A Novel Amylolytic Enzyme from Palaeococcus Ferrophilus with Malto-Oligosaccharide Forming Ability Belonging to GH13_20 Subfamily

2021 ◽  
Author(s):  
Hangyan Ji ◽  
Xiaoxiao Li ◽  
Tong Jiang ◽  
Qi Fang ◽  
Yuxiang Bai ◽  
...  
Keyword(s):  
Author(s):  
Е. M. Serba ◽  
М. B. Overchenko ◽  
L. V. Rimareva ◽  
N. I. Ignatova ◽  
А. E. Orekhova ◽  
...  

In the production of alcohol in the preparation of grain raw materials for fermentation, the main role is given to enzyme preparations of amylolytic action, which are key enzymes that catalyze the hydrolysis of starch. Amylolytic enzyme preparations with a different composition of enzymes and their level of activity, a mechanism of biocatalytic effect on starch, and a range of thermal and pH optimum are widely represented on the Russian market. The development of optimal conditions for the preparation of grain wort, the rational selection and dosage of concentrated enzyme preparations, the properties of which correspond to the parameters of the technological process, will ensure the effective preparation of starch for fermentation, and increase the profitability of alcohol production. The aim of this work was to study the influence of enzyme preparations of amylolytic action and the conditions of their use on the efficiency of the process of alcoholic fermentation and the yield of the final product, ethanol. The effect of various dosages of enzyme preparations of glucoamylase action, with a different ratio of the main enzyme glucoamylase and minor enzyme α-amylase, as well as methods for preparing wheat wort on the process of alcoholic fermentation, was studied. It was found that the enzyme preparation, the source of glucoamylase, in which α-amylase was present in a ratio of 15: 1 (in terms of activity level), turned out to be more effective in fermenting prepared wheat wort: its optimal dosage was 8 units. GLS / g starch. The presence of a sufficient amount of α-amylase in this preparation compensated for the dosage of thermostable α-amylase. The alcohol concentration in the mash was 10.2% vol., The alcohol yield was 67.9 cm3 / 100 g of starch. When glucoamylase with a lower ratio of the main and minor enzyme (75: 1) was used at the saccharification stage, an increase in the wort fermentation depth was observed with an increase in the concentration of glucoamylase to 9-10 units of GLS / g and α-amylase to 0.5 units. AC / g. It was also found that an increase in the duration of enzymatic-hydrolytic preparation of the wort had a positive effect on the fermentation process, the alcohol concentration in the mash increased to 10.2 vol.%. It was shown that the introduction of proteases into the wort helps to reduce the viscosity of grain wort, enriching it with assimilable yeast amino acids, which leads to an increase in the yield of alcohol. It has been confirmed that the synergy of the action of enzymes of amylolytic and proteolytic effects on polymers of grain raw materials allows to increase the efficiency of their conversion to ethanol. The conditions of enzymatic-hydrolytic processing of grain raw materials for fermentation are developed. The use of the digestion stage did not significantly affect the fermentation results of wheat wort.


2013 ◽  
Vol 14 (1) ◽  
pp. 67-74
Author(s):  
Bina Gautam ◽  
Tika B Karki ◽  
Om Prakash Panta

Amylase is an amylolytic enzyme used in food industry which is generally produced by Aspergillus spp. under solid state fermentation. The present study is concerned with the isolation, screening and selection of suitable strains of Aspergillus spp. and optimization of cultural conditions for the biosynthesis of amylase. Rice and wheat brans were used as substrates which are readily available inexpensive raw materials for amylase production. From 85 samples of rice and wheat grains, 55 colonies obtained on potato dextrose agar (PDA) were suspected to be Aspergillus oryzae and only 35 colonies possessed the morphological characteristics similar to that of A. oryzae indicating the isolates were most likely the strains of A. oryzae. Of all the fungal isolates of Aspergillus spps., Asp.31 gave maximum production of amylase (720.782 IUgds-1) in solid state fermentation media. This strain was selected as a parental strain for optimization for cultural conditions. The obtained data were analyzed using SPSS- 11.5 program. Of all the substrates (rice bran, wheat bran and their mixture), rice bran was the best for producing amylase of highest activity 611.614 IUgds-1.The highest enzyme activity of 698.749 IUgds-1 was observed at 50% initial moisture level of the substrate. The optimum temperature was 25°C for producing the crude amylase enzyme with amylase activity of 577.757 IUgds-1. Nepal Journal of Science and Technology Vol. 14, No. 1 (2013) 67-74 DOI: http://dx.doi.org/10.3126/njst.v14i1.8924


1990 ◽  
Vol 71 (1-2) ◽  
pp. 21-26 ◽  
Author(s):  
R. Koch ◽  
P. Zablowski ◽  
A. Spreinat ◽  
G. Antranikian

2020 ◽  
Vol 987 ◽  
pp. 118-123
Author(s):  
Nurul Syafiqa Izyan ◽  
Dg Nurdayana Azman ◽  
Nur Amalina Mohd Saad ◽  
Suhaila Mohd Sauid ◽  
Fazlena Hamzah

The study was done to determine the effect of Tacca starch loading on production of amylolytic enzyme from Ragi Tapai. In this study, Ragi Tapai was used as a starter to produce amylolytic enzyme. The fermentation was done in a solid state fermentation with the presence of Tacca leontopetaloides starch as the carbon source. The analysis of total sugar was conducted using DNS method and amylolytic enzyme was determined using Lowry method. The mixture was fermented and incubated for 24, 48, 72 and 96h. The result revealed that the optimum production of amylase was found at 48 h of incubation with amylase activity of 1.91 U/ml/min and 1.42 mg/ml for total protein. The study shows that increment amount of the Tacca starch in cultivation medium, increase the production of the amylase and total protein content. The highest enzyme activity was obtained at 4% of Tacca starch loading with amylase activity and total protein content of 2.14 U/ml/min and 1.42 mg/ml respectively. The study indicated that growth promoters in Tacca starch capable to enhance the activity of microbial consortium in Ragi Tapai for production of the amylolytic enzyme.


Biologia ◽  
2014 ◽  
Vol 69 (4) ◽  
Author(s):  
Fatma Matpan Bekler ◽  
Kemal Güven

AbstractA novel amylolytic enzyme producing thermophilic bacterial strain KP1 from the Diyadin hot spring water in Ağri, Turkey, was isolated in the present study. Phylogenetic analysis based on the partial 16S rRNA gene, biochemical and physiological tests revealed that the strain KP1 belongs to the genus Anoxybacillus. The pH and temperature optima for the α-amylase production by Anoxybacillus sp. KP1 were 8.0 and 50°C, respectively, where the maximum growth was obtained at the 28th hour of incubation and the highest α-amylase activity was obtained at the 40th hour of incubation (8979.6 U/mL). The optimum pH and temperature for the enzyme activity were 8.0 and 60°C, respectively. The maximum α-amylase production was secreted in the presence of 2% (w/v) soluble starch (10837.7 U/mL). Among the various organic and inorganic nitrogen sources tested, while keeping the beef extract concentration constant, casamino acid (14310.6 U/mL), urea (14126 U/mL), and tryptone (13217.2 U/mL) at a concentration of 2% gave the maximum α-amylase production. The enzyme activity was enhanced in the presence of 1.5 mM Mn2+ (123%), whereas it was strongly inhibited 1.5 mM by Hg2+. Inhibition by 89% was obtained also with sodium dodecyl sulphate (1%). The enzyme was found to be relatively stable at a range of pH and temperature.


1967 ◽  
Vol 105 (2) ◽  
pp. 577-583 ◽  
Author(s):  
N. J. King

1. The major amylolytic enzyme in culture filtrates of Coniophora cerebella grown in starch-containing media has been purified and characterized as a glucoamylase (EC 3.2.1.3). 2. The activity/unit wt. of protein was increased 11-fold and the enzyme showed one major component on polyacrylamide-gel electrophoresis. 3. The glucoamylase had optimum pH4·0–4·5. 4. Hg2+ completely inhibited the enzyme, but other ions tested had little effect on the activity at the concentration of ions used (5mm). 5. The action of the enzyme on amylopectin, amylose and maltose was studied. Hydrolysis proceeded by the stepwise removal of glucose units from the non-reducing ends of the polymer chains, and the enzyme was able to bypass or to hydrolyse the α-(1→6)-glucosidic linkages at branch points in the amylopectin molecule. Glucose was the only product found in digests of these substrates. 6. At the same substrate concentration (0·1%, w/v) and enzyme concentration, the initial rates of glucose production from amylopectin, amylose and maltose were in the proportions 40:10:1. 7. Km values at 40° and pH4·0 were calculated for the enzyme acting on amylopectin, amylose and maltose.


2014 ◽  
Vol 99 (4) ◽  
pp. 1805-1815 ◽  
Author(s):  
Kuta Suzuki ◽  
Mizuki Tanaka ◽  
Yui Konno ◽  
Takanori Ichikawa ◽  
Sakurako Ichinose ◽  
...  

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