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Agricultural and Biological Chemistry is a peer-reviewed journal published by Oxford University Press, covering Enzyme Production and Characterization, Microbial Metabolic Engineering and Bioproduction, Biofuel production and bioconversion.
| Publisher | Oxford University Press |
|---|---|
| Reference style | Author–year (OUP) Author–year — (Smith, 2023) in the text Smith, A., Jones, B. and Lee, C. (2023) 'A representative article title', Agricultural and Biological Chemistry, 12(3), pp. 45–58.
Formats any DOI in the closest standard style — Agricultural and Biological Chemistry has no published style definition, so this is an approximation. No sign-up. |
| Publishes research in | Enzyme Production and Characterization Microbial Metabolic Engineering and Bioproduction Biofuel production and bioconversion Enzyme Catalysis and Immobilization Amino Acid Enzymes and Metabolism |
| ISSN | 0002-1369 |
| h-index | 108 |
| i10-index | 6,711 |
| Total citations | 225,111 |
| Top institutions publishing here | The University of Tokyo |
| Journal website | www.tandfonline.com |
| You get | A submission-ready PDF and the editable LaTeX source — ready to submit. |
Citations each year’s papers have accumulated so far — the most recent years are still building up.
Both whipping and emulsifying properties, the characteristic functional properties of soybean products, were investigated by using the commercial products in Japan. Whipping properties of the soybean products, expressed by foam expansion and foam stability, were found to correlate with water dispersible nitrogen, and the resultant foams were stable when the dissolved proteins were native. Thus,…
Taiji Imoto, Kazuyoshi Yagishita; A Simple Activity Measurement of Lysozyme, Agricultural and Biological Chemistry, Volume 35, Issue 7, 1 July 1971, Pages
A microorganism producing transglutaminase was screened as an indication of hydroxamateform ing activity. The microbial transglutaminase was purified from the culture filtrate of the strain, S-8112, which was supposed to belong to the genus Streptoverticillium. The molecular weight of the purified enzyme was found to be about 40, 000 on SDS-polyacrylamide gel electrophoresis, the isoelectric…
Several microorganisms capable of utilizing 1-aminocyclopropane-1-carboxylate (ACPC) were isolated from soil. A bacterium which belongs to Pseudomonas accumulated cellular α-aminobutyrate with consumption of ACPC and cells incubated with ACPC medium had the activity deaminating the substrate to form α-ketobutyrate. An enzyme, ACPC deaminase, was highly purified and its molecular weight, substrate specificity and absorption spectrum…
Several microorganisms capable of utilizing 1-aminocyclopropane-l-carboxylate (ACPC) were isolated from soil. A bacterium which belongs to Pseudomonas accumulated cellular a-aminobutyrate with consumption of ACPC and cells incubated with ACPC medium had the activity deaminating the substrate to form α-ketobutyrate. An enzyme, ACPC deaminase, was highly purified and its molecular weight, substrate specificity and absorption spectrum…
