Kazuo Sakka

4.9k total citations
182 papers, 3.9k citations indexed

About

Kazuo Sakka is a scholar working on Biomedical Engineering, Biotechnology and Molecular Biology. According to data from OpenAlex, Kazuo Sakka has authored 182 papers receiving a total of 3.9k indexed citations (citations by other indexed papers that have themselves been cited), including 109 papers in Biomedical Engineering, 107 papers in Biotechnology and 87 papers in Molecular Biology. Recurrent topics in Kazuo Sakka's work include Biofuel production and bioconversion (107 papers), Enzyme Production and Characterization (91 papers) and Studies on Chitinases and Chitosanases (30 papers). Kazuo Sakka is often cited by papers focused on Biofuel production and bioconversion (107 papers), Enzyme Production and Characterization (91 papers) and Studies on Chitinases and Chitosanases (30 papers). Kazuo Sakka collaborates with scholars based in Japan, Thailand and South Africa. Kazuo Sakka's co-authors include Kunio Ohmiya, Shuichi Karita, Tetsuya Kimura, Makiko Sakka, Khanok Ratanakhanokchai, Paripok Phitsuwan, Takeshi Kimura, Kenji Morimoto, Kyo Shimada and Tetsuya Kimura and has published in prestigious journals such as Journal of Biological Chemistry, Applied and Environmental Microbiology and Bioresource Technology.

In The Last Decade

Kazuo Sakka

180 papers receiving 3.8k citations

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Kazuo Sakka Japan 34 2.5k 2.0k 2.0k 1.1k 467 182 3.9k
Kunio Ohmiya Japan 37 2.3k 0.9× 2.2k 1.1× 2.6k 1.3× 1.6k 1.5× 648 1.4× 217 4.7k
Vladimir V. Zverlov Russia 37 2.4k 1.0× 1.4k 0.7× 2.0k 1.0× 687 0.7× 428 0.9× 114 3.7k
Shuichi Karita Japan 32 1.8k 0.7× 1.4k 0.7× 1.5k 0.7× 836 0.8× 381 0.8× 133 3.0k
Verawat Champreda Thailand 38 3.0k 1.2× 1.0k 0.5× 2.1k 1.1× 641 0.6× 327 0.7× 196 4.5k
Akihiko Kosugi Japan 31 2.0k 0.8× 1.1k 0.6× 1.5k 0.7× 607 0.6× 308 0.7× 134 3.2k
Rodney J. Bothast United States 45 3.4k 1.4× 995 0.5× 2.9k 1.4× 1.4k 1.4× 714 1.5× 134 5.4k
Bjørge Westereng Norway 35 3.3k 1.3× 1.8k 0.9× 2.9k 1.5× 2.2k 2.1× 629 1.3× 70 5.8k
Timothy D. Leathers United States 34 1.1k 0.4× 782 0.4× 1.4k 0.7× 1.2k 1.2× 407 0.9× 108 3.3k
Matti Siika‐aho Finland 43 4.3k 1.7× 2.1k 1.1× 2.5k 1.2× 1.6k 1.5× 622 1.3× 134 5.8k
Hubert Bahl Germany 39 2.0k 0.8× 642 0.3× 3.2k 1.6× 634 0.6× 387 0.8× 93 4.5k

Countries citing papers authored by Kazuo Sakka

Since Specialization
Citations

This map shows the geographic impact of Kazuo Sakka's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Kazuo Sakka with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Kazuo Sakka more than expected).

Fields of papers citing papers by Kazuo Sakka

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kazuo Sakka. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Kazuo Sakka. The network helps show where Kazuo Sakka may publish in the future.

Co-authorship network of co-authors of Kazuo Sakka

This figure shows the co-authorship network connecting the top 25 collaborators of Kazuo Sakka. A scholar is included among the top collaborators of Kazuo Sakka based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Kazuo Sakka. Kazuo Sakka is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Sakka, Makiko, Akihiko Kosugi, Hirotaka Katsuzaki, et al.. (2020). Significance of a family-6 carbohydrate-binding module in a modular feruloyl esterase for removing ferulic acid from insoluble wheat arabinoxylan. Enzyme and Microbial Technology. 138. 109546–109546. 7 indexed citations
2.
Sakka, Makiko, et al.. (2019). The modular arabinanolytic enzyme Abf43A-Abf43B-Abf43C from Ruminiclostridium josui consists of three GH43 modules classified in different subfamilies. Enzyme and Microbial Technology. 124. 23–31. 5 indexed citations
3.
Wang, Yayun, Makiko Sakka, Satoshi Kaneko, et al.. (2018). Ruminiclostridium josui Abf62A-Axe6A: A tri-functional xylanolytic enzyme exhibiting α-l-arabinofuranosidase, endoxylanase, and acetylxylan esterase activities. Enzyme and Microbial Technology. 117. 1–8. 14 indexed citations
4.
Sakka, Makiko, et al.. (2017). Characterization of Ruminiclostridium josui arabinoxylan arabinofuranohydrolase, RjAxh43B, and RjAxh43B-containing xylanolytic complex. Enzyme and Microbial Technology. 104. 37–43. 13 indexed citations
5.
Baramee, Sirilak, Paripok Phitsuwan, Rattiya Waeonukul, et al.. (2017). Chemical Pretreatment-Independent Saccharifications of Xylan and Cellulose of Rice Straw by Bacterial Weak Lignin-Binding Xylanolytic and Cellulolytic Enzymes. Applied and Environmental Microbiology. 83(22). 27 indexed citations
6.
7.
Sakka, Makiko, et al.. (2014). Essential role of a family‐32 carbohydrate‐binding module in substrate recognition by Clostridium thermocellum mannanase CtMan5A. FEBS Letters. 588(9). 1726–1730. 16 indexed citations
8.
Karita, Shuichi, Ana S. Luís, Makiko Sakka, et al.. (2012). Influence of a Mannan Binding Family 32 Carbohydrate Binding Module on the Activity of the Appended Mannanase. Applied and Environmental Microbiology. 78(14). 4781–4787. 27 indexed citations
9.
Jindou, Sadanari, et al.. (2010). Analysis of cohesin-dockerin interactions using mutant dockerin proteins. FEMS Microbiology Letters. 314(1). 75–80. 17 indexed citations
10.
Jindou, Sadanari, et al.. (2009). Unusual binding properties of the dockerin module ofClostridium thermocellumendoglucanase CelJ (Cel9D-Cel44A). FEMS Microbiology Letters. 300(2). 249–255. 11 indexed citations
11.
Zhao, Guangshan, et al.. (2006). Different Binding Specificities of S-Layer Homology Modules fromClostridium thermocellumAncA, Slp1, and Slp2. Bioscience Biotechnology and Biochemistry. 70(7). 1636–1641. 13 indexed citations
12.
Ali, Ehsan, Guangshan Zhao, Makiko Sakka, et al.. (2005). Functions of Family-22 Carbohydrate-Binding Module inClostridium thermocellumXyn10C. Bioscience Biotechnology and Biochemistry. 69(1). 160–165. 18 indexed citations
13.
Zhao, Guangshan, Ehsan Ali, Makiko Sakka, Tetsuya Kimura, & Kazuo Sakka. (2005). Binding of S-layer homology modules from Clostridium thermocellum SdbA to peptidoglycans. Applied Microbiology and Biotechnology. 70(4). 464–469. 25 indexed citations
14.
Jindou, Sadanari, Tsutomu Kajino, Minoru Inagaki, et al.. (2004). Interaction between a Type-II Dockerin Domain and a Type-II Cohesin Domain fromClostridium thermocellumCellulosome. Bioscience Biotechnology and Biochemistry. 68(4). 924–926. 23 indexed citations
15.
Katō, Susumu, Tetsuya Kimura, Kazuo Sakka, et al.. (2004). Analysis of estrogen-like compounds in the environment by high performance liquid chromatography bioassay. Journal of Bioscience and Bioengineering. 97(3). 216–218. 4 indexed citations
16.
Katō, Susumu, Tetsuya Kimura, Kazuo Sakka, et al.. (2003). The Behavior of Estrogenic Substances in Ago Bay. Journal of Japan Society on Water Environment. 26(11). 687–692. 3 indexed citations
17.
Kimura, Tetsuya, et al.. (2000). Analysis of the Promoter Activity of the Taka-Amylase Gene and the Phosphoglycerate Kinase Gene in a Shoyu-koji Mold Aspergillus oryzae KBN616.. Food Science and Technology Research. 6(1). 44–47. 1 indexed citations
18.
Kimura, Tetsuya, Jun Ito, Akihiro Kawano, et al.. (2000). Purification, Characterization, and Molecular Cloning of Acidophilic Xylanase fromPenicilliumsp.40. Bioscience Biotechnology and Biochemistry. 64(6). 1230–1237. 60 indexed citations
19.
Suzuki, Hayato, Hirofumi Furuhashi, Kenji Morimoto, et al.. (2000). Molecular Cloning, Overexpression, and Purification of a Major Xylanase fromAspergillus oryzae. Bioscience Biotechnology and Biochemistry. 64(12). 2734–2738. 31 indexed citations
20.
Sakka, Kazuo, et al.. (1985). Purification and Some Properties of Serine Proteinase from a Mutant of Aspergillus niger. Journal of Fermentation Technology. 63(5). 479–483. 11 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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