Two Forms of Glucoamylase from Mucor rouxianus

Yamasaki, Yudai; Tsuboi, Akira; Suzuki, Yukio

doi:10.1271/bbb1961.38.543

Cited by 27 publications

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“…The M of purified amylase AI‐2 was similar to that of tasar silkworm, oyster and human saliva α‐amylases (58, 60, and 55.2 kDa, respectively), 18,31 , 32 tilapia intestine β‐amylase (56.4), 5 small abalone amylase II‐1 (55.7 kDa), 33 and Rhizopus sp. γ‐amylase (58.6 kDa), 34 while that of amylase AI‐1 was similar to those α‐amylases from hog pancreas and Alteromonas haloplanctis (45 and 49.3 kDa, respectively) 32,35 and Clostridium thermosulfurogenes β‐amylases (51 kDa), 4 Coniophora cerebella (48 kDa) and Smucor rouxianus II γ‐amylase (49 kDa) 26,36 . Amylase AII was larger than those of amylases from animal as described above and similar to B. stearothermophilus α‐amylase (115 kDa)., 9 …”

Section: Resultssupporting

confidence: 56%

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Purification and characterization of three amylases from viscera of hard clam Meretrix lusoria

et al. 2004

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Three amylases were purified to electrophoretic homogeneity from viscera of hard clam Meretrix lusoria by ammonium sulfate fractionation, Sepharose 6B, DEAE-Sephadex A-50, Sephadex G-200 and PBE 94 chromatographies. The purified amylases had molecular masses of 49.6, 58.7 and 100 kDa and were designated AI-1, AI-2 and AII, respectively. Both AI-1 and AI-2 could digest amylose into glucose and maltose, while AII could digest amylose and pullulan into glucose. The optimal pH and temperatures for AI-1, AI-2 and AII were 7.0, 7.5 and 7.5, and 40, 50 and 50 ∞ C, respectively. According to the substrate specificity, the purified AI-1 and AI-2 were considered to be multifunctional exo-and endo-types of a -amylase-like enzymes, while AII was exo-type g -amylase-like enzyme. They were Ca 2 + -independent enzymes.

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Section: Resultssupporting

confidence: 56%

“…respectively) 32,35 and Clostridium thermosulfurogenes b -amylases (51 kDa), 4 Coniophora cerebella (48 kDa) and Smucor rouxianus II g -amylase (49 kDa). 26,36 Amylase AII was larger than those of amylases from animal as described above and similar to B. stearothermophilus a -amylase (115 kDa)., 9…”

Section: Homogeneity and Molecular Massmentioning

confidence: 62%

Purification and characterization of three amylases from viscera of hard clam Meretrix lusoria

et al. 2004

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“…To avoid this difficulty, substrates like pullulan (every third bond 1,6-glycosidic) are often used to estimate 1,6-hydrolysing activity. Many fungal glucoamylases have been reported to exist in multiple forms (Lineback & Bauman, 1970;Tsuboi et al, 1974;Yamasaki et al, 1977;Takahashi et al, 1978Takahashi et al, , 1981. In order to clone the appropriate gene it is essential to know if these multiple forms are coded by different genes, or if they are results of post-translational Abbreuiations : FMOC, 9-fluorenylmethoxycarbnyl ; OPA, ophthalaldehyde; PTH, phenylthiohydantoin. modification and/or different mRN A splicing (Hayashida et al, 1988 ;Ono et al, 1988).…”

Section: Introductionmentioning

confidence: 99%

Comparison of two glucoamylases from Hormoconis resinae

Fagerstrom¹,

Vainio²,

Suoranta³

et al. 1990

Journal of General Microbiology

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Two extracellular glucoamylases (EC 3.2.1.3), glucoamylase P and glucoamylase S, were purified to homogeneity from the culture medium of Hormoconis resinae (ATCC 20495; formerly Cl&sprium resinae) by a new method. Their apparent molecular masses (71 kDa glucoamylase P; 78 kDa glucoamylase S) and catalytic properties agreed well with those previously reported in the literature. Heat inactivation studies suggested that the high debranching (1,6-glycosidic) activity of glucoamylase P preparations (measured with pullulan) may reside in the same protein molecule as its l,&glycosidic activity (measured with soluble starch). Although glucoamylase S had virtually no debranching activity, it cross-reacted with polyclonal antibodies raised against glucoamylase P, and the two enzymes had very similar amino acid compositions. However, peptide mapping and amino-terminal sequencing studies of the peptides showed that the two enzymes have different sequences and must be encoded by different genes. IntroductionEnzymes that degrade poly-and oligosaccharides are commercially important for the food and fermentation industries. Glucoamylases (1,4-glucan glucohydrolases ; EC 3.2.1 .3) release glucose units sequentially from the nonreducing end of polymeric carbohydrates. The ability of glucoamylases to hydrolyse 1,6-glycosidic bonds is called debranching activity and is of great importance in industrial processes requiring complete degradation of starch to glucose.Glucoamylases are produced by a wide variety of micro-organisms (Manjunath et al., 1983). Most of the known glucoamylases have very low activity towards 1,6-glycosidic bonds. The analytical measurement of debranching activity is not straightforward, since the activity of glucoamylases on substrates containing only 1,6-glycosidic bonds is usually quite low. To avoid this difficulty, substrates like pullulan (every third bond 1,6-glycosidic) are often used to estimate 1,6-hydrolysing activity. Many fungal glucoamylases have been reported to exist in multiple forms (Lineback & Bauman, 1970;Tsuboi et al., 1974;Yamasaki et al., 1977;Takahashi et al., 1978Takahashi et al., , 1981. In order to clone the appropriate gene it is essential to know if these multiple forms are coded by different genes, or if they are results of post-translational al. (1984) these two forms of the enzyme are products of two differently spliced mRNA molecules coded by the same gene, whereas Svensson et al. (1986) have pointed out that proteolytic modification also affects the multiplicity of this enzyme.The fungus Hormoconis resinae (ATCC 20495; formerly Cladosporium resinae) has been reported to produce two forms of glucoamylase which exhibit different substrate specificities and have different molecular masses and PI values (McCleary & Anderson, 1980). The smaller glucoamylase P has a very high debranching activity, while the larger glucoamylase S has virtually no debranching activity. In the present work, we examined whether the 1,4-and 1,6-glycosidic activities of glucoamylase P are both functions...

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“…Glucoamylases from Aspergillus kawachii,lI Rhizopus delemar,2) Asp. niger, 2) and Mucor rouxianus 3 ) have so far been isolated in crystalline form. No attempt, however, has yet been made to isolate glucoamylase from Penicillia.…”

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confidence: 99%

Purification and Properties of Two Forms of Glucoamylase fromPenicillium oxalicum

Yamasaki

Suzuki

Ozawa

1977

Agricultural and Biological Chemistry

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Penicillium oxalicum produced two forms (isoenzymes) of glucoamylase which could be separated from each other by gel electrofocusing, and they were designated as glucoamylase I and glucoamylase II. Glucoamylases I and II were homogeneous on polyacrylamide gel electrophoresis, gel electrofocusing and ultracentrifugation, respectively. The sedimentation constant (sgo,w) and molecular weight of glucoamylase I were 4.42 Sand 84,000, and those of glucoamylase II were 4.53 Sand 86,000, respectively. Certain properties of these enzymes were also investigated.

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Two Forms of Glucoamylase from Mucor rouxianus

Cited by 27 publications

References 0 publications

Purification and characterization of three amylases from viscera of hard clam Meretrix lusoria

Purification and characterization of three amylases from viscera of hard clam Meretrix lusoria

Comparison of two glucoamylases from Hormoconis resinae

Purification and Properties of Two Forms of Glucoamylase fromPenicillium oxalicum

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