Heat stable α amylase

Manufactured by Merck Group

Sourced in United States

Heat stable α-amylase is an enzyme that catalyzes the hydrolysis of alpha-1,4-glycosidic linkages in starch and other polysaccharides. It is resistant to high temperatures, making it suitable for use in various industrial processes that require heat-stable enzymes.

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Lab products found in correlation

Amyloglucosidase, by Merck Group (3 mentions) Trumac cn, by Leco (1 mentions) Tga 701, by Leco (1 mentions) L 8900, by Hitachi (1 mentions) Neutral protease, by Merck Group (1 mentions)

6 protocols using heat stable α amylase

Nutritional Analysis and Digestibility Evaluation of Animal Feeds

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Representative samples of feeds offered, left-over residues and faeces were dried (65°C for 48 h) in hot-air oven (Labco, Delhi, India) till constant weight and ground (Wiley mill) to pass through 1 mm sieve and kept in air-tight zip lock polythene bags awaiting further analyses. Standard methods of AOAC [13 ] were followed for determining DM (ID: 934.01), crude protein (CP; N×6.25; ID: 984.13), ether extract (EE; ID: 920.39), and total ash (ID: 942.05). Fibre fractions like neutral detergent fibre (NDF) and acid detergent fibre (ADF) were assayed [14 (link)] and heat stable α-amylase (Sigma Aldrich, St. Louis, MO, USA) was used in the former for concentrate ingredients only. Acid detergent lignin was recovered from ADF by solubilising cellulose with 72% (w/w) sulphuric acid [14 (link)]. All analyses were done, at least, in triplicate.
Apparent coefficient of digestibility was computed on the basis of intake and faecal excretion of particular nutrient. Energy value of the diets was expressed in terms of metabolisable energy (ME), calculated with the relationship of 1 kg total digestible nutrients = 15 MJ of ME [15 ,16 (link)].

Malik T.A., Thakur S.S., Mahesh M.S, & Yogi R.K. (2017). Replacing groundnut cake with gluten meals of rice and maize in diets for growing Sahiwal cattle. Asian-Australasian Journal of Animal Sciences, 30(10), 1410-1415.

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Comprehensive Nutrient Analysis of Animal Feed

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Feed components and excreta were analysed according to the official methods of analysis (AOAC International, 1995 ). All analyses were performed in duplicate (fresh faeces in triplicate). Dry matter and total ash were determined using a thermogravimetric device (TGA‐701, Leco; AOAC Official Method 942.5), organic matter (OM) was calculated as the difference between them. A C/N analyser (TruMac CN, Leco) was used to determine N amounts in feed components, fresh faeces and acidified urine (AOAC Official Method 968.06), CP was calculated as N × 6.25. A Soxhlet extractor (Extraction System B‐811) was used to determine ether extract (AOAC Official Method 963.15). Ash‐corrected detergent fibre fractions were assessed with a Fibertherm FT 12 (Gerhardt). Heat‐stable α‐amylase (Sigma‐Aldrich) was used for neutral detergent fibre (NDF) analysis (method 6.5.1 of VDLUFA, 2012 ). Acid detergent lignin (ADL, method 6.5.3 of VDLUFA, 2012 ) was determined sequentially after acid detergent fibre (ADF, method 6.5.2 of VDLUFA, 2012 ) analysis by incubation in sulphuric acid (720 ml/L) for 3 h. Gross energy (GE) was assessed in faeces and feed components with a bomb calorimeter (C7000, IKA‐Werke).

Birkinshaw A., Sutter M., Reidy B., Kreuzer M, & Terranova M. (2022). Effects of incremental increases in grass silage proportions from different harvest years on methane emissions, urinary nitrogen losses, and protein and energy utilisation in dairy cows. Journal of Animal Physiology and Animal Nutrition, 107(1), 37-52.

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Starch Digestion Assay with HWHF

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The effects of HWHF on starch digestion were measured as described in detail elsewhere based on sequential incubations of starch with heat stable α-amylase and amyloglucosidase (Sigma-Aldrich, St. Louis, USA) [20 (link)]. Starch (100 mg) was suspended in water in the presence/absence of HWHF. A heat stable α-amylase (0·01%) (Sigma-Aldich) was added to the mixture and incubated for 20 min at 80 °C. After incubation, the reaction was further treated with 0·1% of Rhizopus mold amyloglucosidase (Sigma-Aldich) for 30 min at 60 °C. Samples were aliquoted and stored for subsequent analysis of glucose using the GOD/PAP method (Randox GL 2623). Acarbose was used as a positive control.

Ansari P., Flatt P.R., Harriott P, & Abdel-Wahab Y.H. (2022). Insulin secretory and antidiabetic actions of Heritiera fomes bark together with isolation of active phytomolecules. PLoS ONE, 17(3), e0264632.

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Starch Digestion Evaluation with EEAS

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Chronological incubations with heat-stable α-amylase and amyloglucosidase (Sigma-Aldrich, St. Louis, MO, USA) were performed to evaluate the effects of EEAS on starch digestion, as outlined before [14 (link)]. A mixture of 100 mg/50 mL starch solution plus/minus EEAS was incubated for 20 min at 80 °C with heat-stable α-amylase (0.01%). Additional incubation for 30 min at 60 °C with 0.1% amyloglucosidase (from Rhizopus sp.) was performed. The GOD/PAP (Randox GL 2623) method was used to analyse glucose from aliquots of samples that were afterwards stored at 4 °C. Acarbose was used as a positive control for this assay.

Ansari P., Hannan J.M., Seidel V, & Abdel-Wahab Y.H. (2022). Polyphenol-Rich Leaf of Annona squamosa Stimulates Insulin Release from BRIN-BD11 Cells and Isolated Mouse Islets, Reduces (CH2O)n Digestion and Absorption, and Improves Glucose Tolerance and GLP-1 (7-36) Levels in High-Fat-Fed Rats. Metabolites, 12(10), 995.

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Comprehensive Feed Composition Analysis

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The moisture, CP, ether extract (EE), starch and crude ash contents in the test samples (Table 1) were determined according to AOAC official methods as described by procedures 934.01, 976.05, 920.39, 996.11, and 927.02 (AOAC, 2012 ). Neutral detergent fibre, ADF, and lignin contents were determined by the method of Van Soest et al. (1991) (link) without sodium sulfite. Heat stable α-amylase (A3306, Sigma Chemical Co., St. Louis, MO, USA) was included in the NDF assay (10 μL per 0.50 g of sample). Amino acid content of the feeds, rumen undegraded residues and pepsin/pancreatin digestion residues were determined by AA auto-analyzer (Hitachi L8900, Hitachi, Japan) by the method of AOAC (2012) . Both acid hydrolysis (to determine all AA except methoinine, cystine and tryptophan) and acid hydrolysis with performic oxidation (to determine methionine and cystine) were carried out. Tryptophan was determined separately by colorimetric method after sodium hydroxide hydrolysis. The contents of non-protein nitrogen, soluble crude protein (SP), neutral detergent insoluble crude protein (NDICP), and acid detergent insoluble crude protein (ADICP) were measured by the method of Licitra et al. (1996) . Nonfiber carbohydrate (NFC) was calculated as 100 −(CP+[NDF − NDICP]+EE+ash).

Gao W., Chen A., Zhang B., Kong P., Liu C, & Zhao J. (2015). Rumen Degradability and Post-ruminal Digestion of Dry Matter, Nitrogen and Amino Acids of Three Protein Supplements. Asian-Australasian Journal of Animal Sciences, 28(4), 485-493.

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Millet Bran Processing Protocol

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Millet bran were purchased from Tuogu Millet Factory (Daqing, China), Neutral protease, heat-stable α- amylase, amyloglucosidase were purchased from Sigma Corporation (Beijing, China), 95% ethanol (AR Grade) were purchased from tianjin Yongsheng Fine Chemical Co (Tianjing, China), Soybean oil were purchased from Changchun Jiayu Grain and Oil Co (Changchun China).

Wei C., Ge Y., Liu D., Zhao S., Wei M., Jiliu J., Hu X., Quan Z., Wu Y., Su Y., Wang Y, & Cao L. (2022). Effects of High-Temperature, High-Pressure, and Ultrasonic Treatment on the Physicochemical Properties and Structure of Soluble Dietary Fibers of Millet Bran. Frontiers in Nutrition, 8, 820715.

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