The nucleotide sequence depicted in Figure 1 has been submitted to the DDBJ nucleotide sequence database under the accession no. AB104898. A gene encoding endo-beta-(1-->6)-galactanase from Trichoderma viride was cloned by reverse transcriptase-PCR and expressed in Escherichia coli. The gene contained an open reading frame consisting of 1437 bp (479 amino acids). The deduced amino acid sequence of the protein showed little similarity with other known glycoside hydrolases. A signal sequence (20 amino acids) was found at the N-terminal region of the protein and the molecular mass of the mature form was calculated to be 50.488 kDa. The gene product expressed in E. coli as a recombinant protein fused with thioredoxin and His(6) tags had almost the same substrate specificity and mode of action as native enzyme purified from a commercial cellulase preparation of T. viride, i.e. recombinant enzyme endo-hydrolysed beta-(1-->6)-galacto-oligomers with a DP (degree of polymerization) higher than 3, and it could also hydrolyse alpha-L-arabinofuranosidase-treated arabinogalactan protein from radish. It produced beta-(1-->6)-galacto-oligomers ranging from DP 2 to at least 8 at the initial hydrolysis stage and galactose and beta-(1-->6)-galactobiose as the major products at the final reaction stage. These results indicate that the cloned gene encodes an endo-beta-(1-->6)-galactanase. As far as we know, this is the first time an endo-beta-(1-->6)-galactanase has been cloned.

The presence of sufficient genetic variability, the knowledge of nature of association among different characters and relative contribution of different characters to yield is a prerequisite to any breeding programme. The aim of the present study was to estimate genetic parameters of thirteen yield and yield attributing traits in 40 landraces of rice with a view to select better yield attributes in rice. The higher value of phenotypic co-efficient of variation (PCV) compared to the corresponding genotypic coefficient of variation (GCV) for all the studied traits indicated that there was an influence of the environment. Number of unfilled grains per panicle exhibited high estimates of PCV and GCV followed by number of filled grains per panicle, number of grains per panicle, flag leaf area. High heritability coupled with high genetic advance was observed in flag leaf area, pollen fertility, number of grains per panicle and number of filled grains per panicle which reflected that the direct selection of these characters based on phenotypic expression by simple selection method for yield improvement would be more reliable Grain yield per plant showed significant and positive association with days to 50% flowering, days to maturity, flag leaf area, number of total tillers per hill, number of effective tillers per hill, pollen fertility, number of grains per panicle, number of filled grains per panicle indicating selection of these characters for yield improvement may be rewarding. Both at phenotypic and genotypic level, days to 50% flowering, flag leaf area, number of effective tillers per hill, pollen fertility, panicle length, number of grains per panicle and 100 seed weight had direct positive effect on yield per plant indicating their importance during selection in yield improvement program. Moreover, the information generated from this study, can be exploited in future rice breeding program. J. Bangladesh Agril. Univ. 17(1): 26–32, March 2019

A beta-glucuronidase purified from a commercial pectolytic enzyme preparation of Aspergillus niger hydrolyzed about half of the 4-O-methyl-glucuronic acid (4-Me-GlcA) residues located at the nonreducing terminals of (1-->6)-linked beta-galactosyl side chains of the carbohydrate portion of a radish arabinogalactan-protein (AGP) modified by treatment with fungal alpha-L-arabinosidase. Digestion of the alpha-L-arabinosidase-treated AGP with exo-beta-(1-->3)-galactanase released, by exo-fission of beta-(1-->3)-galactosidic bonds in the backbone chains of the AGP, neutral beta-(1-->6)-galactooligosaccharides with various chain lengths and their acidic derivatives substituted at their nonreducing terminals with 4-Me-beta-GlcA groups. In contrast, successive digestion of the alpha-L-arabinosidase-treated AGP with beta-glucuronidase followed by exo-beta-(1-->3)-galactanase liberated much higher amounts of beta-(1-->6)-galactooligomers together with a small portion of short acidic oligomers, mainly 4-Me-beta-GlcA-(1-->6)-Gal and 4-Me-beta-GlcA-(1-->6)-beta-Gal-(1-->6)-Gal. These results indicate that beta-glucuronidase acts upon 4-Me-beta-GlcA residues in long (1-->6)-linked beta-galactosyl side chains of the AGP, whereas short acidic side chains survive the attack of the enzyme.

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We investigated the properties of a galactosyltransferase (GalT) that is involved in the synthesis of beta-(1-->4)-galactan side chains of pectins. A membrane preparation of etiolated 6-day-old soybean ( Glycine max Merr.) hypocotyls transferred [(14)C]Gal from UDP-[(14)C]Gal into intact and partially hydrolyzed lupin beta-(1-->4)-galactans of various chain lengths as exogenous acceptors, while activity to endogenous acceptors was negligible. Maximal activity occurred at pH 6.5 and 20-25 degrees C in the presence of 25 mM Mn(2+) and 0.75% Triton X-100. The transfer reaction onto the unmodified commercial pectic galactan ( M(r)>150000) from lupin we used was very low but increased when the M(r) of the galactan was reduced by partial acid hydrolysis. Among the partially hydrolyzed galactans, high- M(r) (average M(r) 60000) beta-(1-->4)-galactan was a more efficient acceptor [specific activity 2000-3000 pmol min(-1) (mg protein)(-1)] than low- M(r) (average M(r) 10000 and 5000) polymers. Digestion of the radiolabeled product from high- M(r) galactan with endo-beta-(1-->4)-galactanase released mainly radioactive beta-(1-->4)-galactobiose and Gal, indicating that the transfer of [(14)C]Gal occurred through beta-(1-->4)-linkages. HPLC analysis showed that the enzyme also catalyzes incorporation of Gal into pyridylaminated (PA) beta-(1-->4)-galactooligomers with degree of polymerization at least 5. Gal(7)-PA chains were elongated by attachment of one, two, or three Gal residues leading to the formation of Gal(8-10)-PA.