Laminarinase from Penicillium funiculosum and its role in release of beta-glucosidase.
An extracellular laminarinase (1----3)-beta-glucan glucohydrolase (EC 3.2.1.6) was purified from culture filtrates of Penicillium funiculosum. It was homogeneous on polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate. It had a Mr of 14,000 and isoelectric point of pH 4.2. The apparent Km value for lamimarinase was 8.3 mg/ml and Vmax was 8 mumol/min/mg. The distribution of beta-glucosidase activity in two different species of Penicillium showed that P. funiculosum had a higher ratio of extracellular to cell wall bound activity than Penicillium janthinellum. Treatment of mycelia of both species with NaCl, EDTA, Triton X-100, or proteolytic enzymes did not release the cell wall bound beta-glucosidase. Incubation of the mycelia with the laminarinase released 2-4 times more beta-glucosidase than the estimated cell bound activity in P. janthinellum and P. funiculosum.
Rao
M
M
Division of Biochemical Sciences, National Chemical Laboratory, Pune, India.
Deshpande
V V
VV
Gaikwad
S
S
Mishra
C
C
D002473:Cell Wall / Q000187:drug effects / Q000201:enzymology; D004693:Glucan Endo-1,3-beta-D-Glucosidase / Q000302:isolation & purification / Q000378:metabolism* / Q000494:pharmacology; D007526:Isoelectric Point; D007700:Kinetics; D008970:Molecular Weight; D010407:Penicillium / Q000187:drug effects / Q000201:enzymology*; D013379:Substrate Specificity; D001617:beta-Glucosidase / Q000378:metabolism*
D001617:beta-Glucosidase; D004693:Glucan Endo-1,3-beta-D-Glucosidase