Eri Tabata

ORCID: 0000-0003-2564-2125
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About
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Research Areas
  • Studies on Chitinases and Chitosanases
  • Invertebrate Immune Response Mechanisms
  • Nanocomposite Films for Food Packaging
  • Protein Hydrolysis and Bioactive Peptides
  • Insect symbiosis and bacterial influences
  • Animal Nutrition and Physiology
  • Pineapple and bromelain studies
  • Aquaculture Nutrition and Growth
  • Insect Utilization and Effects
  • Silk-based biomaterials and applications
  • Entomopathogenic Microorganisms in Pest Control
  • Legume Nitrogen Fixing Symbiosis

Kogakuin University
2016-2024

Japan Society for the Promotion of Science
2018-2024

Abstract Chitin, a polymer of N -acetyl-D-glucosamine (GlcNAc), functions as major structural component in chitin-containing organism including crustaceans, insects and fungi. Recently, we reported that acidic chitinase (Chia) is highly expressed mouse, chicken pig stomach tissues it can digest chitin the respective gastrointestinal tracts (GIT). In this study, focus on livestock domestic animals show levels Chia mRNA their are governed by feeding behavior. were significantly lower bovine...

10.1038/s41598-018-19940-8 article EN cc-by Scientific Reports 2018-01-17

Abstract Chitinases are enzymes that hydrolyze chitin, a polymer of β-1, 4-linked N -acetyl-D-glucosamine (GlcNAc). Chitin has long been considered as source dietary fiber is not digested in the mammalian digestive system. Here, we provide evidence acidic chitinase (AMCase) can function major enzyme constitutively degrades chitin substrates and produces (GlcNAc) 2 fragments mouse gastrointestinal environment. AMCase was resistant to endogenous pepsin C digestion remained active stomach...

10.1038/srep37756 article EN cc-by Scientific Reports 2016-11-24

Abstract Chitin, a polymer of N -acetyl-D-glucosamine (GlcNAc), functions as major structural component in crustaceans, insects and fungi is the second most abundant polysaccharide nature. Although these chitin-containing organisms have been suggested novel animal feed resources, chitin has long considered indigestible fibers body. Recently, we reported that acidic chitinase (Chia) protease-resistant glycosidase mouse gastrointestinal tract (GIT) it digests stomach. However, physiological...

10.1038/s41598-017-07146-3 article EN cc-by Scientific Reports 2017-07-21

Chitin, a polymer of N-acetyl-D-glucosamine (GlcNAc), is major structural component in chitin-containing organism including crustaceans, insects and fungi. Mammals express two chitinases, chitotriosidase (Chit1) acidic mammalian chitinase (AMCase). Here, we report that pig AMCase stable the presence other digestive proteases functions as chitinolytic enzyme under gastrointestinal conditions. Quantification chitinases expression tissues using quantitative real-time PCR showed Chit1 mRNA was...

10.1038/s41598-017-13526-6 article EN cc-by Scientific Reports 2017-10-05

Abstract Chitin is a polymer of N -acetyl-D-glucosamine (GlcNAc) and main constituent insects’ exoskeleton. Insects are rich in protein with high energy conversion efficiency. Recently, we have reported that acidic chitinases (Chia) act as digestive enzymes mouse, pig chicken (omnivorous) but not dog (carnivorous) bovine (herbivorous), indicating feeding behavior affects Chia expression levels, determines chitin digestibility the particular animals. Common marmoset ( Callithrix jacchus )...

10.1038/s41598-018-36477-y article EN cc-by Scientific Reports 2019-01-12

Abstract Commercially available porcine pepsin preparations have been used for the production of chitooligosaccharides with various biomedical activities. However, origin this activity is not well understood. Here we show that chitosan-degrading conferred by residues chitinolytic truncated forms acidic chitinase (Chia) persisting in preparation. Chia an acid-stable and pepsin-resistant enzyme degrades chitin to produce N -acetyl-D-glucosamine dimer. We found can be under stomach-like...

10.1038/s41598-019-52136-2 article EN cc-by Scientific Reports 2019-10-30

Abstract Acidic chitinase (Chia) digests the chitin of insects in omnivorous stomach and activity carnivorous Chia is significantly lower than that enzyme. However, mechanistic evolutionary insights into functional changes remain unclear. Here we show a noninsect-based diet has caused structural during course evolution Carnivora. By creating mouse-dog chimeric proteins modifying amino acid sequences, revealed F214L A216G substitutions led to dog enzyme activation. In 31 Carnivora, was...

10.1093/molbev/msab331 article EN Molecular Biology and Evolution 2021-11-16

Acidic chitinase (Chia) has been implicated in asthma, allergic inflammations, and food processing. We have purified Chia enzymes with striking acid stability protease resistance from chicken pig stomach tissues using a chitin column 8 M urea (urea-Chia). Here, we report that acetic is suitable agent for native purification the (acetic acid-Chia). protein can be eluted 0.1 (pH 2.8), but not by Gly-HCl 2.5) or sodium acetate 4.0 5.5). The melting temperatures of are affected substantially...

10.3390/ijms19020362 article EN International Journal of Molecular Sciences 2018-01-25

Diet of the crab-eating monkey (Macaca fascicularis) consists both plants and animals, including chitin-containing organisms such as crabs insects. This omnivorous has a high expression acidic chitinase (CHIA) in stomach here, we report on its enzymatic properties under different conditions. When compared with Mus musculus CHIA (Mm-CHIA), Macaca fascicularis (Mf-CHIA) exhibits higher chitinolytic activity at broad pH (1.0-7.0) temperature (30-70 ℃) range. Interestingly, optimum (5.0),...

10.1038/s41598-021-95010-w article EN cc-by Scientific Reports 2021-07-29

Placental mammals' ancestors were insectivores, suggesting that modern mammals may have inherited the ability to digest insects. Acidic chitinase (Chia) is a crucial enzyme hydrolyzing significant component of insects' exoskeleton in many species. On other hand, herbivorous animal groups, such as cattle, extremely low activity compared omnivorous species, e.g., mice. The cattle Chia has been attributed R128H mutation. presence either these amino acids correlates with feeding behavior...

10.1016/j.isci.2023.107254 article EN cc-by iScience 2023-07-03

Chitooligosaccharides, the degradation products of chitin and chitosan, possess anti-bacterial, anti-tumor, anti-inflammatory activities. The enzymatic production chitooligosaccharides may increase interest in their potential biomedical or agricultural usability terms safety simplicity manufacturing process. Crab-eating monkey acidic chitinase (CHIA) is an enzyme with robust activity various environments. Here, we report efficient chitosan by CHIA under high-temperature conditions. Monkey...

10.3390/molecules27020409 article EN cc-by Molecules 2022-01-09

Mice and humans express two active chitinases: acidic mammalian chitinase (AMCase) chitotriosidase (CHIT1). Both chitinases are thought to play important roles in specific pathophysiological conditions. The crab-eating monkey (Macaca fascicularis) is one of the most frequently used nonhuman primate models basic applied biomedical research. Here, we performed gene expression analysis normal tissues by way quantitative real-time polymerase chain reaction (qPCR) using a single standard DNA...

10.3390/genes9050244 article EN Genes 2018-05-09

Chitooligosaccharides exhibit several biomedical activities, such as inflammation and tumorigenesis reduction in mammals. The mechanism of the chitooligosaccharides' formation vivo has been, however, poorly understood. Here we report that mouse acidic chitinase (Chia), which is widely expressed tissues, can produce chitooligosaccharides from deacetylated chitin (chitosan) at pH levels corresponding to stomach lung tissues. Chia degraded N-acetyl-d-glucosamine (GlcNAc) dimers. block-type...

10.3390/molecules26216706 article EN cc-by Molecules 2021-11-05

Ym1 (chitinase-like 3, Chil3) expressed in mice is a nonenzymatic chitinase-like protein, which shows 67% identity with mouse acidic chitinase (Chia). Similar to Chia, overexpressed asthma and parasitic infections lungs. Due the lack of chitin-degrading activity, biomedical role under these pathophysiological conditions remains be determined. In this study, we investigated what region amino acid changes resulted loss enzymatic activity. Replacing two acids at catalytic motif obtain Chia-like...

10.1002/pro.4620 article EN Protein Science 2023-03-08
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