The present paper comparatively characterized starch and glycogen branching enzymes (BEs) from various organisms. All these BEs examined were purified from recombinant proteins expressed in Escherichia coli ( E. coli ) cells encoding rice BEI (OsBEI), rice BEIIa (OsBEIIa), rice BEIIb (OsBEIIb), E. coli BE (EcoBE), Synechococcus elongatus BE (ScoBE), Saccharomyces cerevisiae BE (SacBE) and human BE (HosBE). All the BEs had commonly the same properties in terms of the minimum chain-length of DP 6 for the transferred chains, that of DP 6 for the residual chain, and hence that of DP 12 for the substrate chains. Detailed analysis of chain-length distribution of the BE reaction products revealed that the chain-length preference of BE can be classified into three types. First, the OsBEI type which included EcoBE formed short to intermediate chains having degree of polymerization (DP) 6－15 with the most abundant chains of DP 6 and 10－12. Second, the OsBEIIb type into which ScoBE was classified transferred almost exclusively very short chains of DP 6 and 7. Third, the OsBEIIa type to which SacBE and HosBE belonged formed very short chains of DP 6 and 7 as OsBEIIb, but it also significantly produced short chains of DP ≦ 10. The optimal temperatures for the catalytic activities of BEs were comparatively low in the range of 20－30°C, and the activities were markedly inhibited by higher temperatures above 30°C with an exception that ScoBE maintained its high activity until 40°C.