in New York .
Written in English
|Other titles||Malt amylase.|
|Statement||by Winifred J. Wood ...|
|LC Classifications||QP601 .W75 1927|
|The Physical Object|
|Pagination||27,  p., 1 l.|
|Number of Pages||27|
|LC Control Number||27007739|
Structural and enzyme kinetic studies of retrograded starch: Inhibition of α-amylase and consequences for intestinal digestion of starch Hamung Patel, a Paul G. Royall, b Simon Gaisford, c Gareth R. Williams, c Cathrina H. Edwards, a, d Frederick J. Warren, d, e Bernadine M. Flanagan, e Peter R. Ellis, a and Peter J. Butterworth a, ⁎Cited by: Search term. Advanced Search Citation Search. Search. The temperature optimum of, for example, sorghum malt a-amylase is around 70 C and that of sorghum malt b-amylase is around 50 C (19, 20), with complete inactivation of b-amylase . Harrington. Zymographic analysis of the Harrington green malt extracts using commercial preparations of barley beta-amylase incorporated as a proteolytic substrate in 2-D SDS gels shows multiple proteolytic activities. A developmental study shows that the several green malt beta-amylase-degrading activities appear at around day 2 of germination.
Modelling studies showed that the quadratic fit inactivation model accurately represented the inactivation data for α-amylase from Bacillus sp. during hydrolysis of corn, rice and wheat starch. On the other hand, the data for α-amylase produced from Bacillus licheniformis were fitted to a single-step unimolecular non-first-order enzyme inactivation model during hydrolysis of corn, rice and wheat by: α-Amylase Activity. Amylase activity in malt is a critical quality parameter. The amylase activity in malt is often referred to as diastatic power and refers to the production of reducing substances by the action of α- and β-amylases on by: 5. β-amylase was first purified in the s (Schoch , and Haworth et al. ). Hopkins et al. first began to study the kinetics of β-amylase in In the s and s, techniques in the purification of sweet potato β-amylase improved (Nakayama and Amagase , Takeda and Hizukuri , and Hegde et al. ). The major amylase from malted jowar, a 47 kDa α-amylase, purified to homogeneity, is rich in β structure (∼60%) like other cereal amylases. Tm, the midpoint of thermal inactivation, is found to be ± °C. Thermal inactivation is found to follow first Cited by:
Two independent studies used the presence of the bp insertion to demonstrate it could be used to select for lines with higher thermostability of β-amylase, as it was not present in the Sd2L allele (Coventry et al., ; Gunkel et al., ). This study shows an approximate 8‐fold increase in α‐amylase activity by producing sorghum malt from grains steeped in 10 m m phosphate buffer pH at 20°C, compared with water, which has traditionally been employed. The appearance of the resulting malt was comparable to the control (water‐steeped malt) even after the kilning by: 4. The study of a large number of chemical reactions reveals that most do not go to true completion. This is likewise true of enzymatically-catalyzed reactions. This is due to the reversibility of most reactions. In general: where K+1 is the forward reaction rate constant and K File Size: KB. In fact, it is swallowed with chewed food and subsequently inactivated by extremely low gastric pH; amylase in fact has an optimal pH around 7, and the pH of saliva is generally between and α‐Amylase is produced by salivary glands and mainly from exocrine by: 4.