar to the number in other invertebrates, but only half that found in vertebrates. Vertebrate gene families are typically found in simplified form in Ciona, suggesting that ascidians contain the basic ancestral complement of genes involved in cell signaling and development. The ascidian genome has also acquired a number of lineage-specific innovations, including a group of genes engaged in cellulose metabolism that are related to those in bacteria and fungi.
ESTHER : Dehal_2002_Science_298_2157
PubMedSearch : Dehal_2002_Science_298_2157
PubMedID: 12481130
Gene_locus related to this paper: cioin-141645 , cioin-147959 , cioin-150181 , cioin-154370 , cioin-ACHE1 , cioin-ACHE2 , cioin-cxest , cioin-f6qcp0 , cioin-f6r8z1 , cioin-f6u176 , cioin-f6vac9 , cioin-f6x584 , cioin-f6xa69 , cioin-f6y403 , cioin-h2xqb4 , cioin-H2XTI0 , cioin-F6T1M3 , cioin-H2XUP7 , cioin-CIN.7233 , cioin-F6V269 , cioin-Cin16330 , cioin-h2xua2 , cioin-f6vaa5 , cioin-f6v9x6 , cioin-f6swc9 , cioin-f7amz2 , cioin-f6s021 , cioin-h2xxq9 , cioin-h2xne6 , cioin-f6ynr2

Title : A cDNA resource from the basal chordate Ciona intestinalis -
Author(s) : Satou Y , Yamada L , Mochizuki Y , Takatori N , Kawashima T , Sasaki A , Hamaguchi M , Awazu S , Yagi K , Sasakura Y , Nakayama A , Ishikawa H , Inaba K , Satoh N
Ref : Genesis , 33 :153 , 2002
PubMedID: 12203911
Gene_locus related to this paper: cioin-141645 , cioin-147959 , cioin-150181 , cioin-154370 , cioin-ACHE1 , cioin-ACHE2 , cioin-cxest , cioin-F6V269