Pectic Enzymes of Pigmented Strains of Clostridium

Abstract

59The pectic enzymes of six strains of pigmented, pectolytic clostridia isolated from potatoes were examined and compared with those strains of Clostridium felsineum and Clostridium aurantibutyricum using cup-plate assays. The organisms could be divided into two groups. Group I consisted of the potato isolates and the strain of C. aurantibutyricum; these formed pectic lyase enzymes and pectinesterase but no pectic hydrolase. Group 2 consisted of eight strains of C. felsineum (and one culture labelled Clostridium roseum) ; these formed pectic lyase and pectic hydrolase but no detectable pectinesterase. Viscometric studies and analyses of degradation products of pectate formed by enzymes of four representative strains from group I and two strains from group 2 showed that all these clostridia formed endopectate lyase enzymes; studies of one enzyme preparation showed that the pH optimum was about 9-5. In addition, the group 2 organisms formed endopolygalacturonase and probably also exopolygalacturonase. I N T R O D U C T I O NDuring studies of bacterial soft rot of potatoes, pectolytic clostridia have regularly been detected in rotting tissue (Lund, 1972;Lund & Kelman, 1977). Although the primary cause of this spoilage is usually Erwinia carotovora, some of these pectolytic clostridia cause rapid maceration of potato tissue and undoubtedly enhance the effect of E. carotovora (Rudd-Jones & Dowson, 1950). The pectolytic clostridia associated with rotting potatoes probably belong to several species (Lund, 1972) and include a group of bacteria which form a pink pigment. Apart from the colour of the pigment, these clostridia have many properties in common with Clostridium felsineum (B. M. Lund & G. M. Wyatt, unpublished). The purpose of this work was to determine whether pigmented clostridia isolated from potatoes differed from C. felsineum or another pigmented clostridium, Clostridium aurantibutyricum, in the type of pectic enzymes formed.Of the bacterial enzymes which depolymerize pectic substances, the most widely reported are those with lyase activity, although bacteria from several genera form enzymes which hydrolyse pectate (see Rombouts, 1972;Rombouts & Pilnik, 1972;Fogarty & Ward, 1974

Pectinolytic activity ofClostridium thermocellum: Its use for anaerobic fermentation of sugar beet pulp

“…The low activity of this enzyme might be responsible for the failure of our measurement assays. Despite the results of Lund and Brocklehurst (1978), who did not find any pigmentated Clostridium able to express the three types of pectinase activity at the same time, this strain seems to have this ability. Although the increase in galacturonase activity is associated with the growth phase and stops with it, the pectin lyase activity production begins later and goes on after the growth has stopped.…”

A Polygalacturonate Lyase Produced by Lachnospira multiparus Isolated from the Bovine Rumen

“…DISCUSSION The predominant pectinolytic enzyme of L. multiparus is a polygalacturonate lyase, similar to the lyase of Bacteroides ruminicola described earlier (Wojciechowicz, 1971). Its optimum pH of 8.0, Ca2+ requirement and preference for polygalacturonate as substrate resemble those of partially purified polygalacturonate Iyases of certain other bacteria: Bacillus polymyxa (Nagel & Vaughn,196 l), Bacillus subtilis, Flavobacterium pectinovorum (Ward & Fogarty, 1974), Clostridium felsineum (Kapitonova et al, 1973;Lund & Brocklehurst, 1978), Xanthomonas campestris , Arthrobacter (Rombouts, 1972) and Erwinia aroideae (Kamimiya et a/., 1977).…”

“…There are many reports on the production by bacteria of a mixture of polygalacturonate lyase and polygalacturonase (Hasegawa & Nagel, 1967;Kapitonova et al, 1972;Hatanaka & Ozawa, 1971 ;Lund & Brocklehurst, 1978;Nasuno & Starr, 1966a, b ;Preiss & Ashwell, 1963). It also seems to be a common feature of the pectinolytic rumen bacteria, having been observed in some strains of Bacteroides ruminicola (M. Wojciechowicz, unpublished observations), in the large rumen treponemes (Wojciechowicz & Ziolecki, 1979) and now in L. rnultiparus.…”

Characterization of pectinolytic enzymes of Clostridium thermosulfurogenes

“…Mesophilic Clostridium species vary in regard to the type of pectin depolymerizing enzymes produced. In this regard, C. thermosulfurogenes utilizes the same enzymes as reported in C. felsineum and C. roseum [15]; however, it does not form polygalacturonate lyase common to C. multifermentans [ 14]. The cellular distribution of pectinase activity in C. thermosulfurogenes is similar to that of cellulase activity in C. thermoeellum [16].…”