References
- Kitahata S, Chiba S, Brewer CF, Hehre EJ. Mechanism of maltal hydration catalyzed by beta-amylase: role of protein structure in controlling the steric outcome of reactions catalyzed by a glycosylase. Biochemistry 30: 6769-6775 (1991) https://doi.org/10.1021/bi00241a020
- Ruzanski C, Smirnova J, Rejzek M, Cockburn D, Pedersen HL, Pike M, Willats WGT, Svensson B, Steup M, Ebenhoh O, Smith AM, Field RA. A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night. J. Biol. Chem. 288: 28581-28598 (2013) https://doi.org/10.1074/jbc.M113.497867
-
Takaha T, Yanase M, Okada S, Smith SM. Disproportionating enzyme (4-
${\alpha}$ -Glucanotransferase; EC 2.4.1.25) of potato: purification, molecular cloning, and potential role in starch metabolism. J. Biol. Chem. 268: 1391-1396 (1993) - Cenci U, Nitschle F, Steup M, Minassian BA, Colleoni C, Ball SG. Transition from glycogen to starch metabolism in archaeplastida. Trends Plant Sci. 19: 18-28 (2014)
-
Daba T, Kojima K, Inouye K. Characterization and solvent engineering of wheat
${\beta}$ -amylase for enhancing its activity and stability. Enzyme Microb. Technol. 51: 245-251 (2012) https://doi.org/10.1016/j.enzmictec.2012.07.004 -
Nguyen DH, Tran PL, Ha HS, Lee JS, Hong WS, Le QT, Oh BC, Park SH. Presence of
${\beta}$ -amylase in ramie leaf and its antistaling effect on rice cake. Food Sci. Biotechnol. 24: 37-40 (2015) https://doi.org/10.1007/s10068-015-0006-2 - Teotia S, Khare SK, Gupta MN. An efcient purication process for sweet potato beta-amylase by afnity precipitation with alginate. Enzyme Microb. Technol. 28: 792-795 (2001) https://doi.org/10.1016/S0141-0229(01)00338-6
- Lundgard R, Svensson B. The four major forms of barley amylase. Purification, characterization and structural relationship. Carlsberg Res. Commun. 52: 313-326 (1987) https://doi.org/10.1007/BF02907173
- Sagu ST, Nso EJ, Homann T, Kapseu C, Rawel HM. Extraction and purification of beta-amylase from stems of Abrus precatorius by three phase partitioning. Food Chem. 183: 144-153 (2015) https://doi.org/10.1016/j.foodchem.2015.03.028
-
Vikso-Nielsen A, Christensen TMIE, Bojko M, Marcussen J. Purification and characterization of
${\beta}$ -amylase from leaves of potato (Solanum tuberosum). Physiol. Planta. 99: 190-196 (1997) https://doi.org/10.1111/j.1399-3054.1997.tb03448.x - Mehrnoush A, Mustafa S, Yazid AMM. Heat treatment aqueous two phase system for purification of serine protease from Kesinal (Streblus asper) leaves. Molecules 16: 10202-10213 (2011) https://doi.org/10.3390/molecules161210202
- Olichon A, Schweizer D, Muyldermans S, Marco AD. Heating as a rapid purification method for recovering correctly-folded thermotolerant VH and VHH domains. BMC Biotechnol. 7 (2007)
- Kraus JK, Hebeda RE. Method for retarding staling of baked goods. U.S. Patent 5,209,938 (1993)
- Deylami MZ, Rahman RA, C. Tan CP, Bakar J, Olusegun L. Effect of blanching on enzyme activity, color changes, anthocyanin stability and extractability of mangosteen pericarp: A kinetic study. J. Food Eng. 178: 12-19 (2016) https://doi.org/10.1016/j.jfoodeng.2016.01.001
- Goncalves EM, Pinheiro J, Abreu M, Brandao TRS, Silva CLM. Carrot (Daucus carota L.) peroxidase inactivation, phenolic content and physical changes kinetics due to blanching. J. Food Eng. 97: 574-581 (2010) https://doi.org/10.1016/j.jfoodeng.2009.12.005
- Park KH, Kim YM, Lee CW. Thermal inactivation kinetics of potato tuber lipoxygenase. J. Agr. Food Chem. 36: 1012-1015 (1988) https://doi.org/10.1021/jf00083a027
- Chang BS, Park KH, Lund DB. Thermal inactivation kinetics of horseradish peroxidase. J. Food Sci. 53: 920-923 (1988) https://doi.org/10.1111/j.1365-2621.1988.tb08986.x
- Gusakov AV, Kondratyeva EG, Sinitsyn AP. Comparison of two methods for assaying reducing sugars in the determination of carbohydrase activities. Int. J. Anal. Chem. 2011: 283658 (2011)
- Park KH, Kim MJ, Lee HS, Han, NS, Kim D, Robyt JF. Transglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors. Carbohydr. Res. 313: 235-246 (1998) https://doi.org/10.1016/S0008-6215(98)00276-6
-
Tran PL, Lee JS, Park KH. Experimental evidence for a 9-binding subsite of Bacillus licheniformis
${\alpha}$ -amyalse. FEBS Lett. 588: 620-624 (2014) https://doi.org/10.1016/j.febslet.2013.12.032 - Cha HJ, Yoon HG, Kim YW, Lee HS, Kim JW, Kwon K, Cha SS, Cho MJ, Oh BH, Park KH. Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose. Eur. J. Biochem. 253: 251-262 (1998) https://doi.org/10.1046/j.1432-1327.1998.2530251.x
- Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 72: 248-254 (1976) https://doi.org/10.1016/0003-2697(76)90527-3
- Kohno A, Nanmori T, Shinke R. Purification of beta-amylase from alfalfa (Medicago sativa L.) seeds. J. Biochem. 105: 231-233 (1989) https://doi.org/10.1093/oxfordjournals.jbchem.a122644
- Cudney R, McPherson A. Preliminary crystallographic analysis of sweet potato beta amylase. J. Mol. Biol. 229: 253-254 (1993) https://doi.org/10.1006/jmbi.1993.1026
- Yamasaki Y. Beta-amylase in germinating millet seeds. Phytochemistry 64: 935-939 (2003) https://doi.org/10.1016/S0031-9422(03)00430-8
-
Lin TP, Preiss J. Characterization of D-enzyme (4-
${\alpha}$ -glucanotransferase) in arabidopsis leaf. Plant Physiol. 86: 260-265 (1988) https://doi.org/10.1104/pp.86.1.260 - Yao Y1, Zhang J, Ding X. Partial beta-amylolysis retards starch retrogradation in rice products. J. Agr. Food Chem. 51: 4066-4071 (2003) https://doi.org/10.1021/jf0209488
- Nondal A, Datta AK. Bread baking-A review. J. Food Eng. 86: 465-474 (2008) https://doi.org/10.1016/j.jfoodeng.2007.11.014
- Spendler T, Nilsson L, Fuglsang C. Preparation of dough and baked products. U.S. Patent 0055635 A1 (2001)
-
Chou YL, Ko CY, Chen LFO, Yen CC, Shaw JF. Purification and immobilization of the recombinant Brassica oleracea chlorophyllase 1 (BoCLH1) on
$DIAION^{(R)}$ CR11 as potential biocatalyst for the production of chlorophyllide and phytol. Molecules 20: 3744-3757 (2015) https://doi.org/10.3390/molecules20033744