8. POLYSACCHARIDASES
375
amyloliquefaciens, a variety of B. subtilis, secretes a small amount of
amylase when shaken aerobically in the presence of phosphate (155).
The effects of carbon sources and base analogs of nucleic acid on the
amylase formation have been studied and have been found to be of
great importance (156). Fseudomonas saccharophila also emits an aamylase into the culture medium (157).
d. Mold a-Amylases. A great number of molds are known to produce
α-amylase. Rhizopus japonicus contains α-amylase, but there is probably also some ß-amylase present (158). The best known of all amylases
of mold occurs in Aspergillus oryzae. This microorganism has been
known in Japan for more than 2000 years under the name koji (159) and
has been used in the manufacture of alcoholic beverages called sake.
Details on the preparation of koji and a full description of its amylase
have been given by Atkinson (160, 161). Later, Takamine (162) investigated this enzyme further, compared its action to that of malt
amylases, and finally brought on the market a commercial preparation
of the enzyme, called Taka-amylase, for use in the textile industry (163).
The shortage of barley malt in the United States during World War II
led to extensive research through which the commercial production of
mold bran on a large scale became possible (164). This mold bran was
used in the manufacture of industrial alcohol from grains (165).
The purification and crystallization of α-amylase from A. oryzae has
been achieved in several laboratories (166-169), and the properties and
action patterns of the pure (36, 170, 171), as well as of crude preparations have been described (172-176).
Certain strains of A. niger have also been reported to produce starchhydrolyzing enzymes in substantial amounts (177).
The amylolytic system in the black-fco/ϊ molds of the A. oryzae and
of similar species such as A. awamori, A. usamii, etc., has been extensively studied by the Japanese workers (178-180).
e. Yeast Amylases. In a thorough investigation of 64 different yeast
species, Smits Van Waesberghe (181) came to the conclusion that the
starch-degrading yeast enzymes are phosphorylases rather than amylases. These are supplemented by various glucosidases.
The enhancement of amylase action by yeasts has been known for a
long time and has been explained by Schwimmer (182) and by Pan
et al. (183) on the basis of the removal by yeast of maltose formed
during amylatic digestion. That maltose inhibits the action of amylase
is well known (25).
A report of the presence of extracellular amylase in Endomycopsis
fibuliger (184) should be considered with caution. The action observed
may well be due to phosphorylase.
375
amyloliquefaciens, a variety of B. subtilis, secretes a small amount of
amylase when shaken aerobically in the presence of phosphate (155).
The effects of carbon sources and base analogs of nucleic acid on the
amylase formation have been studied and have been found to be of
great importance (156). Fseudomonas saccharophila also emits an aamylase into the culture medium (157).
d. Mold a-Amylases. A great number of molds are known to produce
α-amylase. Rhizopus japonicus contains α-amylase, but there is probably also some ß-amylase present (158). The best known of all amylases
of mold occurs in Aspergillus oryzae. This microorganism has been
known in Japan for more than 2000 years under the name koji (159) and
has been used in the manufacture of alcoholic beverages called sake.
Details on the preparation of koji and a full description of its amylase
have been given by Atkinson (160, 161). Later, Takamine (162) investigated this enzyme further, compared its action to that of malt
amylases, and finally brought on the market a commercial preparation
of the enzyme, called Taka-amylase, for use in the textile industry (163).
The shortage of barley malt in the United States during World War II
led to extensive research through which the commercial production of
mold bran on a large scale became possible (164). This mold bran was
used in the manufacture of industrial alcohol from grains (165).
The purification and crystallization of α-amylase from A. oryzae has
been achieved in several laboratories (166-169), and the properties and
action patterns of the pure (36, 170, 171), as well as of crude preparations have been described (172-176).
Certain strains of A. niger have also been reported to produce starchhydrolyzing enzymes in substantial amounts (177).
The amylolytic system in the black-fco/ϊ molds of the A. oryzae and
of similar species such as A. awamori, A. usamii, etc., has been extensively studied by the Japanese workers (178-180).
e. Yeast Amylases. In a thorough investigation of 64 different yeast
species, Smits Van Waesberghe (181) came to the conclusion that the
starch-degrading yeast enzymes are phosphorylases rather than amylases. These are supplemented by various glucosidases.
The enhancement of amylase action by yeasts has been known for a
long time and has been explained by Schwimmer (182) and by Pan
et al. (183) on the basis of the removal by yeast of maltose formed
during amylatic digestion. That maltose inhibits the action of amylase
is well known (25).
A report of the presence of extracellular amylase in Endomycopsis
fibuliger (184) should be considered with caution. The action observed
may well be due to phosphorylase.