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Dioscorea opposita Thunb. a-mannosidase belongs to the glycosyl hydrolase family 38

100%

Uno Y. , Hashidume S. , Kurita O. , Fujiwara T. , Nomura K.

nr 4

α-Mannosidase (EC 3.2.1.24) was purified from ‘Iseimo’, a native variety of Dioscorea opposita Thunb. Before purification, we investigated the composition of a viscous polysaccharide that interferes with column chromatography procedures. The polysaccharide consisted mainly of mannose, and also contained uronic acid. We used the cationic detergent cetylpyridinium chloride (CPC) to remove the polysaccharide. CPC treatment decreased viscosity without affecting α-mannosidase activity. We purified α-mannosidase 2,650-fold. The optimal pH of the enzyme was 6.0 and the optimum temperature was 65℃. The Km value for p-nitrophenyl-α-D-mannopyranoside was 0.35 ± 0.03 mM. Activity was inhibited by swainsonine but not kifunensine. The enzyme cleaved α-1,2 linkages preferentially to α-1,6 and α-1,3 linkages. The Mr of purified α-mannosidase was estimated to be 250–260 kDa by gel filtration and native-PAGE. Four polypeptides (86, 83, 80, and 28 kDa) were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. It is unclear whether the polypeptides are encoded by one gene or multiple genes. However, N-terminal sequence analysis suggested that post-translational cleavage and/or glycosylation resulted in the three large fragments, if these amino acids were encoded by the same gene. Homology searches and characterization of the enzyme’s properties indicated that Iseimo α-mannosidase belongs to the glycoside hydrolase family 38 proteins, and to the Class II mannosidase group.

Comprehensive analysis of soil nitrogen removal by catch crops based on growth and water use

86%

Yasutake D. , Kondo K. , Yamane S. , Kitano M. , Mori M. , Fujiwara T.

International Agrophysics

2016

tom 30

nr 3

Three dimensional structure of actin-based membrane skeleton as revealed by electron microscopic computed tomograpy of rapidly- frozen, deep-etchen plasma membrane

72%

Morone N. , Kasai R. , Fujiwara T. , Ike H. , Hirata Y. , Yuasa S. , Nishizawa Y. , Wakabayashi T. , Usukura J. , Kusumi A.

nr Supplement 1

Investigation of low temperature plasma capabilities to modify the structure and function of bio-polymers

72%

Motrescu I. , Hara T. , Ogino A. , Tanaka S. , Fujiwara T. , Kawagishi H. , Kodani S. , Popa G. , Nagatsu M.

tom Vol. 3, No. 4

150-152

The possibility to modify biopolymers using low temperature plasma is investigated. Two types of plasma are employed in this study: an atmospheric pressure plasma and a low pressure microwave plasma. In both cases changes of the structure and function of the exposed molecules are reported, the effects being stronger for the low-pressure plasma irradiation.

Chitooligosaccharide plays essential roles in regulating proline metabolism and cold stress tolerance in rice seedlings

72%

Zhang Y. , Fan L. , Zhao M. , Chen Q. , Qin Z. , Feng Z. , Fujiwara T. , Zhao L.

Acta Physiologiae Plantarum

2019

tom 41

nr 06

Rice is one of the most important crops around the world. The cold temperature as a major abiotic stress occurs frequently affecting rice growth and final plant yield. Chitooligosaccharide (COS) has been reported as an elicitor of plant immunity that can improve plant seedling tolerance to cold stress. However, the mechanisms on the enhanced cold tolerance is unclear. Here, we report that the rice seedlings treated by COS demonstrated good cold tolerance with promoted root vigor and plant growth. COS could increase contents of proline and glutamate in the seedlings. Moreover, expression analysis revealed COS significantly induced the transcripts of the key genes associated with the glutamate and proline biosynthesis pathway during cold stress. These results indicate that COS enhanced seedling growth and cold tolerance in rice may be caused by the osmotic regulation through the accumulations of glutamate and proline to provide significant osmo-protection.