国立研究開発法人 国際農林水産業研究センター | JIRCAS

Characterization and Origin of Protease Activity in Cultivated Soils

JARQ : Japan Agricultural Research Quarterly
ISSN
00213551
書誌レコードID(総合目録DB)
AA0068709X
本文フルテキスト

Most organisms, especially non-nitrogen fixers, must decompose to low molecular nitrogenous compounds in order to assimilate nitrogen. Hydrolysis of proteins, like ammonification and nitrification, is an important process in the nitrogen cycle with plays an essential role in soil fertility. Soils have sufficient levels of proteolytic activity to support the nitrogen metabolism in situ in soils. Most soils contained a neutral metalloprotease when protease activity was assayed using N-benzyloxycarbonyl-L-phenylalanyl-L-tyrosyl-Lleucine (Z-Phe-Tyr-Leu) as a substrate. The isoelectric points of the main metalloprotease component in the extract of samples from an Andosol in a tomato field and a Gray Lowland soil in a paddy field were estimated to be 4.9 and 2.9, respectively. The molecular weight of the main metalloprotease component from the Andosol and the Gray Lowland soil was estimated to be 47×103 and 37×103, respectively. The metalloprotease split preferentially the peptide bonds with hydrophobic amino acid residues. Characteristics of the protease activity of paddy field soil under double cropping conditions (rice-wheat) were intermediate between those of an upland soil and a paddy soil under monoculture of rice. Proteolytic Bacillus spp. was a major source of soil protease in water-logged paddy fields.

刊行年月1996-04-01
作成者Koichi HAYANO
データ作成日1996-04-01
国立情報学研究所メタデータ主題語彙集(資源タイプ)Journal Article
30
2
開始ページ79
終了ページ84
言語eng