Multiple forms of endo-polygalacturonase from Saccharomyces fragilis.

Lim, Jai-Yun; Yamasaki, Yudai; Suzuki, Yukio; Ozawa, Junjiro

doi:10.1271/bbb1961.44.473

Cited by 26 publications

(19 citation statements)

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“…This value is higher than those reported for the endo-PGs I, II and III of K. fragilis (Lim et al, 1980), but similar to those of the pectic enzymes of some phytopathogenic fungi (Cervone et al, 1977). The enzyme had an apparent MWr o f 41000 dal, as estimated by gel filtration on Sephadex G-100 (Fig.…”

Section: Resultssupporting

confidence: 49%

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Production, purification and partial characterization of an endopolygalacturonase fromCryptococcus albidus var.albidus

Federici

1985

Antonie van Leeuwenhoek

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Cryptococcus albidus var. albidus produced an extracellular endo-polygalacturonase (poly (1,4-alpha-D-galacturonide) glycanohydrolase EC 3.2.1.15) when grown in a synthetic medium containing one of a variety of pectic substances or galacturonic acid. The highest level of enzyme activity (15.5 VU X ml-1) was obtained after 72 h of growth on 1.0% low-methoxyl pectin. The enzyme, purified by gel filtration (Sephadex G-100) after repeated ammonium sulphate precipitation and dialysis, showed only one band by polyacrylamide gel electrophoresis and had the following properties: mol wt (MWr) 41000 dal; isoelectric point (pI) = 8.10 +/- 0.10; optimum temperature and pH for activity around 37 degrees C and pH 3.75, respectively; pH stability in the pH range 4.0 to 8.0; complete heat inactivation after 10 min at 55 degrees C; Km and Vmax values 5.7 X 10(-1) mg X ml-1 and 5.1 X 10(-1) mmoles X min-1, respectively.

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Section: Resultssupporting

confidence: 49%

“…Very few yeast species, however, have been thoroughly studied with regard to this capacity. So far, most research has been carried out with Kluyveromyces fragilis (Luh and Phaff, t954;Wimborne and Rickard, 1978;Lim et al, 1980) which, among these microorganisms, is regarded as the most potent producer of pectinase.…”

Section: Introductionmentioning

confidence: 99%

Production, purification and partial characterization of an endopolygalacturonase fromCryptococcus albidus var.albidus

Federici

1985

Antonie van Leeuwenhoek

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“…LKN could be a good PG producer. It also showed a high degree of pectic acid hydrolysis, cleaving about 12% of the bonds when the viscosity was reduced into half and hydrolyzing about 45% of the bonds after 2 h (data not shown but will appear elsewhere), comparable to that of R, arrhizus (I1) and Saccharomyces fragilis (10). In terms of good pH stability and higher temperature tolerance, Rhizopus sp.…”

Section: And Discussionmentioning

confidence: 84%

“…On the basis of PG activity assay, pH optimum of PG was determined at indicated pH by using various buffer pH, i.e., 0.1 M glycine buffer (glycine-HCI, pH 2-3), acetate buffer (pH 3.5-5.5), 0.1 M phosphate buffer (pH 6-8) and 0.1 M sodium carbonate buffer (Na2CO3-NaHCO3, pH [8][9][10][11]. Temperature optimum of PG activity was determined at the range from 20 to 70°C at the optimum pH of the respective enzyme solution.…”

Section: Methodsmentioning

confidence: 99%

Polygalacturonase production by Rhizopus spp.

Elegado¹,

Fujio²

1993

J. Gen. Appl. Microbiol.

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Two good polygalacturonase (PG) producing strains were selected from 21 Rhizopus spp. isolates from `ragi' and fermented foods and from 4 authentic Rhizopus strains. Strain LKN produced 3.2 U/mg protein of crude enzyme extract (0.68 U/g substrate) in 3 days solid culture of pectin and cassava starch supplemented wheat bran. Strain Al 1-enzyme showed a wide pH stability range of pH 2-11 and tolerance at 50°C for 20 min.Pectic enzymes from plant and microbial sources have been studied intensively in the past and they are broadly classified into pectinesterase (PE), which saponifies the esterified portions of the pectin chain, and depolymerases which are responsible for cleaving the chain (17). Among the depolymerases, the major one in terms of hydrolytic function is the endo-polygalacturonase (PG, EC 3.2.1.15). Several review articles that covered the Pectic enzymes secreted by various plants and microorganisms, generally reported that plants contain high PE activities. On the other hand, PG is said to be the major pectic enzymes of molds and yeast while bacteria possess higher activities for PE and the lyases (2,4,18, 23, 25) . But molds seemingly prove to be more useful because of higher pectic enzyme production and optimum activity at a lower pH range suited for the most common industrial use, i.e. juice clarification (3). Hence, a lot of efforts have been devoted to the study of the pectic enzymes by molds. In the case of researches on the pectolytic activity of Rhizopus spp., most are related to fruit and vegetable degradation (1). A recent study used citrus waste as substrate for PG production by Rhizopus oryzae (7). But in general, it seems that less attention is being paid regarding the utilization of waste substrate material for the culture and screening of Rhizopus strains for PG production.In this study, most of the Rhizopus strains used were isolated from `ragi,' a rice wine inoculum, and some fermented foods, such as `tempeh' that are native to

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“…However, studies on the enzymes production in yeast was quite limited. Some studies have been conducted from yeast of Kluyveromyces fragilis , from Galactomyces reesei , from Trichosporon penicillatum , from Saccharomyces fragilis (Lim et al, 1980). Isolated yeasts are likely to produce pectinolytic enzymes (Kaur et al, 2004;Leizerson and Shimoni, 2005), as they are able to utilize pectin as a sole carbon source.…”

Section: Introductionmentioning

confidence: 99%