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Draft genome sequence of a thermostable, alkaliphilic α-amylase and protease producing .

3 Biotech

Prajapati VS, Ray S, Narayan J, Joshi CC, Patel KC, Trivedi UB, Patel RM.
PMID: 29071169
3 Biotech. 2017 Dec;7(6):372. doi: 10.1007/s13205-017-1005-1. Epub 2017 Oct 13.

No abstract available.

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Prajapati VS, Ray S, Narayan J, et al. Draft genome sequence of a thermostable, alkaliphilic α-amylase and protease producing . 3 Biotech. 2017;7(6):372doi: 10.1007/s13205-017-1005-1.
Prajapati, V. S., Ray, S., Narayan, J., Joshi, C. C., Patel, K. C., Trivedi, U. B., & Patel, R. M. (2017). Draft genome sequence of a thermostable, alkaliphilic α-amylase and protease producing . 3 Biotech, 7(6), 372. https://doi.org/10.1007/s13205-017-1005-1
Prajapati, Vimalkumar S, et al. "Draft genome sequence of a thermostable, alkaliphilic α-amylase and protease producing ." 3 Biotech vol. 7,6 (2017): 372. doi: https://doi.org/10.1007/s13205-017-1005-1
Prajapati VS, Ray S, Narayan J, Joshi CC, Patel KC, Trivedi UB, Patel RM. Draft genome sequence of a thermostable, alkaliphilic α-amylase and protease producing . 3 Biotech. 2017 Dec;7(6):372. doi: 10.1007/s13205-017-1005-1. Epub 2017 Oct 13. PMID: 29071169; PMCID: PMC5640519.
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The Effect of Oral Processing on the Viscosity of Thickened Drinks for Patients With Dysphagia.

Annals of rehabilitation medicine

Vallons KJ, Oudhuis LA, Helmens HJ, Kistemaker C.
PMID: 26605175
Ann Rehabil Med. 2015 Oct;39(5):772-7. doi: 10.5535/arm.2015.39.5.772. Epub 2015 Oct 26.

OBJECTIVE: To determine whether a gum-containing thickener maintains its viscosity better during oral processing than a completely starch-based thickener.METHODS: Thirty-five healthy volunteers participated in a double-blind, cross-over study. Artificial tap water was thickened to honey-like consistency (effective viscosity of...

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Vallons KJ, Oudhuis LA, Helmens HJ, et al. The Effect of Oral Processing on the Viscosity of Thickened Drinks for Patients With Dysphagia. Ann Rehabil Med. 2015;39(5):772-7doi: 10.5535/arm.2015.39.5.772.
Vallons, K. J., Oudhuis, L. A., Helmens, H. J., & Kistemaker, C. (2015). The Effect of Oral Processing on the Viscosity of Thickened Drinks for Patients With Dysphagia. Annals of rehabilitation medicine, 39(5), 772-7. https://doi.org/10.5535/arm.2015.39.5.772
Vallons, Katleen J R, et al. "The Effect of Oral Processing on the Viscosity of Thickened Drinks for Patients With Dysphagia." Annals of rehabilitation medicine vol. 39,5 (2015): 772-7. doi: https://doi.org/10.5535/arm.2015.39.5.772
Vallons KJ, Oudhuis LA, Helmens HJ, Kistemaker C. The Effect of Oral Processing on the Viscosity of Thickened Drinks for Patients With Dysphagia. Ann Rehabil Med. 2015 Oct;39(5):772-7. doi: 10.5535/arm.2015.39.5.772. Epub 2015 Oct 26. PMID: 26605175; PMCID: PMC4654084.
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Draft Genome Sequence of Talaromyces cellulolyticus Strain Y-94, a Source of Lignocellulosic Biomass-Degrading Enzymes.

Genome announcements

Fujii T, Koike H, Sawayama S, Yano S, Inoue H.
PMID: 25720677
Genome Announc. 2015 Feb 26;3(1). doi: 10.1128/genomeA.00014-15.

Talaromyces cellulolyticus (formerly Acremonium cellulolyticus) is a promising fungus for cellulase production. Here, we present the draft genome sequence of T. cellulolyticus strain Y-94. The genome is 36.4 Mbp long and contains genes for several enzymes involved in the...

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Fujii T, Koike H, Sawayama S, et al. Draft Genome Sequence of Talaromyces cellulolyticus Strain Y-94, a Source of Lignocellulosic Biomass-Degrading Enzymes. Genome Announc. 2015;3(1)doi: 10.1128/genomeA.00014-15.
Fujii, T., Koike, H., Sawayama, S., Yano, S., & Inoue, H. (2015). Draft Genome Sequence of Talaromyces cellulolyticus Strain Y-94, a Source of Lignocellulosic Biomass-Degrading Enzymes. Genome announcements, 3(1), . https://doi.org/10.1128/genomeA.00014-15
Fujii, Tatsuya, et al. "Draft Genome Sequence of Talaromyces cellulolyticus Strain Y-94, a Source of Lignocellulosic Biomass-Degrading Enzymes." Genome announcements vol. 3,1 (2015). doi: https://doi.org/10.1128/genomeA.00014-15
Fujii T, Koike H, Sawayama S, Yano S, Inoue H. Draft Genome Sequence of Talaromyces cellulolyticus Strain Y-94, a Source of Lignocellulosic Biomass-Degrading Enzymes. Genome Announc. 2015 Feb 26;3(1). doi: 10.1128/genomeA.00014-15. PMID: 25720677; PMCID: PMC4342418.
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Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications.

Frontiers in microbiology

Mehta D, Satyanarayana T.
PMID: 27516755
Front Microbiol. 2016 Jul 28;7:1129. doi: 10.3389/fmicb.2016.01129. eCollection 2016.

Industrial enzyme market has been projected to reach US$ 6.2 billion by 2020. Major reasons for continuous rise in the global sales of microbial enzymes are because of increase in the demand for consumer goods and biofuels. Among major...

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Mehta D, Satyanarayana T. Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications. Front Microbiol. 2016;7:1129doi: 10.3389/fmicb.2016.01129.
Mehta, D., & Satyanarayana, T. (2016). Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications. Frontiers in microbiology, 71129. https://doi.org/10.3389/fmicb.2016.01129
Mehta, Deepika, and Satyanarayana, Tulasi. "Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications." Frontiers in microbiology vol. 7 (2016): 1129. doi: https://doi.org/10.3389/fmicb.2016.01129
Mehta D, Satyanarayana T. Bacterial and Archaeal α-Amylases: Diversity and Amelioration of the Desirable Characteristics for Industrial Applications. Front Microbiol. 2016 Jul 28;7:1129. doi: 10.3389/fmicb.2016.01129. eCollection 2016. PMID: 27516755; PMCID: PMC4963412.
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Penicillium echinulatum secretome analysis reveals the fungi potential for degradation of lignocellulosic biomass.

Biotechnology for biofuels

Schneider WDH, Gonçalves TA, Uchima CA, Couger MB, Prade R, Squina FM, Dillon AJP, Camassola M.
PMID: 26989443
Biotechnol Biofuels. 2016 Mar 17;9:66. doi: 10.1186/s13068-016-0476-3. eCollection 2016.

BACKGROUND: The enzymatic degradation of lignocellulosic materials by fungal enzyme systems has been extensively studied due to its effectiveness in the liberation of fermentable sugars for bioethanol production. Recently, variants of the fungus Penicillium echinulatum have been described as...

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Schneider WDH, Gonçalves TA, Uchima CA, et al. Penicillium echinulatum secretome analysis reveals the fungi potential for degradation of lignocellulosic biomass. Biotechnol Biofuels. 2016;9:66doi: 10.1186/s13068-016-0476-3.
Schneider, W. D. H., Gonçalves, T. A., Uchima, C. A., Couger, M. B., Prade, R., Squina, F. M., Dillon, A. J. P., & Camassola, M. (2016). Penicillium echinulatum secretome analysis reveals the fungi potential for degradation of lignocellulosic biomass. Biotechnology for biofuels, 966. https://doi.org/10.1186/s13068-016-0476-3
Schneider, Willian Daniel Hahn, et al. "Penicillium echinulatum secretome analysis reveals the fungi potential for degradation of lignocellulosic biomass." Biotechnology for biofuels vol. 9 (2016): 66. doi: https://doi.org/10.1186/s13068-016-0476-3
Schneider WDH, Gonçalves TA, Uchima CA, Couger MB, Prade R, Squina FM, Dillon AJP, Camassola M. Penicillium echinulatum secretome analysis reveals the fungi potential for degradation of lignocellulosic biomass. Biotechnol Biofuels. 2016 Mar 17;9:66. doi: 10.1186/s13068-016-0476-3. eCollection 2016. PMID: 26989443; PMCID: PMC4794826.
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Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings.

Physiology and molecular biology of plants : an international journal of functional plant biology

Devi R, Munjral N, Gupta AK, Kaur N.
PMID: 24381440
Physiol Mol Biol Plants. 2013 Jan;19(1):81-9. doi: 10.1007/s12298-012-0143-5.

The present study investigated the effect of exogenous lead (Pb) on seedling growth, carbohydrate composition and vital enzymes of sucrose metabolism, starch degradation, pentose phosphate pathway and glycolysis in pea seedlings. With 0.5 mM Pb, reduction of about 50...

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Devi R, Munjral N, Gupta AK, et al. Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings. Physiol Mol Biol Plants. 2013;19(1):81-9doi: 10.1007/s12298-012-0143-5.
Devi, R., Munjral, N., Gupta, A. K., & Kaur, N. (2013). Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings. Physiology and molecular biology of plants : an international journal of functional plant biology, 19(1), 81-9. https://doi.org/10.1007/s12298-012-0143-5
Devi, Rachana, et al. "Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings." Physiology and molecular biology of plants : an international journal of functional plant biology vol. 19,1 (2013): 81-9. doi: https://doi.org/10.1007/s12298-012-0143-5
Devi R, Munjral N, Gupta AK, Kaur N. Effect of exogenous lead on growth and carbon metabolism of pea (Pisum sativum L) seedlings. Physiol Mol Biol Plants. 2013 Jan;19(1):81-9. doi: 10.1007/s12298-012-0143-5. PMID: 24381440; PMCID: PMC3550685.
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Chemical modification of lysine residues in Bacillus alpha-amylases: effect on activity and stability.

Enzyme and microbial technology

Khajeh K, Naderi-Manesh H, Ranjbar B, Moosavi-Movahedi A, Nemat-Gorgani M.
PMID: 11267650
Enzyme Microb Technol. 2001 Apr 05;28(6):543-549. doi: 10.1016/s0141-0229(01)00296-4.

Chemical modification of lysine residues in two bacterial alpha-amylases, a mesophilic enzyme from Bacillus amyloliquefaciens (BAA) and a thermophilic enzyme from Bacillus licheniformis (BLA) was carried out using citraconic anhydride. 13 +/- 1 residues in BAA and 10 +/-...

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Khajeh K, Naderi-Manesh H, Ranjbar B, et al. Chemical modification of lysine residues in Bacillus alpha-amylases: effect on activity and stability. Enzyme Microb Technol. 2001;28(6):543-549doi: 10.1016/s0141-0229(01)00296-4.
Khajeh, K., Naderi-Manesh, H., Ranjbar, B., Moosavi-Movahedi, A., & Nemat-Gorgani, M. (2001). Chemical modification of lysine residues in Bacillus alpha-amylases: effect on activity and stability. Enzyme and microbial technology, 28(6), 543-549. https://doi.org/10.1016/s0141-0229(01)00296-4
Khajeh, K, et al. "Chemical modification of lysine residues in Bacillus alpha-amylases: effect on activity and stability." Enzyme and microbial technology vol. 28,6 (2001): 543-549. doi: https://doi.org/10.1016/s0141-0229(01)00296-4
Khajeh K, Naderi-Manesh H, Ranjbar B, Moosavi-Movahedi A, Nemat-Gorgani M. Chemical modification of lysine residues in Bacillus alpha-amylases: effect on activity and stability. Enzyme Microb Technol. 2001 Apr 05;28(6):543-549. doi: 10.1016/s0141-0229(01)00296-4. PMID: 11267650.
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Production of Mold Amylases in Submerged Culture.

Journal of bacteriology

Le Mense EH, Corman J, Van Lanen JM, Langlykke AF.
PMID: 16561342
J Bacteriol. 1947 Aug;54(2):149-59.

No abstract available.

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Le Mense EH, Corman J, Van Lanen JM, et al. Production of Mold Amylases in Submerged Culture. J Bacteriol. 1947;54(2):149-59
Le Mense, E. H., Corman, J., Van Lanen, J. M., & Langlykke, A. F. (1947). Production of Mold Amylases in Submerged Culture. Journal of bacteriology, 54(2), 149-59.
Le Mense, E H, et al. "Production of Mold Amylases in Submerged Culture." Journal of bacteriology vol. 54,2 (1947): 149-59.
Le Mense EH, Corman J, Van Lanen JM, Langlykke AF. Production of Mold Amylases in Submerged Culture. J Bacteriol. 1947 Aug;54(2):149-59. PMID: 16561342; PMCID: PMC526530.
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Preparation and Properties of the Amylases Produced by Bacillus macerans and Bacillus polymyxa.

Journal of bacteriology

Tilden EB, Hudson CS.
PMID: 16560519
J Bacteriol. 1942 Apr;43(4):527-44. doi: 10.1128/jb.43.4.527-544.1942.

No abstract available.

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Tilden EB, Hudson CS. Preparation and Properties of the Amylases Produced by Bacillus macerans and Bacillus polymyxa. J Bacteriol. 1942;43(4):527-44doi: 10.1128/jb.43.4.527-544.1942.
Tilden, E. B., & Hudson, C. S. (1942). Preparation and Properties of the Amylases Produced by Bacillus macerans and Bacillus polymyxa. Journal of bacteriology, 43(4), 527-44. https://doi.org/10.1128/jb.43.4.527-544.1942
Tilden, E B, and Hudson, C S. "Preparation and Properties of the Amylases Produced by Bacillus macerans and Bacillus polymyxa." Journal of bacteriology vol. 43,4 (1942): 527-44. doi: https://doi.org/10.1128/jb.43.4.527-544.1942
Tilden EB, Hudson CS. Preparation and Properties of the Amylases Produced by Bacillus macerans and Bacillus polymyxa. J Bacteriol. 1942 Apr;43(4):527-44. doi: 10.1128/jb.43.4.527-544.1942. PMID: 16560519; PMCID: PMC373623.
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Specific Determination of alpha-Amylase Activity in Crude Plant Extracts Containing beta-Amylase.

Plant physiology

Doehlert DC, Duke SH.
PMID: 16662809
Plant Physiol. 1983 Feb;71(2):229-34. doi: 10.1104/pp.71.2.229.

The specific measurement of alpha-amylase activity in crude plant extracts is difficult because of the presence of beta-amylases which directly interfere with most assay methods. Methods compared in this study include heat treatment at 70 degrees C for 20...

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Doehlert DC, Duke SH. Specific Determination of alpha-Amylase Activity in Crude Plant Extracts Containing beta-Amylase. Plant Physiol. 1983;71(2):229-34doi: 10.1104/pp.71.2.229.
Doehlert, D. C., & Duke, S. H. (1983). Specific Determination of alpha-Amylase Activity in Crude Plant Extracts Containing beta-Amylase. Plant physiology, 71(2), 229-34. https://doi.org/10.1104/pp.71.2.229
Doehlert, D C, and Duke, S H. "Specific Determination of alpha-Amylase Activity in Crude Plant Extracts Containing beta-Amylase." Plant physiology vol. 71,2 (1983): 229-34. doi: https://doi.org/10.1104/pp.71.2.229
Doehlert DC, Duke SH. Specific Determination of alpha-Amylase Activity in Crude Plant Extracts Containing beta-Amylase. Plant Physiol. 1983 Feb;71(2):229-34. doi: 10.1104/pp.71.2.229. PMID: 16662809; PMCID: PMC1066016.
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Tobacco Plants Transformed with the Bean alphaai Gene Express an Inhibitor of Insect alpha-Amylase in Their Seeds.

Plant physiology

Altabella T, Chrispeels MJ.
PMID: 16667540
Plant Physiol. 1990 Jun;93(2):805-10. doi: 10.1104/pp.93.2.805.

Bean (Phaseolus vulgaris L.) seeds contain a putative plant defense protein that inhibits insect and mammalian but not plant alpha-amylases. We recently (J Moreno, MJ Chrispeels [1989] Proc Natl Acad Sci USA 86:7885-7889) presented strong circumstantial evidence that this...

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Altabella T, Chrispeels MJ. Tobacco Plants Transformed with the Bean alphaai Gene Express an Inhibitor of Insect alpha-Amylase in Their Seeds. Plant Physiol. 1990;93(2):805-10doi: 10.1104/pp.93.2.805.
Altabella, T., & Chrispeels, M. J. (1990). Tobacco Plants Transformed with the Bean alphaai Gene Express an Inhibitor of Insect alpha-Amylase in Their Seeds. Plant physiology, 93(2), 805-10. https://doi.org/10.1104/pp.93.2.805
Altabella, T, and Chrispeels, M J. "Tobacco Plants Transformed with the Bean alphaai Gene Express an Inhibitor of Insect alpha-Amylase in Their Seeds." Plant physiology vol. 93,2 (1990): 805-10. doi: https://doi.org/10.1104/pp.93.2.805
Altabella T, Chrispeels MJ. Tobacco Plants Transformed with the Bean alphaai Gene Express an Inhibitor of Insect alpha-Amylase in Their Seeds. Plant Physiol. 1990 Jun;93(2):805-10. doi: 10.1104/pp.93.2.805. PMID: 16667540; PMCID: PMC1062587.
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Degradation of Native Starch Granules by Barley alpha-Glucosidases.

Plant physiology

Sun Z, Henson CA.
PMID: 16667704
Plant Physiol. 1990 Sep;94(1):320-7. doi: 10.1104/pp.94.1.320.

The initial hydrolysis of native (unboiled) starch granules in germinating cereal kernels is considered to be due to alpha-amylases. We report that barley (Hordeum vulgare L.) seed alpha-glucosidases (EC 3.2.1.20) can hydrolyze native starch granules isolated from barley kernels...

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Sun Z, Henson CA. Degradation of Native Starch Granules by Barley alpha-Glucosidases. Plant Physiol. 1990;94(1):320-7doi: 10.1104/pp.94.1.320.
Sun, Z., & Henson, C. A. (1990). Degradation of Native Starch Granules by Barley alpha-Glucosidases. Plant physiology, 94(1), 320-7. https://doi.org/10.1104/pp.94.1.320
Sun, Z, and Henson, C A. "Degradation of Native Starch Granules by Barley alpha-Glucosidases." Plant physiology vol. 94,1 (1990): 320-7. doi: https://doi.org/10.1104/pp.94.1.320
Sun Z, Henson CA. Degradation of Native Starch Granules by Barley alpha-Glucosidases. Plant Physiol. 1990 Sep;94(1):320-7. doi: 10.1104/pp.94.1.320. PMID: 16667704; PMCID: PMC1077227.
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