Comparison of Enzymatic Properties of Microbial Transglutaminase from Streptomyces sp.

Umezawa, Yukiko; Ohtsuka, Tomoko; Yokoyama, Keiichi; Nio, Noriki

doi:10.3136/fstr.8.113

Cited by 16 publications

(11 citation statements)

References 23 publications

(21 reference statements)

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“…The sequences of the S. lydicus, S. platensis, and S. cinnamoneus TGases corresponding to these S. mobaraensis segments are highly conserved, although there are a few substitutions such as a Ser replacement by Lys on the loop between the β4 and β5 strands in S. platensis. Thus, the main characteristics of the Streptomyces TGases would be expected to be similar, as observed by this and other studies (8).…”

Section: Streptomyces Tgasessupporting

confidence: 83%

“…mobaraensis, S. lydicus, S. platensis, and S. cinnamoneus TGases have high homology (~80%) in terms of protein sequence (5,8). The suggested catalytic amino acid residues, a Cys, an Asp, and a His, for S. mobaraensis TGase are conserved among the enzymes (Fig.…”

Section: Streptomyces Tgasesmentioning

confidence: 96%

“…The purified TGases were found to be free of detectable protease side activity. Preparation of S. mobaraensis and S. lydicus TGase showed the correct N-terminal sequences (8). Because of their abundance, only S. mobaraensis, S. lydicus, S. platensis, and S. nigrescens TGases were characterized in terms of pH and temperature profiles, and only S. lydicus TGase was characterized for its substrate specificity.…”

Section: Purificationmentioning

confidence: 99%

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Substrate specificity of Streptomyces transglutaminases

Langston

Blinkovsky

Byun

et al. 2007

Appl Biochem Biotechnol

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Transglutaminase (TGase) is a multifunctional enzyme vital for many physiologic processes, such as cell differentiation, tissue regeneration, and plant pathogenicity. The acyl transfer function of the enzyme can activate primary amines and, consequently, attach them onto a peptidyl glutamine, a reaction important for various in vivo and in vitro protein crosslinking and modification processes. To understand better the structure-function relationship of the enzyme and to develop it further as an industrial biocatalyst, we studied TGase secreted by several Streptomyces species and Phytophthora cactorum. We purified the enzyme from S. lydicus, S. platensis, S. nigrescens, S. cinnamoneus, and S. hachijoensis. The pH and temperature profiles of S. lydicus, S. platensis, and S. nigrescens TGases were determined. The specificity of S. lydicus TGase toward its acyl-accepting amine substrates was characterized. Correlation of the electronic and steric features of the substrates with their reactivity supported the mechanism previously proposed for Streptomyces mobaraensis TGase.

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Section: Streptomyces Tgasessupporting

confidence: 83%

Section: Streptomyces Tgasesmentioning

confidence: 96%

Section: Purificationmentioning

confidence: 99%

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Substrate specificity of Streptomyces transglutaminases

Langston

Blinkovsky

Byun

et al. 2007

Appl Biochem Biotechnol

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“…MTGase from Streptomyces libani showed slightly lower optimum reaction temperature and thermal stability than from Streptomyces mobaraensis (Umezawa et al, 2002).…”

Section: Introductionmentioning

confidence: 89%

Properties and Application of Microbial Transglutaminase Produced From a Newly Isolated Strain of Streptomyces Sp.

Eshra.¹,

Iraki²,

Bakr.³

2017

IJAR

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The aim of the present work is to study some physical properties of microbial transglutaminase (MTGase) produced from a newly isolated strain of Streptomyces sp. Also, its application in producing Shamy bread from a mixture of wheat and corn flours was investigated. The results revealed that the enzyme exhibited optimum activity at 45 ᴼ C; it retained about 80% of the initial activity after incubation for one hour at this temperature. The optimum activity was at pH 6.5 and was stable at this pH for one hour. The cross-linking effect of the enzyme was tested through cross-linking of wheat dough prepared for Shamy bread. The results indicated that the enzyme have a cross-linking effects towards the free amino and thiol groups of wheat dough. The free amino groups of the wheat dough were 0.538 µM/ mg flour without adding the enzyme. It decreased to 0.378 µM/ mg flour when treated with the enzyme; the percent of reduction was 29.74. Mixing corn flour with wheat flour decreased the free amino groups of the resulted dough. It decreased to 0.248 µM/ mg flour in the sample treated with the enzyme and containing 30% corn flour with percentage of reduction 34.39. In general, increasing the percentage of corn flour in the blends treated with MTGase decreases the free thiol groups. The free thiol groups of the wheat dough (without enzyme) were 11.222µM/ g flour, it decreased to 10.342 µM/ g flour when treated with the enzyme, with percentage of reduction 7.849 %. When the levels of corn flour increased to 30% the free thiol groups decreased and the percent of the reduction increased to 8.575. It was noted that the prepared Shamy bread from dough containing 70% wheat flour and 30% corn flour and treated with the enzyme have a higher volume with pronounced improvement in the general appearance and quality than that without the enzyme.

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“…Alpha-amylases have been also produced with S. aureofaciens, S. rimosus, S. gulbargensis, S. hygroscopicus, S. preacox (12, 34, 40). The study of transglutaminase production by Streptomyces higroscopus, Streptomyces mobaraensis, S. libani, Streptoverticillium mobaraense is more recent (11, 37, 24, 30, 8). …”

Section: Introductionmentioning

confidence: 99%

Partial characterization of cold active amylases and proteases of Streptomyces sp. from Antarctica

Cotârleț¹,

Negoiţă²,

Bahrim³

et al. 2011

Braz. J. Microbiol.

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The aim of this study was to isolate novel enzyme-producing bacteria from vegetation samples from East Antarctica and also to characterize them genetically and biochemically in order to establish their phylogeny. The ability to grow at low temperature and to produce amylases and proteases cold-active was also tested. The results of the 16S rRNA gene sequence analysis showed that the 4 Alga rRNA was 100% identical to the sequences of Streptomyces sp. rRNA from Norway and from the Solomon Islands. The Streptomyces grew well in submerged system at 20°C, cells multiplication up to stationary phase being drastically increased after 120 h of submerged cultivation. The beta-amylase production reached a maximum peak after seven days, while alpha-amylase and proteases were performing biosynthesis after nine days of submerged cultivation at 20°C. Newly Streptomyces were able to produce amylase and proteases in a cold environment. The ability to adapt to low temperature of these enzymes could make them valuable ingredients for detergents, the food industry and bioremediation processes which require low temperatures.

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Comparison of Enzymatic Properties of Microbial Transglutaminase from Streptomyces sp.

Cited by 16 publications

References 23 publications

Substrate specificity of Streptomyces transglutaminases

Substrate specificity of Streptomyces transglutaminases

Properties and Application of Microbial Transglutaminase Produced From a Newly Isolated Strain of Streptomyces Sp.

Partial characterization of cold active amylases and proteases of Streptomyces sp. from Antarctica

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