Pectin lyase of Penicillium paxilli

Abstract

A ?enicillium paxilli strain afforded a 4epolymerase specific for highmethoxyl pectin: pectin lyase EC 4.2.2.10, capable of macerating potato and cucumber tissues.

Kinetic behaviour and thermal inactivation of pectinlyase used in food processing

“…The lack of standardization in the enzyme assays (type of substrate, temperature and pH conditions) used by different authors, made it difficult to compare the K m values of PLs from different sources. Nevertheless, these apparent values are within the range reported for PLs; Cytolase PCL5 Ò (Gist Brocades; 1.29 mg mL )1 ) (Vaillant et al, 2000); Aspergillus niger CH4 (2.28 mg mL )1 ) (Acun˜a-Argu¨elles et al, 1995); Penicillium paxilli (2.5 mg mL )1 ) (Szajer & Szajer, 1982) and Pichia pinus (3.3 mg mL )1 ) (Moharib et al, 2000). Other authors have described PLs with lower affinity for the substrate, i.e.…”

“…, 2000); Aspergillus niger CH4 (2.28 mg mL −1 ) (Acuña‐Argüelles et al. , 1995); Penicillium paxilli (2.5 mg mL −1 ) (Szajer & Szajer, 1982) and Pichia pinus (3.3 mg mL −1 ) (Moharib et al. , 2000).…”

Purification and some properties of the pectin lyase from Penicillium italicum

“…in the case of J~enieillium spp., pectin iyase has been detected in crude preparations of Penicillium citrinurn, P. italicum and Penicillium paxilli [17][18][19] The purification scheme here reported describes, for the first time, the application of a hydrophobic interaction chromatography to obtain a homogeneous pectin lyase preparation from a fungus source, This preparation showed a specific activity of 3934 U/rag protein at 40"C (pH 6,0) with citrus pectin (DE 70%0) which corresponded to 7650 U/rag protein at the same temperature (pl-[ 9.0) with citrus pectin (DE 86%), The former value is similar to that reported in Dothidea ribesia (3790 U/rag protein) [i2] but much higher than those shown by enriched pectin lyase preparations of Penicillium spp. (22-48 U/rag protein) [20,221 and other fungi (20-355 U/rag protein) [8,10,23,25].…”

“…Mono P, Phellyl-Superos¢ and Superose 12 columns, Pl`t:tstGel [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25]. SDS buffer strips, Pol:,,buffcr 96, ampholytes (8-10.5).…”

A cold‐active pectin lyase from the psychrophilic and basidiomycetous yeast Cystofilobasidium capitatum strain PPY‐1

“…The PNL from strain PPY‐1 exhibited sufficient activity below 20 °C (approx. half the activity at 20 °C compared with that at optimal temperature, like the PNL from Penicillium paxilli [22]) (Figure 2), although specific activity of the enzyme was lower than those of PNLs from Penicillium italicum and Pseudomonas fluorescens at 40 °C (3934 and 3436 units/mg respectively) [23,24]. Moreover, the purified PNL was able to reduce the viscosity of a pectin solution at 5 °C, and after 1.5 h, the viscosity of the pectin solution had become the same as that of water (Figure 4).…”